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*** 6GHV_monomero ***elNémo ID: 2403131446023063835Job options:ID = 2403131446023063835 JOBID = 6GHV_monomero USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:
HEADER 6GHV_monomero
HEADER SUGAR BINDING PROTEIN 09-MAY-18 6GHV
TITLE STRUCTURE OF A DC-SIGN CRD IN COMPLEX WITH HIGH AFFINITY GLYCOMIMETIC.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CD209 ANTIGEN;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: C-TYPE LECTIN DOMAIN FAMILY 4 MEMBER L,DENDRITIC CELL-
COMPND 5 SPECIFIC ICAM-3-GRABBING NON-INTEGRIN 1,DC-SIGN1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CD209, CLEC4L;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET30
KEYWDS DC-SIGN, INHIBITOR, SUGAR BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.THEPAUT,S.ACHILLI,L.MEDVE,A.BERNARDI,F.FIESCHI
REVDAT 3 17-JAN-24 6GHV 1 LINK
REVDAT 2 27-NOV-19 6GHV 1 JRNL
REVDAT 1 11-SEP-19 6GHV 0
JRNL AUTH L.MEDVE,S.ACHILLI,J.GUZMAN-CALDENTEY,M.THEPAUT,L.SENALDI,
JRNL AUTH 2 A.LE ROY,S.SATTIN,C.EBEL,C.VIVES,S.MARTIN-SANTAMARIA,
JRNL AUTH 3 A.BERNARDI,F.FIESCHI
JRNL TITL ENHANCING POTENCY AND SELECTIVITY OF A DC-SIGN GLYCOMIMETIC
JRNL TITL 2 LIGAND BY FRAGMENT-BASED DESIGN: STRUCTURAL BASIS.
JRNL REF CHEMISTRY V. 25 14659 2019
JRNL REFN ISSN 0947-6539
JRNL PMID 31469191
JRNL DOI 10.1002/CHEM.201903391
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0218
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 62185
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3261
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4508
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE SET COUNT : 235
REMARK 3 BIN FREE R VALUE : 0.3320
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6444
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 344
REMARK 3 SOLVENT ATOMS : 660
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.77
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.48000
REMARK 3 B22 (A**2) : -2.31000
REMARK 3 B33 (A**2) : 0.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.55000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.184
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.175
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.145
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.856
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7139 ; 0.017 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 5793 ; 0.008 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9737 ; 1.625 ; 1.932
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13637 ; 1.113 ; 3.019
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 829 ; 6.758 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 386 ;36.877 ;25.466
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1072 ;13.447 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;21.049 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 938 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7977 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1579 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3214 ; 2.538 ; 3.251
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3213 ; 2.534 ; 3.249
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4017 ; 3.727 ; 4.847
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4018 ; 3.727 ; 4.849
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3925 ; 2.901 ; 3.477
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3926 ; 2.901 ; 3.476
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5701 ; 4.379 ; 5.104
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8791 ; 6.114 ;37.375
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 8707 ; 6.059 ;37.159
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6GHV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1200009734.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-FEB-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : MASSIF-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.966
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 20180126
REMARK 200 DATA SCALING SOFTWARE : XSCALE 20180126
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65455
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 3.087
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.4700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.81
REMARK 200 R MERGE FOR SHELL (I) : 0.54500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.010
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.6.02
REMARK 200 STARTING MODEL: 1K9I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 200MM MG(NO3)2, 100MM
REMARK 280 MES PH6. PROTEIN SAMPLE: 150MM NACL, 4MM CACL2, 25MM TRIS PH8, 2%
REMARK 280 DMSO, 3.25 MM LIGAND AND 5.54MG/ML PROTEIN., VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 28.75350
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLU A 250
REMARK 465 ARG A 251
REMARK 465 LEU A 252
REMARK 465 SER A 385
REMARK 465 ARG A 386
REMARK 465 ASP A 387
REMARK 465 GLU A 388
REMARK 465 GLU A 389
REMARK 465 GLN A 390
REMARK 465 PHE A 391
REMARK 465 LEU A 392
REMARK 465 SER A 393
REMARK 465 PRO A 394
REMARK 465 ALA A 395
REMARK 465 PRO A 396
REMARK 465 ALA A 397
REMARK 465 THR A 398
REMARK 465 PRO A 399
REMARK 465 ASN A 400
REMARK 465 PRO A 401
REMARK 465 PRO A 402
REMARK 465 PRO A 403
REMARK 465 ALA A 404
REMARK 465 GLU B 250
REMARK 465 ARG B 251
REMARK 465 LEU B 252
REMARK 465 SER B 385
REMARK 465 ARG B 386
REMARK 465 ASP B 387
REMARK 465 GLU B 388
REMARK 465 GLU B 389
REMARK 465 GLN B 390
REMARK 465 PHE B 391
REMARK 465 LEU B 392
REMARK 465 SER B 393
REMARK 465 PRO B 394
REMARK 465 ALA B 395
REMARK 465 PRO B 396
REMARK 465 ALA B 397
REMARK 465 THR B 398
REMARK 465 PRO B 399
REMARK 465 ASN B 400
REMARK 465 PRO B 401
REMARK 465 PRO B 402
REMARK 465 PRO B 403
REMARK 465 ALA B 404
REMARK 465 GLU C 250
REMARK 465 ARG C 251
REMARK 465 SER C 385
REMARK 465 ARG C 386
REMARK 465 ASP C 387
REMARK 465 GLU C 388
REMARK 465 GLU C 389
REMARK 465 GLN C 390
REMARK 465 PHE C 391
REMARK 465 LEU C 392
REMARK 465 SER C 393
REMARK 465 PRO C 394
REMARK 465 ALA C 395
REMARK 465 PRO C 396
REMARK 465 ALA C 397
REMARK 465 THR C 398
REMARK 465 PRO C 399
REMARK 465 ASN C 400
REMARK 465 PRO C 401
REMARK 465 PRO C 402
REMARK 465 PRO C 403
REMARK 465 ALA C 404
REMARK 465 GLU D 250
REMARK 465 ARG D 251
REMARK 465 SER D 385
REMARK 465 ARG D 386
REMARK 465 ASP D 387
REMARK 465 GLU D 388
REMARK 465 GLU D 389
REMARK 465 GLN D 390
REMARK 465 PHE D 391
REMARK 465 LEU D 392
REMARK 465 SER D 393
REMARK 465 PRO D 394
REMARK 465 ALA D 395
REMARK 465 PRO D 396
REMARK 465 ALA D 397
REMARK 465 THR D 398
REMARK 465 PRO D 399
REMARK 465 ASN D 400
REMARK 465 PRO D 401
REMARK 465 PRO D 402
REMARK 465 PRO D 403
REMARK 465 ALA D 404
REMARK 465 GLU E 250
REMARK 465 ARG E 251
REMARK 465 SER E 385
REMARK 465 ARG E 386
REMARK 465 ASP E 387
REMARK 465 GLU E 388
REMARK 465 GLU E 389
REMARK 465 GLN E 390
REMARK 465 PHE E 391
REMARK 465 LEU E 392
REMARK 465 SER E 393
REMARK 465 PRO E 394
REMARK 465 ALA E 395
REMARK 465 PRO E 396
REMARK 465 ALA E 397
REMARK 465 THR E 398
REMARK 465 PRO E 399
REMARK 465 ASN E 400
REMARK 465 PRO E 401
REMARK 465 PRO E 402
REMARK 465 PRO E 403
REMARK 465 ALA E 404
REMARK 465 GLU F 250
REMARK 465 ARG F 251
REMARK 465 LEU F 252
REMARK 465 SER F 385
REMARK 465 ARG F 386
REMARK 465 ASP F 387
REMARK 465 GLU F 388
REMARK 465 GLU F 389
REMARK 465 GLN F 390
REMARK 465 PHE F 391
REMARK 465 LEU F 392
REMARK 465 SER F 393
REMARK 465 PRO F 394
REMARK 465 ALA F 395
REMARK 465 PRO F 396
REMARK 465 ALA F 397
REMARK 465 THR F 398
REMARK 465 PRO F 399
REMARK 465 ASN F 400
REMARK 465 PRO F 401
REMARK 465 PRO F 402
REMARK 465 PRO F 403
REMARK 465 ALA F 404
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 259 -9.19 88.08
REMARK 500 GLU A 353 95.07 63.86
REMARK 500 GLU B 259 -10.31 87.58
REMARK 500 GLN B 264 52.45 38.98
REMARK 500 GLU B 353 97.74 76.19
REMARK 500 GLU C 259 -14.16 82.94
REMARK 500 GLU C 353 92.18 70.67
REMARK 500 GLU D 259 -12.06 89.61
REMARK 500 ASN D 311 47.70 34.04
REMARK 500 GLU D 353 95.22 75.04
REMARK 500 GLU E 259 -9.01 84.19
REMARK 500 GLN E 264 53.29 32.95
REMARK 500 GLU E 353 101.18 63.51
REMARK 500 GLU F 259 -15.11 90.44
REMARK 500 GLU F 353 105.04 79.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1195 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH B1225 DISTANCE = 7.06 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 320 OD1
REMARK 620 2 ASP A 320 OD2 51.3
REMARK 620 3 GLU A 324 OE1 90.9 82.8
REMARK 620 4 GLU A 324 OE2 116.4 71.6 53.0
REMARK 620 5 ASN A 350 OD1 158.3 147.8 84.3 77.1
REMARK 620 6 GLU A 354 O 95.6 122.9 150.9 142.6 79.2
REMARK 620 7 ASP A 355 OD1 72.6 119.0 75.4 126.5 85.8 79.6
REMARK 620 8 HOH A1129 O 111.2 79.1 131.1 78.2 87.4 72.2 151.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 347 OE1
REMARK 620 2 ASN A 349 OD1 71.4
REMARK 620 3 GLU A 354 OE1 139.3 68.6
REMARK 620 4 ASN A 365 OD1 70.6 141.1 150.1
REMARK 620 5 ASP A 366 O 138.2 136.7 73.5 79.8
REMARK 620 6 ASP A 366 OD1 76.4 84.8 92.8 94.1 77.0
REMARK 620 7 EZ8 A1001 O4 72.9 75.8 103.6 85.5 134.3 147.6
REMARK 620 8 EZ8 A1001 O3 129.5 118.7 78.0 80.8 71.0 148.0 63.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1004 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 355 OD2
REMARK 620 2 HOH A1102 O 84.1
REMARK 620 3 HOH A1118 O 76.9 85.0
REMARK 620 4 HOH A1139 O 89.1 166.2 81.7
REMARK 620 5 HOH D 607 O 95.1 96.7 171.6 95.9
REMARK 620 6 HOH D 695 O 167.8 88.1 93.2 96.4 95.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 320 OD1
REMARK 620 2 ASP B 320 OD2 53.7
REMARK 620 3 GLU B 324 OE1 99.5 79.7
REMARK 620 4 GLU B 324 OE2 121.2 70.7 49.0
REMARK 620 5 ASN B 350 OD1 159.5 142.2 76.6 71.5
REMARK 620 6 GLU B 354 O 93.8 134.5 142.6 143.0 78.8
REMARK 620 7 ASP B 355 OD1 75.9 116.7 73.0 120.3 83.8 76.7
REMARK 620 8 HOH B1133 O 106.1 80.6 128.4 79.5 91.5 79.7 156.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 347 OE1
REMARK 620 2 ASN B 349 OD1 68.1
REMARK 620 3 GLU B 354 OE1 141.7 75.6
REMARK 620 4 ASN B 365 OD1 72.5 140.1 144.2
REMARK 620 5 ASP B 366 O 130.5 140.5 73.8 72.9
REMARK 620 6 ASP B 366 OD1 71.3 82.9 93.1 90.3 74.6
REMARK 620 7 EZ8 B1001 O4 74.1 76.6 109.3 87.3 137.4 144.3
REMARK 620 8 EZ8 B1001 O3 133.2 123.9 77.8 80.2 72.4 147.1 67.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1004 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 355 OD2
REMARK 620 2 HOH B1108 O 92.4
REMARK 620 3 HOH B1126 O 86.9 83.0
REMARK 620 4 HOH B1148 O 90.6 93.7 175.8
REMARK 620 5 HOH B1155 O 85.0 174.6 92.1 91.1
REMARK 620 6 HOH B1212 O 165.6 99.4 86.4 96.7 82.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C1003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 320 OD1
REMARK 620 2 ASP C 320 OD2 51.7
REMARK 620 3 GLU C 324 OE1 93.0 80.5
REMARK 620 4 GLU C 324 OE2 116.4 71.1 48.2
REMARK 620 5 ASN C 350 OD1 156.9 149.8 86.1 79.8
REMARK 620 6 GLU C 354 O 91.0 123.2 151.3 148.7 79.2
REMARK 620 7 ASP C 355 OD1 72.3 118.9 80.1 126.5 84.8 74.2
REMARK 620 8 HOH C1121 O 108.5 81.7 133.4 85.3 88.3 71.1 145.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C1002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 347 OE1
REMARK 620 2 ASN C 349 OD1 72.6
REMARK 620 3 GLU C 354 OE1 140.4 68.8
REMARK 620 4 ASN C 365 OD1 68.3 140.6 150.6
REMARK 620 5 ASP C 366 O 136.5 129.4 68.7 84.5
REMARK 620 6 ASP C 366 OD1 73.8 81.6 92.0 92.0 73.8
REMARK 620 7 EZ8 C1001 O4 71.4 78.6 108.4 84.6 141.1 143.7
REMARK 620 8 EZ8 C1001 O3 131.9 120.8 77.6 83.8 74.1 148.0 67.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C1004 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 355 OD2
REMARK 620 2 HOH C1112 O 104.4
REMARK 620 3 HOH C1126 O 87.9 90.1
REMARK 620 4 HOH C1128 O 91.1 95.3 174.6
REMARK 620 5 HOH C1130 O 83.1 169.8 97.1 77.5
REMARK 620 6 HOH C1221 O 164.0 90.9 96.9 82.8 81.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 320 OD1
REMARK 620 2 ASP D 320 OD2 51.6
REMARK 620 3 GLU D 324 OE1 94.9 78.7
REMARK 620 4 GLU D 324 OE2 119.4 70.7 52.9
REMARK 620 5 ASN D 350 OD1 156.3 149.0 83.5 78.3
REMARK 620 6 GLU D 354 O 91.5 129.1 146.3 145.3 77.8
REMARK 620 7 ASP D 355 OD1 71.8 112.9 72.8 124.4 85.3 78.0
REMARK 620 8 HOH D 623 O 106.2 84.8 135.9 83.1 90.7 72.5 150.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 347 OE1
REMARK 620 2 ASN D 349 OD1 74.3
REMARK 620 3 GLU D 354 OE1 150.7 76.4
REMARK 620 4 ASN D 365 OD1 65.8 140.1 143.5
REMARK 620 5 ASP D 366 O 131.6 140.2 73.0 74.1
REMARK 620 6 ASP D 366 OD1 74.7 84.2 100.8 86.8 77.2
REMARK 620 7 EZ8 D 502 O4 66.0 78.5 109.6 84.0 136.0 140.0
REMARK 620 8 EZ8 D 502 O3 123.6 126.6 76.4 77.6 69.4 145.8 68.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 505 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 355 OD2
REMARK 620 2 HOH D 610 O 84.7
REMARK 620 3 HOH D 617 O 88.7 94.1
REMARK 620 4 HOH D 622 O 73.5 83.6 162.2
REMARK 620 5 HOH D 649 O 83.7 168.3 86.6 92.2
REMARK 620 6 HOH D 697 O 161.8 92.0 109.3 88.4 98.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 505 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 320 OD1
REMARK 620 2 ASP E 320 OD2 50.4
REMARK 620 3 GLU E 324 OE1 92.9 82.9
REMARK 620 4 GLU E 324 OE2 111.5 66.5 52.2
REMARK 620 5 ASN E 350 OD1 164.0 143.2 82.8 78.0
REMARK 620 6 GLU E 354 O 94.8 121.5 153.0 144.5 82.6
REMARK 620 7 ASP E 355 OD1 71.9 116.6 75.4 127.4 92.1 82.5
REMARK 620 8 HOH E 638 O 106.8 72.5 124.3 72.0 88.2 77.9 160.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 347 OE1
REMARK 620 2 ASN E 349 OD1 70.9
REMARK 620 3 GLU E 354 OE1 137.9 67.9
REMARK 620 4 ASN E 365 OD1 74.7 145.5 145.6
REMARK 620 5 ASP E 366 O 138.5 132.8 71.3 75.2
REMARK 620 6 ASP E 366 OD1 77.3 81.8 88.9 89.5 74.6
REMARK 620 7 EZ8 E 503 O4 71.2 83.1 111.1 87.2 134.4 148.0
REMARK 620 8 EZ8 E 503 O3 132.6 119.7 77.3 85.2 71.5 146.0 65.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 506 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 355 OD1
REMARK 620 2 ASP E 355 OD2 47.8
REMARK 620 3 HOH E 608 O 71.0 98.0
REMARK 620 4 HOH E 613 O 113.8 72.1 153.9
REMARK 620 5 HOH E 622 O 106.2 76.2 75.3 78.8
REMARK 620 6 HOH E 629 O 62.3 95.4 98.5 106.4 168.5
REMARK 620 7 HOH E 707 O 152.3 158.2 88.7 92.9 85.7 104.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 505 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH E 614 O
REMARK 620 2 HOH E 616 O 77.5
REMARK 620 3 ASP F 355 OD2 88.1 83.1
REMARK 620 4 HOH F 604 O 158.7 82.6 82.2
REMARK 620 5 HOH F 605 O 96.1 172.9 93.6 103.3
REMARK 620 6 HOH F 693 O 96.5 80.5 161.5 87.4 103.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 320 OD1
REMARK 620 2 ASP F 320 OD2 49.9
REMARK 620 3 GLU F 324 OE1 94.3 76.5
REMARK 620 4 GLU F 324 OE2 114.4 66.8 51.3
REMARK 620 5 ASN F 350 OD1 161.4 141.0 78.1 74.2
REMARK 620 6 GLU F 354 O 98.5 133.4 147.6 142.1 80.4
REMARK 620 7 ASP F 355 OD1 76.5 115.7 74.9 124.9 85.1 79.3
REMARK 620 8 HOH F 618 O 109.0 84.4 128.4 77.1 88.7 74.7 154.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 347 OE1
REMARK 620 2 ASN F 349 OD1 74.6
REMARK 620 3 GLU F 354 OE1 148.1 75.6
REMARK 620 4 ASN F 365 OD1 69.6 144.2 138.8
REMARK 620 5 ASP F 366 O 129.5 136.9 69.4 70.4
REMARK 620 6 ASP F 366 OD1 74.6 81.3 89.8 88.0 74.5
REMARK 620 7 EZ8 F 502 O4 75.6 79.1 109.6 93.1 135.9 147.7
REMARK 620 8 EZ8 F 502 O3 134.0 123.5 73.5 84.2 69.2 143.3 68.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EZ8 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EZ8 B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EZ8 C 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EZ8 D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EZ8 E 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EZ8 F 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 506
DBREF 6GHV A 250 404 UNP Q9NNX6 CD209_HUMAN 250 404
DBREF 6GHV B 250 404 UNP Q9NNX6 CD209_HUMAN 250 404
DBREF 6GHV C 250 404 UNP Q9NNX6 CD209_HUMAN 250 404
DBREF 6GHV D 250 404 UNP Q9NNX6 CD209_HUMAN 250 404
DBREF 6GHV E 250 404 UNP Q9NNX6 CD209_HUMAN 250 404
DBREF 6GHV F 250 404 UNP Q9NNX6 CD209_HUMAN 250 404
SEQRES 1 A 155 GLU ARG LEU CYS HIS PRO CYS PRO TRP GLU TRP THR PHE
SEQRES 2 A 155 PHE GLN GLY ASN CYS TYR PHE MET SER ASN SER GLN ARG
SEQRES 3 A 155 ASN TRP HIS ASP SER ILE THR ALA CYS LYS GLU VAL GLY
SEQRES 4 A 155 ALA GLN LEU VAL VAL ILE LYS SER ALA GLU GLU GLN ASN
SEQRES 5 A 155 PHE LEU GLN LEU GLN SER SER ARG SER ASN ARG PHE THR
SEQRES 6 A 155 TRP MET GLY LEU SER ASP LEU ASN GLN GLU GLY THR TRP
SEQRES 7 A 155 GLN TRP VAL ASP GLY SER PRO LEU LEU PRO SER PHE LYS
SEQRES 8 A 155 GLN TYR TRP ASN ARG GLY GLU PRO ASN ASN VAL GLY GLU
SEQRES 9 A 155 GLU ASP CYS ALA GLU PHE SER GLY ASN GLY TRP ASN ASP
SEQRES 10 A 155 ASP LYS CYS ASN LEU ALA LYS PHE TRP ILE CYS LYS LYS
SEQRES 11 A 155 SER ALA ALA SER CYS SER ARG ASP GLU GLU GLN PHE LEU
SEQRES 12 A 155 SER PRO ALA PRO ALA THR PRO ASN PRO PRO PRO ALA
SEQRES 1 B 155 GLU ARG LEU CYS HIS PRO CYS PRO TRP GLU TRP THR PHE
SEQRES 2 B 155 PHE GLN GLY ASN CYS TYR PHE MET SER ASN SER GLN ARG
SEQRES 3 B 155 ASN TRP HIS ASP SER ILE THR ALA CYS LYS GLU VAL GLY
SEQRES 4 B 155 ALA GLN LEU VAL VAL ILE LYS SER ALA GLU GLU GLN ASN
SEQRES 5 B 155 PHE LEU GLN LEU GLN SER SER ARG SER ASN ARG PHE THR
SEQRES 6 B 155 TRP MET GLY LEU SER ASP LEU ASN GLN GLU GLY THR TRP
SEQRES 7 B 155 GLN TRP VAL ASP GLY SER PRO LEU LEU PRO SER PHE LYS
SEQRES 8 B 155 GLN TYR TRP ASN ARG GLY GLU PRO ASN ASN VAL GLY GLU
SEQRES 9 B 155 GLU ASP CYS ALA GLU PHE SER GLY ASN GLY TRP ASN ASP
SEQRES 10 B 155 ASP LYS CYS ASN LEU ALA LYS PHE TRP ILE CYS LYS LYS
SEQRES 11 B 155 SER ALA ALA SER CYS SER ARG ASP GLU GLU GLN PHE LEU
SEQRES 12 B 155 SER PRO ALA PRO ALA THR PRO ASN PRO PRO PRO ALA
SEQRES 1 C 155 GLU ARG LEU CYS HIS PRO CYS PRO TRP GLU TRP THR PHE
SEQRES 2 C 155 PHE GLN GLY ASN CYS TYR PHE MET SER ASN SER GLN ARG
SEQRES 3 C 155 ASN TRP HIS ASP SER ILE THR ALA CYS LYS GLU VAL GLY
SEQRES 4 C 155 ALA GLN LEU VAL VAL ILE LYS SER ALA GLU GLU GLN ASN
SEQRES 5 C 155 PHE LEU GLN LEU GLN SER SER ARG SER ASN ARG PHE THR
SEQRES 6 C 155 TRP MET GLY LEU SER ASP LEU ASN GLN GLU GLY THR TRP
SEQRES 7 C 155 GLN TRP VAL ASP GLY SER PRO LEU LEU PRO SER PHE LYS
SEQRES 8 C 155 GLN TYR TRP ASN ARG GLY GLU PRO ASN ASN VAL GLY GLU
SEQRES 9 C 155 GLU ASP CYS ALA GLU PHE SER GLY ASN GLY TRP ASN ASP
SEQRES 10 C 155 ASP LYS CYS ASN LEU ALA LYS PHE TRP ILE CYS LYS LYS
SEQRES 11 C 155 SER ALA ALA SER CYS SER ARG ASP GLU GLU GLN PHE LEU
SEQRES 12 C 155 SER PRO ALA PRO ALA THR PRO ASN PRO PRO PRO ALA
SEQRES 1 D 155 GLU ARG LEU CYS HIS PRO CYS PRO TRP GLU TRP THR PHE
SEQRES 2 D 155 PHE GLN GLY ASN CYS TYR PHE MET SER ASN SER GLN ARG
SEQRES 3 D 155 ASN TRP HIS ASP SER ILE THR ALA CYS LYS GLU VAL GLY
SEQRES 4 D 155 ALA GLN LEU VAL VAL ILE LYS SER ALA GLU GLU GLN ASN
SEQRES 5 D 155 PHE LEU GLN LEU GLN SER SER ARG SER ASN ARG PHE THR
SEQRES 6 D 155 TRP MET GLY LEU SER ASP LEU ASN GLN GLU GLY THR TRP
SEQRES 7 D 155 GLN TRP VAL ASP GLY SER PRO LEU LEU PRO SER PHE LYS
SEQRES 8 D 155 GLN TYR TRP ASN ARG GLY GLU PRO ASN ASN VAL GLY GLU
SEQRES 9 D 155 GLU ASP CYS ALA GLU PHE SER GLY ASN GLY TRP ASN ASP
SEQRES 10 D 155 ASP LYS CYS ASN LEU ALA LYS PHE TRP ILE CYS LYS LYS
SEQRES 11 D 155 SER ALA ALA SER CYS SER ARG ASP GLU GLU GLN PHE LEU
SEQRES 12 D 155 SER PRO ALA PRO ALA THR PRO ASN PRO PRO PRO ALA
SEQRES 1 E 155 GLU ARG LEU CYS HIS PRO CYS PRO TRP GLU TRP THR PHE
SEQRES 2 E 155 PHE GLN GLY ASN CYS TYR PHE MET SER ASN SER GLN ARG
SEQRES 3 E 155 ASN TRP HIS ASP SER ILE THR ALA CYS LYS GLU VAL GLY
SEQRES 4 E 155 ALA GLN LEU VAL VAL ILE LYS SER ALA GLU GLU GLN ASN
SEQRES 5 E 155 PHE LEU GLN LEU GLN SER SER ARG SER ASN ARG PHE THR
SEQRES 6 E 155 TRP MET GLY LEU SER ASP LEU ASN GLN GLU GLY THR TRP
SEQRES 7 E 155 GLN TRP VAL ASP GLY SER PRO LEU LEU PRO SER PHE LYS
SEQRES 8 E 155 GLN TYR TRP ASN ARG GLY GLU PRO ASN ASN VAL GLY GLU
SEQRES 9 E 155 GLU ASP CYS ALA GLU PHE SER GLY ASN GLY TRP ASN ASP
SEQRES 10 E 155 ASP LYS CYS ASN LEU ALA LYS PHE TRP ILE CYS LYS LYS
SEQRES 11 E 155 SER ALA ALA SER CYS SER ARG ASP GLU GLU GLN PHE LEU
SEQRES 12 E 155 SER PRO ALA PRO ALA THR PRO ASN PRO PRO PRO ALA
SEQRES 1 F 155 GLU ARG LEU CYS HIS PRO CYS PRO TRP GLU TRP THR PHE
SEQRES 2 F 155 PHE GLN GLY ASN CYS TYR PHE MET SER ASN SER GLN ARG
SEQRES 3 F 155 ASN TRP HIS ASP SER ILE THR ALA CYS LYS GLU VAL GLY
SEQRES 4 F 155 ALA GLN LEU VAL VAL ILE LYS SER ALA GLU GLU GLN ASN
SEQRES 5 F 155 PHE LEU GLN LEU GLN SER SER ARG SER ASN ARG PHE THR
SEQRES 6 F 155 TRP MET GLY LEU SER ASP LEU ASN GLN GLU GLY THR TRP
SEQRES 7 F 155 GLN TRP VAL ASP GLY SER PRO LEU LEU PRO SER PHE LYS
SEQRES 8 F 155 GLN TYR TRP ASN ARG GLY GLU PRO ASN ASN VAL GLY GLU
SEQRES 9 F 155 GLU ASP CYS ALA GLU PHE SER GLY ASN GLY TRP ASN ASP
SEQRES 10 F 155 ASP LYS CYS ASN LEU ALA LYS PHE TRP ILE CYS LYS LYS
SEQRES 11 F 155 SER ALA ALA SER CYS SER ARG ASP GLU GLU GLN PHE LEU
SEQRES 12 F 155 SER PRO ALA PRO ALA THR PRO ASN PRO PRO PRO ALA
HET EZ8 A1001 52
HET CA A1002 1
HET CA A1003 1
HET CA A1004 1
HET CL A1005 1
HET CL A1006 1
HET CL A1007 1
HET EZ8 B1001 52
HET CA B1002 1
HET CA B1003 1
HET CA B1004 1
HET CL B1005 1
HET CL B1006 1
HET EZ8 C1001 52
HET CA C1002 1
HET CA C1003 1
HET CA C1004 1
HET CL C1005 1
HET CL C1006 1
HET CL D 501 1
HET EZ8 D 502 52
HET CA D 503 1
HET CA D 504 1
HET CA D 505 1
HET CL D 506 1
HET CL E 501 1
HET CL E 502 1
HET EZ8 E 503 52
HET CA E 504 1
HET CA E 505 1
HET CA E 506 1
HET CL E 507 1
HET CL F 501 1
HET EZ8 F 502 52
HET CA F 503 1
HET CA F 504 1
HET CA F 505 1
HET CL F 506 1
HETNAM EZ8 [1-[(2~{S},3~{S},4~{R},5~{S},6~{R})-2-[(1~{S},2~{S},
HETNAM 2 EZ8 4~{S},5~{S})-2-(2-CHLOROETHYLOXY)-4,5-BIS[[4-
HETNAM 3 EZ8 (HYDROXYMETHYL)PHENYL]METHYLCARBAMOYL]CYCLOHEXYL]OXY-
HETNAM 4 EZ8 6-(HYDROXYMETHYL)-4,5-BIS(OXIDANYL)OXAN-3-YL]-1,2,3-
HETNAM 5 EZ8 TRIAZOL-4-YL]METHYLAZANIUM
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 7 EZ8 6(C35 H48 CL N6 O10 1+)
FORMUL 8 CA 18(CA 2+)
FORMUL 11 CL 14(CL 1-)
FORMUL 45 HOH *660(H2 O)
HELIX 1 1 ASN C 276 VAL C 287 1 12
HELIX 2 2 SER C 296 ASN C 311 1 16
HELIX 3 3 LEU C 336 TRP C 343 1 8
SHEET 1 1 1 THR C 261 PHE C 263 0
SHEET 2 2 1 ASN C 266 MET C 270 0
SHEET 3 3 1 GLN C 290 LEU C 291 0
SHEET 4 4 1 THR C 314 GLN C 323 0
SHEET 5 5 1 THR C 326 TRP C 329 0
SHEET 6 6 1 CYS C 356 SER C 360 0
SHEET 7 7 1 GLY C 363 ASP C 367 0
SHEET 8 8 1 PHE C 374 SER C 380 0
SSBOND 1 CYS A 253 CYS A 384 1555 1555 2.06
SSBOND 2 CYS A 256 CYS A 267 1555 1555 2.07
SSBOND 3 CYS A 284 CYS A 377 1555 1555 2.06
SSBOND 4 CYS A 356 CYS A 369 1555 1555 2.10
SSBOND 5 CYS B 253 CYS B 384 1555 1555 2.05
SSBOND 6 CYS B 256 CYS B 267 1555 1555 2.06
SSBOND 7 CYS B 284 CYS B 377 1555 1555 2.08
SSBOND 8 CYS B 356 CYS B 369 1555 1555 2.05
SSBOND 9 CYS C 253 CYS C 384 1555 1555 2.04
SSBOND 10 CYS C 256 CYS C 267 1555 1555 2.07
SSBOND 11 CYS C 284 CYS C 377 1555 1555 2.09
SSBOND 12 CYS C 356 CYS C 369 1555 1555 2.00
SSBOND 13 CYS D 253 CYS D 384 1555 1555 2.03
SSBOND 14 CYS D 256 CYS D 267 1555 1555 2.06
SSBOND 15 CYS D 284 CYS D 377 1555 1555 2.06
SSBOND 16 CYS D 356 CYS D 369 1555 1555 2.06
SSBOND 17 CYS E 253 CYS E 384 1555 1555 2.05
SSBOND 18 CYS E 256 CYS E 267 1555 1555 2.07
SSBOND 19 CYS E 284 CYS E 377 1555 1555 2.09
SSBOND 20 CYS E 356 CYS E 369 1555 1555 2.04
SSBOND 21 CYS F 253 CYS F 384 1555 1555 2.05
SSBOND 22 CYS F 256 CYS F 267 1555 1555 2.06
SSBOND 23 CYS F 284 CYS F 377 1555 1555 2.08
SSBOND 24 CYS F 356 CYS F 369 1555 1555 2.04
LINK OD1 ASP A 320 CA CA A1003 1555 1555 2.53
LINK OD2 ASP A 320 CA CA A1003 1555 1555 2.52
LINK OE1 GLU A 324 CA CA A1003 1555 1555 2.38
LINK OE2 GLU A 324 CA CA A1003 1555 1555 2.55
LINK OE1 GLU A 347 CA CA A1002 1555 1555 2.40
LINK OD1 ASN A 349 CA CA A1002 1555 1555 2.48
LINK OD1 ASN A 350 CA CA A1003 1555 1555 2.54
LINK OE1 GLU A 354 CA CA A1002 1555 1555 2.41
LINK O GLU A 354 CA CA A1003 1555 1555 2.54
LINK OD1 ASP A 355 CA CA A1003 1555 1555 2.20
LINK OD2 ASP A 355 CA CA A1004 1555 1555 2.21
LINK OD1 ASN A 365 CA CA A1002 1555 1555 2.40
LINK O ASP A 366 CA CA A1002 1555 1555 2.43
LINK OD1 ASP A 366 CA CA A1002 1555 1555 2.21
LINK O4 EZ8 A1001 CA CA A1002 1555 1555 2.65
LINK O3 EZ8 A1001 CA CA A1002 1555 1555 2.57
LINK CA CA A1003 O HOH A1129 1555 1555 2.08
LINK CA CA A1004 O HOH A1102 1555 1555 2.25
LINK CA CA A1004 O HOH A1118 1555 1555 2.21
LINK CA CA A1004 O HOH A1139 1555 1555 1.92
LINK CA CA A1004 O HOH D 607 1555 2555 2.05
LINK CA CA A1004 O HOH D 695 1555 2555 2.12
LINK OD1 ASP B 320 CA CA B1003 1555 1555 2.50
LINK OD2 ASP B 320 CA CA B1003 1555 1555 2.44
LINK OE1 GLU B 324 CA CA B1003 1555 1555 2.56
LINK OE2 GLU B 324 CA CA B1003 1555 1555 2.75
LINK OE1 GLU B 347 CA CA B1002 1555 1555 2.51
LINK OD1 ASN B 349 CA CA B1002 1555 1555 2.39
LINK OD1 ASN B 350 CA CA B1003 1555 1555 2.59
LINK OE1 GLU B 354 CA CA B1002 1555 1555 2.22
LINK O GLU B 354 CA CA B1003 1555 1555 2.30
LINK OD1 ASP B 355 CA CA B1003 1555 1555 2.30
LINK OD2 ASP B 355 CA CA B1004 1555 1555 2.09
LINK OD1 ASN B 365 CA CA B1002 1555 1555 2.51
LINK O ASP B 366 CA CA B1002 1555 1555 2.53
LINK OD1 ASP B 366 CA CA B1002 1555 1555 2.31
LINK O4 EZ8 B1001 CA CA B1002 1555 1555 2.51
LINK O3 EZ8 B1001 CA CA B1002 1555 1555 2.56
LINK CA CA B1003 O HOH B1133 1555 1555 2.43
LINK CA CA B1004 O HOH B1108 1555 1555 2.24
LINK CA CA B1004 O HOH B1126 1555 1555 2.33
LINK CA CA B1004 O HOH B1148 1555 1555 2.09
LINK CA CA B1004 O HOH B1155 1555 1555 2.24
LINK CA CA B1004 O HOH B1212 1555 1555 2.12
LINK OD1 ASP C 320 CA CA C1003 1555 1555 2.54
LINK OD2 ASP C 320 CA CA C1003 1555 1555 2.54
LINK OE1 GLU C 324 CA CA C1003 1555 1555 2.52
LINK OE2 GLU C 324 CA CA C1003 1555 1555 2.85
LINK OE1 GLU C 347 CA CA C1002 1555 1555 2.54
LINK OD1 ASN C 349 CA CA C1002 1555 1555 2.65
LINK OD1 ASN C 350 CA CA C1003 1555 1555 2.49
LINK OE1 GLU C 354 CA CA C1002 1555 1555 2.30
LINK O GLU C 354 CA CA C1003 1555 1555 2.46
LINK OD1 ASP C 355 CA CA C1003 1555 1555 2.40
LINK OD2 ASP C 355 CA CA C1004 1555 1555 2.05
LINK OD1 ASN C 365 CA CA C1002 1555 1555 2.35
LINK O ASP C 366 CA CA C1002 1555 1555 2.37
LINK OD1 ASP C 366 CA CA C1002 1555 1555 2.45
LINK O4 EZ8 C1001 CA CA C1002 1555 1555 2.53
LINK O3 EZ8 C1001 CA CA C1002 1555 1555 2.48
LINK CA CA C1003 O HOH C1121 1555 1555 2.18
LINK CA CA C1004 O HOH C1112 1555 1555 2.01
LINK CA CA C1004 O HOH C1126 1555 1555 2.00
LINK CA CA C1004 O HOH C1128 1555 1555 2.28
LINK CA CA C1004 O HOH C1130 1555 1555 2.04
LINK CA CA C1004 O HOH C1221 1555 1555 2.14
LINK OD1 ASP D 320 CA CA D 504 1555 1555 2.62
LINK OD2 ASP D 320 CA CA D 504 1555 1555 2.38
LINK OE1 GLU D 324 CA CA D 504 1555 1555 2.40
LINK OE2 GLU D 324 CA CA D 504 1555 1555 2.47
LINK OE1 GLU D 347 CA CA D 503 1555 1555 2.46
LINK OD1 ASN D 349 CA CA D 503 1555 1555 2.49
LINK OD1 ASN D 350 CA CA D 504 1555 1555 2.42
LINK OE1 GLU D 354 CA CA D 503 1555 1555 2.21
LINK O GLU D 354 CA CA D 504 1555 1555 2.39
LINK OD1 ASP D 355 CA CA D 504 1555 1555 2.19
LINK OD2 ASP D 355 CA CA D 505 1555 1555 2.38
LINK OD1 ASN D 365 CA CA D 503 1555 1555 2.65
LINK O ASP D 366 CA CA D 503 1555 1555 2.49
LINK OD1 ASP D 366 CA CA D 503 1555 1555 2.41
LINK O4 EZ8 D 502 CA CA D 503 1555 1555 2.51
LINK O3 EZ8 D 502 CA CA D 503 1555 1555 2.49
LINK CA CA D 504 O HOH D 623 1555 1555 2.16
LINK CA CA D 505 O HOH D 610 1555 1555 2.27
LINK CA CA D 505 O HOH D 617 1555 1555 2.16
LINK CA CA D 505 O HOH D 622 1555 1555 2.11
LINK CA CA D 505 O HOH D 649 1555 1555 2.01
LINK CA CA D 505 O HOH D 697 1555 1555 2.26
LINK OD1 ASP E 320 CA CA E 505 1555 1555 2.54
LINK OD2 ASP E 320 CA CA E 505 1555 1555 2.64
LINK OE1 GLU E 324 CA CA E 505 1555 1555 2.48
LINK OE2 GLU E 324 CA CA E 505 1555 1555 2.61
LINK OE1 GLU E 347 CA CA E 504 1555 1555 2.40
LINK OD1 ASN E 349 CA CA E 504 1555 1555 2.51
LINK OD1 ASN E 350 CA CA E 505 1555 1555 2.52
LINK OE1 GLU E 354 CA CA E 504 1555 1555 2.43
LINK O GLU E 354 CA CA E 505 1555 1555 2.45
LINK OD1 ASP E 355 CA CA E 505 1555 1555 2.24
LINK OD1 ASP E 355 CA CA E 506 1555 1555 2.99
LINK OD2 ASP E 355 CA CA E 506 1555 1555 2.28
LINK OD1 ASN E 365 CA CA E 504 1555 1555 2.35
LINK O ASP E 366 CA CA E 504 1555 1555 2.47
LINK OD1 ASP E 366 CA CA E 504 1555 1555 2.41
LINK O4 EZ8 E 503 CA CA E 504 1555 1555 2.59
LINK O3 EZ8 E 503 CA CA E 504 1555 1555 2.56
LINK CA CA E 505 O HOH E 638 1555 1555 2.03
LINK CA CA E 506 O HOH E 608 1555 1555 2.04
LINK CA CA E 506 O HOH E 613 1555 1555 2.09
LINK CA CA E 506 O HOH E 622 1555 1555 2.31
LINK CA CA E 506 O HOH E 629 1555 1555 2.03
LINK CA CA E 506 O HOH E 707 1555 1555 2.16
LINK O HOH E 614 CA CA F 505 2657 1555 2.13
LINK O HOH E 616 CA CA F 505 2657 1555 2.09
LINK OD1 ASP F 320 CA CA F 504 1555 1555 2.42
LINK OD2 ASP F 320 CA CA F 504 1555 1555 2.64
LINK OE1 GLU F 324 CA CA F 504 1555 1555 2.51
LINK OE2 GLU F 324 CA CA F 504 1555 1555 2.65
LINK OE1 GLU F 347 CA CA F 503 1555 1555 2.32
LINK OD1 ASN F 349 CA CA F 503 1555 1555 2.43
LINK OD1 ASN F 350 CA CA F 504 1555 1555 2.37
LINK OE1 GLU F 354 CA CA F 503 1555 1555 2.33
LINK O GLU F 354 CA CA F 504 1555 1555 2.35
LINK OD1 ASP F 355 CA CA F 504 1555 1555 2.38
LINK OD2 ASP F 355 CA CA F 505 1555 1555 2.20
LINK OD1 ASN F 365 CA CA F 503 1555 1555 2.36
LINK O ASP F 366 CA CA F 503 1555 1555 2.45
LINK OD1 ASP F 366 CA CA F 503 1555 1555 2.36
LINK O4 EZ8 F 502 CA CA F 503 1555 1555 2.51
LINK O3 EZ8 F 502 CA CA F 503 1555 1555 2.45
LINK CA CA F 504 O HOH F 618 1555 1555 2.33
LINK CA CA F 505 O HOH F 604 1555 1555 2.06
LINK CA CA F 505 O HOH F 605 1555 1555 2.02
LINK CA CA F 505 O HOH F 693 1555 1555 2.29
CISPEP 1 GLU A 347 PRO A 348 0 2.28
CISPEP 2 GLU B 347 PRO B 348 0 -11.02
CISPEP 3 GLU C 347 PRO C 348 0 4.23
CISPEP 4 GLU D 347 PRO D 348 0 -3.43
CISPEP 5 GLU E 347 PRO E 348 0 -6.96
CISPEP 6 GLU F 347 PRO F 348 0 -6.57
SITE 1 AC1 21 PHE A 313 GLU A 347 ASN A 349 GLY A 352
SITE 2 AC1 21 GLU A 354 GLU A 358 SER A 360 ASN A 365
SITE 3 AC1 21 ASP A 366 ASP A 367 LYS A 368 CA A1002
SITE 4 AC1 21 HOH A1108 HOH A1113 ASN D 272 ARG D 309
SITE 5 AC1 21 SER D 310 ASN D 311 ARG D 312 THR D 314
SITE 6 AC1 21 CL D 501
SITE 1 AC2 6 GLU A 347 ASN A 349 GLU A 354 ASN A 365
SITE 2 AC2 6 ASP A 366 EZ8 A1001
SITE 1 AC3 6 ASP A 320 GLU A 324 ASN A 350 GLU A 354
SITE 2 AC3 6 ASP A 355 HOH A1129
SITE 1 AC4 4 ASP A 355 HOH A1102 HOH A1118 HOH A1139
SITE 1 AC5 2 ASN A 272 SER A 273
SITE 1 AC6 1 ARG A 309
SITE 1 AC7 2 GLN A 264 EZ8 B1001
SITE 1 AC8 29 GLN A 264 GLY A 265 CL A1007 PHE B 313
SITE 2 AC8 29 GLU B 347 ASN B 349 VAL B 351 GLY B 352
SITE 3 AC8 29 GLU B 354 GLU B 358 SER B 360 ASN B 365
SITE 4 AC8 29 ASP B 366 ASP B 367 LYS B 368 CA B1002
SITE 5 AC8 29 HOH B1105 HOH B1111 HOH B1116 HOH B1151
SITE 6 AC8 29 ASN C 272 GLN C 306 ARG C 309 SER C 310
SITE 7 AC8 29 ASN C 311 ARG C 312 THR C 314 PHE C 374
SITE 8 AC8 29 HOH C1139
SITE 1 AC9 6 GLU B 347 ASN B 349 GLU B 354 ASN B 365
SITE 2 AC9 6 ASP B 366 EZ8 B1001
SITE 1 AD1 6 ASP B 320 GLU B 324 ASN B 350 GLU B 354
SITE 2 AD1 6 ASP B 355 HOH B1133
SITE 1 AD2 6 ASP B 355 HOH B1108 HOH B1126 HOH B1148
SITE 2 AD2 6 HOH B1155 HOH B1212
SITE 1 AD3 1 SER B 273
SITE 1 AD4 2 GLN B 264 EZ8 F 502
SITE 1 AD5 28 ASN B 272 GLN B 306 ARG B 309 SER B 310
SITE 2 AD5 28 ASN B 311 ARG B 312 THR B 314 PHE B 374
SITE 3 AD5 28 PHE C 313 GLU C 347 ASN C 349 VAL C 351
SITE 4 AD5 28 GLY C 352 GLU C 354 GLU C 358 SER C 360
SITE 5 AD5 28 ASN C 365 ASP C 366 ASP C 367 LYS C 368
SITE 6 AD5 28 CA C1002 HOH C1105 HOH C1111 HOH C1124
SITE 7 AD5 28 GLN E 264 GLY E 265 GLU E 298 CL E 502
SITE 1 AD6 6 GLU C 347 ASN C 349 GLU C 354 ASN C 365
SITE 2 AD6 6 ASP C 366 EZ8 C1001
SITE 1 AD7 6 ASP C 320 GLU C 324 ASN C 350 GLU C 354
SITE 2 AD7 6 ASP C 355 HOH C1121
SITE 1 AD8 6 ASP C 355 HOH C1112 HOH C1126 HOH C1128
SITE 2 AD8 6 HOH C1130 HOH C1221
SITE 1 AD9 2 ASN C 272 SER C 273
SITE 1 AE1 2 GLN C 264 EZ8 D 502
SITE 1 AE2 1 EZ8 A1001
SITE 1 AE3 27 SER A 271 ASN A 272 ARG A 309 SER A 310
SITE 2 AE3 27 ASN A 311 ARG A 312 THR A 314 PHE A 374
SITE 3 AE3 27 PHE C 263 GLN C 264 GLY C 265 GLU C 298
SITE 4 AE3 27 CL C1006 PHE D 313 GLU D 347 ASN D 349
SITE 5 AE3 27 VAL D 351 GLU D 354 GLU D 358 SER D 360
SITE 6 AE3 27 ASN D 365 ASP D 366 ASP D 367 LYS D 368
SITE 7 AE3 27 CA D 503 HOH D 601 HOH D 628
SITE 1 AE4 6 GLU D 347 ASN D 349 GLU D 354 ASN D 365
SITE 2 AE4 6 ASP D 366 EZ8 D 502
SITE 1 AE5 6 ASP D 320 GLU D 324 ASN D 350 GLU D 354
SITE 2 AE5 6 ASP D 355 HOH D 623
SITE 1 AE6 6 ASP D 355 HOH D 610 HOH D 617 HOH D 622
SITE 2 AE6 6 HOH D 649 HOH D 697
SITE 1 AE7 2 ASN D 272 SER D 273
SITE 1 AE8 2 ARG B 309 ARG E 309
SITE 1 AE9 2 EZ8 C1001 GLN E 264
SITE 1 AF1 25 PHE E 313 GLU E 347 ASN E 349 VAL E 351
SITE 2 AF1 25 GLY E 352 GLU E 354 GLU E 358 SER E 360
SITE 3 AF1 25 ASN E 365 ASP E 366 ASP E 367 LYS E 368
SITE 4 AF1 25 CA E 504 HOH E 615 HOH E 620 HOH E 648
SITE 5 AF1 25 HOH E 650 ASN F 272 ARG F 309 SER F 310
SITE 6 AF1 25 ASN F 311 ARG F 312 THR F 314 PHE F 374
SITE 7 AF1 25 CL F 501
SITE 1 AF2 6 GLU E 347 ASN E 349 GLU E 354 ASN E 365
SITE 2 AF2 6 ASP E 366 EZ8 E 503
SITE 1 AF3 6 ASP E 320 GLU E 324 ASN E 350 GLU E 354
SITE 2 AF3 6 ASP E 355 HOH E 638
SITE 1 AF4 7 GLU E 324 ASP E 355 HOH E 608 HOH E 613
SITE 2 AF4 7 HOH E 622 HOH E 629 HOH E 707
SITE 1 AF5 2 ASN E 272 SER E 273
SITE 1 AF6 1 EZ8 E 503
SITE 1 AF7 26 GLN B 264 GLY B 265 CL B1006 ASN E 272
SITE 2 AF7 26 ARG E 309 SER E 310 ASN E 311 ARG E 312
SITE 3 AF7 26 THR E 314 PHE E 374 PHE F 313 GLU F 347
SITE 4 AF7 26 ASN F 349 VAL F 351 GLY F 352 GLU F 354
SITE 5 AF7 26 GLU F 358 SER F 360 ASN F 365 ASP F 366
SITE 6 AF7 26 ASP F 367 LYS F 368 CA F 503 HOH F 602
SITE 7 AF7 26 HOH F 615 HOH F 622
SITE 1 AF8 6 GLU F 347 ASN F 349 GLU F 354 ASN F 365
SITE 2 AF8 6 ASP F 366 EZ8 F 502
SITE 1 AF9 6 ASP F 320 GLU F 324 ASN F 350 GLU F 354
SITE 2 AF9 6 ASP F 355 HOH F 618
SITE 1 AG1 4 ASP F 355 HOH F 604 HOH F 605 HOH F 693
SITE 1 AG2 3 SER F 271 ASN F 272 SER F 273
CRYST1 105.612 57.507 107.247 90.00 118.67 90.00 P 1 21 1 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009469 0.000000 0.005177 0.00000
SCALE2 0.000000 0.017389 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010627 0.00000
ATOM 1 N LEU C 252 -29.118 -11.127 20.479 1.00 68.74 N
ATOM 2 CA LEU C 252 -27.729 -11.680 20.521 1.00 66.36 C
ATOM 3 C LEU C 252 -27.462 -12.380 21.863 1.00 65.89 C
ATOM 4 O LEU C 252 -27.884 -11.898 22.920 1.00 71.43 O
ATOM 5 CB LEU C 252 -26.692 -10.569 20.301 1.00 65.39 C
ATOM 6 CG LEU C 252 -25.307 -11.072 19.849 1.00 69.06 C
ATOM 7 CD1 LEU C 252 -25.360 -11.516 18.385 1.00 67.88 C
ATOM 8 CD2 LEU C 252 -24.210 -10.025 20.061 1.00 66.96 C
ATOM 9 N CYS C 253 -26.770 -13.517 21.806 1.00 60.18 N
ATOM 10 CA CYS C 253 -26.334 -14.261 22.994 1.00 52.49 C
ATOM 11 C CYS C 253 -24.956 -13.736 23.457 1.00 47.74 C
ATOM 12 O CYS C 253 -24.056 -13.542 22.634 1.00 44.62 O
ATOM 13 CB CYS C 253 -26.246 -15.733 22.618 1.00 49.88 C
ATOM 14 SG CYS C 253 -25.583 -16.872 23.859 1.00 44.89 S
ATOM 15 N HIS C 254 -24.786 -13.520 24.756 1.00 39.39 N
ATOM 16 CA HIS C 254 -23.457 -13.162 25.293 1.00 36.10 C
ATOM 17 C HIS C 254 -23.005 -14.242 26.237 1.00 35.49 C
ATOM 18 O HIS C 254 -23.838 -14.835 26.951 1.00 33.08 O
ATOM 19 CB HIS C 254 -23.466 -11.801 26.008 1.00 37.55 C
ATOM 20 CG HIS C 254 -24.049 -10.683 25.191 1.00 39.73 C
ATOM 21 ND1 HIS C 254 -23.280 -9.850 24.404 1.00 41.14 N
ATOM 22 CD2 HIS C 254 -25.331 -10.264 25.037 1.00 40.27 C
ATOM 23 CE1 HIS C 254 -24.062 -8.970 23.800 1.00 39.56 C
ATOM 24 NE2 HIS C 254 -25.309 -9.195 24.172 1.00 37.91 N
ATOM 25 N PRO C 255 -21.673 -14.518 26.257 1.00 30.93 N
ATOM 26 CA PRO C 255 -21.168 -15.519 27.181 1.00 28.15 C
ATOM 27 C PRO C 255 -21.536 -15.223 28.612 1.00 26.91 C
ATOM 28 O PRO C 255 -21.913 -16.124 29.353 1.00 23.00 O
ATOM 29 CB PRO C 255 -19.660 -15.425 26.994 1.00 31.22 C
ATOM 30 CG PRO C 255 -19.501 -14.973 25.574 1.00 31.48 C
ATOM 31 CD PRO C 255 -20.588 -13.956 25.432 1.00 30.92 C
ATOM 32 N CYS C 256 -21.425 -13.965 28.999 1.00 26.32 N
ATOM 33 CA CYS C 256 -21.693 -13.581 30.383 1.00 27.51 C
ATOM 34 C CYS C 256 -22.772 -12.498 30.480 1.00 29.78 C
ATOM 35 O CYS C 256 -23.051 -11.794 29.504 1.00 28.78 O
ATOM 36 CB CYS C 256 -20.421 -13.018 31.010 1.00 28.02 C
ATOM 37 SG CYS C 256 -19.110 -14.204 31.112 1.00 31.38 S
ATOM 38 N PRO C 257 -23.337 -12.311 31.681 1.00 33.01 N
ATOM 39 CA PRO C 257 -24.219 -11.189 31.844 1.00 31.49 C
ATOM 40 C PRO C 257 -23.450 -9.888 31.789 1.00 30.36 C
ATOM 41 O PRO C 257 -22.202 -9.845 31.939 1.00 29.30 O
ATOM 42 CB PRO C 257 -24.819 -11.409 33.247 1.00 34.15 C
ATOM 43 CG PRO C 257 -24.663 -12.879 33.493 1.00 36.60 C
ATOM 44 CD PRO C 257 -23.305 -13.145 32.897 1.00 36.41 C
ATOM 45 N TRP C 258 -24.209 -8.829 31.572 1.00 32.59 N
ATOM 46 CA TRP C 258 -23.658 -7.503 31.341 1.00 34.87 C
ATOM 47 C TRP C 258 -22.903 -7.092 32.601 1.00 35.94 C
ATOM 48 O TRP C 258 -23.415 -7.237 33.740 1.00 36.41 O
ATOM 49 CB TRP C 258 -24.804 -6.547 31.010 1.00 35.95 C
ATOM 50 CG TRP C 258 -24.440 -5.252 30.285 1.00 39.09 C
ATOM 51 CD1 TRP C 258 -23.273 -4.554 30.375 1.00 39.58 C
ATOM 52 CD2 TRP C 258 -25.298 -4.477 29.436 1.00 39.11 C
ATOM 53 NE1 TRP C 258 -23.332 -3.424 29.605 1.00 39.96 N
ATOM 54 CE2 TRP C 258 -24.567 -3.340 29.030 1.00 38.78 C
ATOM 55 CE3 TRP C 258 -26.614 -4.633 28.987 1.00 40.88 C
ATOM 56 CZ2 TRP C 258 -25.101 -2.358 28.194 1.00 41.13 C
ATOM 57 CZ3 TRP C 258 -27.146 -3.665 28.155 1.00 43.22 C
ATOM 58 CH2 TRP C 258 -26.381 -2.537 27.757 1.00 44.02 C
ATOM 59 N GLU C 259 -21.680 -6.619 32.391 1.00 35.39 N
ATOM 60 CA GLU C 259 -20.747 -6.209 33.459 1.00 39.35 C
ATOM 61 C GLU C 259 -19.937 -7.320 34.116 1.00 38.70 C
ATOM 62 O GLU C 259 -18.952 -7.018 34.793 1.00 45.38 O
ATOM 63 CB GLU C 259 -21.421 -5.356 34.549 1.00 42.94 C
ATOM 64 CG GLU C 259 -22.247 -4.232 33.947 1.00 47.40 C
ATOM 65 CD GLU C 259 -22.541 -3.104 34.900 1.00 49.70 C
ATOM 66 OE1 GLU C 259 -22.036 -3.150 36.031 1.00 54.78 O
ATOM 67 OE2 GLU C 259 -23.275 -2.173 34.504 1.00 50.31 O
ATOM 68 N TRP C 260 -20.306 -8.586 33.912 1.00 33.22 N
ATOM 69 CA TRP C 260 -19.502 -9.682 34.407 1.00 30.39 C
ATOM 70 C TRP C 260 -18.304 -9.763 33.490 1.00 30.21 C
ATOM 71 O TRP C 260 -18.396 -9.372 32.334 1.00 27.77 O
ATOM 72 CB TRP C 260 -20.259 -10.998 34.399 1.00 28.77 C
ATOM 73 CG TRP C 260 -21.359 -11.042 35.399 1.00 28.87 C
ATOM 74 CD1 TRP C 260 -22.317 -10.107 35.574 1.00 31.75 C
ATOM 75 CD2 TRP C 260 -21.624 -12.071 36.370 1.00 28.11 C
ATOM 76 NE1 TRP C 260 -23.167 -10.484 36.584 1.00 31.95 N
ATOM 77 CE2 TRP C 260 -22.748 -11.677 37.097 1.00 29.49 C
ATOM 78 CE3 TRP C 260 -20.995 -13.262 36.715 1.00 29.35 C
ATOM 79 CZ2 TRP C 260 -23.278 -12.433 38.111 1.00 30.58 C
ATOM 80 CZ3 TRP C 260 -21.514 -14.007 37.741 1.00 29.34 C
ATOM 81 CH2 TRP C 260 -22.649 -13.588 38.427 1.00 29.17 C
ATOM 82 N THR C 261 -17.187 -10.268 34.019 1.00 29.02 N
ATOM 83 CA THR C 261 -15.978 -10.500 33.235 1.00 29.20 C
ATOM 84 C THR C 261 -15.877 -11.941 32.797 1.00 28.70 C
ATOM 85 O THR C 261 -16.023 -12.855 33.607 1.00 30.78 O
ATOM 86 CB THR C 261 -14.770 -10.225 34.114 1.00 27.61 C
ATOM 87 OG1 THR C 261 -14.845 -8.900 34.566 1.00 30.55 O
ATOM 88 CG2 THR C 261 -13.475 -10.420 33.367 1.00 29.81 C
ATOM 89 N PHE C 262 -15.593 -12.151 31.522 1.00 30.86 N
ATOM 90 CA PHE C 262 -15.430 -13.489 30.976 1.00 27.19 C
ATOM 91 C PHE C 262 -14.016 -13.892 31.270 1.00 26.84 C
ATOM 92 O PHE C 262 -13.123 -13.124 30.953 1.00 29.48 O
ATOM 93 CB PHE C 262 -15.597 -13.493 29.450 1.00 29.33 C
ATOM 94 CG PHE C 262 -15.366 -14.858 28.831 1.00 27.68 C
ATOM 95 CD1 PHE C 262 -16.394 -15.771 28.762 1.00 28.12 C
ATOM 96 CD2 PHE C 262 -14.116 -15.231 28.360 1.00 28.00 C
ATOM 97 CE1 PHE C 262 -16.196 -17.034 28.202 1.00 29.67 C
ATOM 98 CE2 PHE C 262 -13.896 -16.504 27.843 1.00 28.03 C
ATOM 99 CZ PHE C 262 -14.940 -17.404 27.760 1.00 29.89 C
ATOM 100 N PHE C 263 -13.784 -15.068 31.834 1.00 23.91 N
ATOM 101 CA PHE C 263 -12.411 -15.582 31.953 1.00 26.83 C
ATOM 102 C PHE C 263 -12.420 -17.125 31.857 1.00 28.90 C
ATOM 103 O PHE C 263 -13.034 -17.843 32.713 1.00 26.03 O
ATOM 104 CB PHE C 263 -11.729 -15.087 33.238 1.00 28.52 C
ATOM 105 CG PHE C 263 -10.336 -15.606 33.442 1.00 29.35 C
ATOM 106 CD1 PHE C 263 -10.120 -16.793 34.106 1.00 31.01 C
ATOM 107 CD2 PHE C 263 -9.257 -14.923 32.952 1.00 31.58 C
ATOM 108 CE1 PHE C 263 -8.846 -17.287 34.292 1.00 32.46 C
ATOM 109 CE2 PHE C 263 -7.980 -15.404 33.146 1.00 32.91 C
ATOM 110 CZ PHE C 263 -7.774 -16.585 33.815 1.00 31.55 C
ATOM 111 N GLN C 264 -11.746 -17.612 30.802 1.00 24.96 N
ATOM 112 CA GLN C 264 -11.581 -19.047 30.534 1.00 26.16 C
ATOM 113 C GLN C 264 -12.859 -19.850 30.719 1.00 25.19 C
ATOM 114 O GLN C 264 -12.875 -20.864 31.398 1.00 26.58 O
ATOM 115 CB GLN C 264 -10.466 -19.667 31.401 1.00 25.50 C
ATOM 116 CG GLN C 264 -9.187 -18.898 31.340 1.00 26.07 C
ATOM 117 CD GLN C 264 -7.969 -19.726 31.692 1.00 30.34 C
ATOM 118 OE1 GLN C 264 -8.028 -20.659 32.504 1.00 28.97 O
ATOM 119 NE2 GLN C 264 -6.832 -19.377 31.075 1.00 28.56 N
ATOM 120 N GLY C 265 -13.923 -19.372 30.102 1.00 27.65 N
ATOM 121 CA GLY C 265 -15.196 -20.082 30.059 1.00 29.66 C
ATOM 122 C GLY C 265 -16.116 -19.868 31.248 1.00 29.17 C
ATOM 123 O GLY C 265 -17.150 -20.550 31.374 1.00 27.88 O
ATOM 124 N ASN C 266 -15.728 -18.977 32.154 1.00 28.69 N
ATOM 125 CA ASN C 266 -16.584 -18.646 33.294 1.00 26.57 C
ATOM 126 C ASN C 266 -16.748 -17.127 33.328 1.00 28.80 C
ATOM 127 O ASN C 266 -16.017 -16.363 32.657 1.00 27.54 O
ATOM 128 CB ASN C 266 -16.001 -19.193 34.610 1.00 26.31 C
ATOM 129 CG ASN C 266 -15.937 -20.751 34.657 1.00 28.55 C
ATOM 130 OD1 ASN C 266 -16.945 -21.412 34.839 1.00 28.93 O
ATOM 131 ND2 ASN C 266 -14.728 -21.315 34.565 1.00 24.94 N
ATOM 132 N CYS C 267 -17.742 -16.718 34.092 1.00 27.65 N
ATOM 133 CA CYS C 267 -18.127 -15.354 34.248 1.00 29.47 C
ATOM 134 C CYS C 267 -17.934 -15.002 35.693 1.00 29.99 C
ATOM 135 O CYS C 267 -18.440 -15.734 36.576 1.00 26.67 O
ATOM 136 CB CYS C 267 -19.622 -15.211 33.899 1.00 31.00 C
ATOM 137 SG CYS C 267 -19.969 -15.730 32.213 1.00 30.36 S
ATOM 138 N TYR C 268 -17.274 -13.866 35.920 1.00 27.72 N
ATOM 139 CA TYR C 268 -17.003 -13.365 37.243 1.00 27.75 C
ATOM 140 C TYR C 268 -17.654 -11.997 37.481 1.00 27.16 C
ATOM 141 O TYR C 268 -17.553 -11.056 36.650 1.00 27.39 O
ATOM 142 CB TYR C 268 -15.485 -13.311 37.502 1.00 28.40 C
ATOM 143 CG TYR C 268 -14.803 -14.654 37.334 1.00 28.61 C
ATOM 144 CD1 TYR C 268 -14.495 -15.142 36.070 1.00 27.27 C
ATOM 145 CD2 TYR C 268 -14.478 -15.447 38.430 1.00 28.12 C
ATOM 146 CE1 TYR C 268 -13.877 -16.376 35.899 1.00 29.66 C
ATOM 147 CE2 TYR C 268 -13.869 -16.681 38.264 1.00 28.29 C
ATOM 148 CZ TYR C 268 -13.551 -17.126 36.985 1.00 27.89 C
ATOM 149 OH TYR C 268 -12.971 -18.353 36.794 1.00 29.71 O
ATOM 150 N PHE C 269 -18.362 -11.916 38.605 1.00 26.07 N
ATOM 151 CA PHE C 269 -18.873 -10.675 39.133 1.00 26.73 C
ATOM 152 C PHE C 269 -17.933 -10.163 40.223 1.00 26.26 C
ATOM 153 O PHE C 269 -17.733 -10.834 41.222 1.00 26.50 O
ATOM 154 CB PHE C 269 -20.240 -10.885 39.730 1.00 28.84 C
ATOM 155 CG PHE C 269 -20.858 -9.618 40.256 1.00 31.35 C
ATOM 156 CD1 PHE C 269 -21.165 -8.578 39.384 1.00 34.90 C
ATOM 157 CD2 PHE C 269 -21.086 -9.445 41.618 1.00 33.18 C
ATOM 158 CE1 PHE C 269 -21.724 -7.377 39.855 1.00 36.70 C
ATOM 159 CE2 PHE C 269 -21.637 -8.252 42.105 1.00 34.31 C
ATOM 160 CZ PHE C 269 -21.964 -7.221 41.220 1.00 35.64 C
ATOM 161 N MET C 270 -17.354 -8.992 40.010 1.00 28.08 N
ATOM 162 CA MET C 270 -16.534 -8.334 41.012 1.00 27.74 C
ATOM 163 C MET C 270 -17.440 -7.320 41.691 1.00 25.64 C
ATOM 164 O MET C 270 -17.881 -6.405 41.044 1.00 24.80 O
ATOM 165 CB MET C 270 -15.344 -7.598 40.370 1.00 31.89 C
ATOM 166 CG MET C 270 -14.688 -8.277 39.169 1.00 39.62 C
ATOM 167 SD MET C 270 -14.141 -9.929 39.503 1.00 46.97 S
ATOM 168 CE MET C 270 -12.841 -10.162 38.298 1.00 48.86 C
ATOM 169 N SER C 271 -17.743 -7.482 42.972 1.00 24.65 N
ATOM 170 CA SER C 271 -18.640 -6.523 43.662 1.00 26.55 C
ATOM 171 C SER C 271 -17.985 -5.139 43.772 1.00 26.66 C
ATOM 172 O SER C 271 -16.767 -5.046 43.837 1.00 25.32 O
ATOM 173 CB SER C 271 -18.960 -7.027 45.082 1.00 22.62 C
ATOM 174 OG SER C 271 -17.849 -6.777 45.935 1.00 24.31 O
ATOM 175 N ASN C 272 -18.764 -4.079 43.886 1.00 29.43 N
ATOM 176 CA AASN C 272 -18.207 -2.770 44.178 0.50 29.80 C
ATOM 177 CA BASN C 272 -18.159 -2.763 44.235 0.50 30.39 C
ATOM 178 C ASN C 272 -18.696 -2.308 45.563 1.00 30.10 C
ATOM 179 O ASN C 272 -18.531 -1.152 45.917 1.00 29.82 O
ATOM 180 CB AASN C 272 -18.536 -1.768 43.046 0.50 31.63 C
ATOM 181 CB BASN C 272 -18.351 -1.657 43.169 0.50 33.18 C
ATOM 182 CG AASN C 272 -17.700 -1.996 41.762 0.50 31.66 C
ATOM 183 CG BASN C 272 -17.274 -0.529 43.238 0.50 34.59 C
ATOM 184 OD1AASN C 272 -16.493 -2.313 41.805 0.50 30.89 O
ATOM 185 OD1BASN C 272 -16.752 -0.155 44.313 0.50 36.43 O
ATOM 186 ND2AASN C 272 -18.346 -1.799 40.608 0.50 30.93 N
ATOM 187 ND2BASN C 272 -16.975 0.047 42.074 0.50 34.10 N
ATOM 188 N SER C 273 -19.276 -3.229 46.336 1.00 28.07 N
ATOM 189 CA SER C 273 -19.546 -2.957 47.754 1.00 27.93 C
ATOM 190 C SER C 273 -19.106 -4.162 48.624 1.00 27.46 C
ATOM 191 O SER C 273 -18.477 -5.131 48.116 1.00 25.90 O
ATOM 192 CB SER C 273 -21.032 -2.632 47.951 1.00 31.25 C
ATOM 193 OG SER C 273 -21.808 -3.786 47.659 1.00 33.61 O
ATOM 194 N GLN C 274 -19.387 -4.103 49.920 1.00 23.65 N
ATOM 195 CA GLN C 274 -18.796 -5.056 50.849 1.00 26.64 C
ATOM 196 C GLN C 274 -19.841 -5.789 51.694 1.00 26.39 C
ATOM 197 O GLN C 274 -20.825 -5.218 52.093 1.00 25.46 O
ATOM 198 CB GLN C 274 -17.776 -4.365 51.767 1.00 26.10 C
ATOM 199 CG GLN C 274 -16.703 -3.532 51.041 1.00 27.47 C
ATOM 200 CD GLN C 274 -16.321 -2.274 51.837 1.00 28.83 C
ATOM 201 OE1 GLN C 274 -17.106 -1.315 51.912 1.00 28.11 O
ATOM 202 NE2 GLN C 274 -15.132 -2.284 52.448 1.00 26.38 N
ATOM 203 N ARG C 275 -19.588 -7.056 51.951 1.00 24.80 N
ATOM 204 CA ARG C 275 -20.497 -7.911 52.706 1.00 26.00 C
ATOM 205 C ARG C 275 -19.677 -8.894 53.499 1.00 25.07 C
ATOM 206 O ARG C 275 -18.547 -9.235 53.126 1.00 22.00 O
ATOM 207 CB ARG C 275 -21.420 -8.687 51.767 1.00 28.84 C
ATOM 208 CG ARG C 275 -22.585 -7.915 51.233 1.00 28.98 C
ATOM 209 CD ARG C 275 -23.371 -8.768 50.289 1.00 34.31 C
ATOM 210 NE ARG C 275 -24.540 -8.053 49.796 1.00 40.38 N
ATOM 211 CZ ARG C 275 -25.787 -8.534 49.769 1.00 44.79 C
ATOM 212 NH1 ARG C 275 -26.080 -9.795 50.153 1.00 43.60 N
ATOM 213 NH2 ARG C 275 -26.753 -7.746 49.323 1.00 43.84 N
ATOM 214 N ASN C 276 -20.243 -9.370 54.593 1.00 26.13 N
ATOM 215 CA ASN C 276 -19.614 -10.439 55.302 1.00 25.05 C
ATOM 216 C ASN C 276 -19.651 -11.680 54.419 1.00 23.10 C
ATOM 217 O ASN C 276 -20.314 -11.726 53.385 1.00 26.16 O
ATOM 218 CB ASN C 276 -20.204 -10.638 56.730 1.00 24.33 C
ATOM 219 CG ASN C 276 -21.638 -11.182 56.735 1.00 26.28 C
ATOM 220 OD1 ASN C 276 -22.030 -11.927 55.856 1.00 22.82 O
ATOM 221 ND2 ASN C 276 -22.410 -10.821 57.758 1.00 23.04 N
ATOM 222 N TRP C 277 -18.937 -12.696 54.839 1.00 23.05 N
ATOM 223 CA TRP C 277 -18.762 -13.895 54.025 1.00 22.29 C
ATOM 224 C TRP C 277 -20.096 -14.587 53.694 1.00 22.51 C
ATOM 225 O TRP C 277 -20.327 -14.988 52.565 1.00 21.11 O
ATOM 226 CB TRP C 277 -17.786 -14.824 54.717 1.00 20.37 C
ATOM 227 CG TRP C 277 -17.254 -15.933 53.878 1.00 20.38 C
ATOM 228 CD1 TRP C 277 -16.241 -15.877 52.995 1.00 18.82 C
ATOM 229 CD2 TRP C 277 -17.684 -17.293 53.913 1.00 20.90 C
ATOM 230 NE1 TRP C 277 -16.016 -17.117 52.444 1.00 17.83 N
ATOM 231 CE2 TRP C 277 -16.889 -18.004 53.007 1.00 20.12 C
ATOM 232 CE3 TRP C 277 -18.674 -17.976 54.628 1.00 23.18 C
ATOM 233 CZ2 TRP C 277 -17.055 -19.349 52.778 1.00 20.85 C
ATOM 234 CZ3 TRP C 277 -18.836 -19.325 54.399 1.00 23.75 C
ATOM 235 CH2 TRP C 277 -18.029 -19.991 53.473 1.00 23.79 C
ATOM 236 N HIS C 278 -21.002 -14.651 54.660 1.00 22.48 N
ATOM 237 CA HIS C 278 -22.168 -15.445 54.545 1.00 24.58 C
ATOM 238 C HIS C 278 -23.139 -14.733 53.652 1.00 24.28 C
ATOM 239 O HIS C 278 -23.762 -15.343 52.764 1.00 27.61 O
ATOM 240 CB HIS C 278 -22.767 -15.784 55.958 1.00 27.51 C
ATOM 241 CG HIS C 278 -22.160 -17.003 56.578 1.00 33.72 C
ATOM 242 ND1 HIS C 278 -21.226 -16.947 57.602 1.00 37.73 N
ATOM 243 CD2 HIS C 278 -22.341 -18.324 56.304 1.00 38.26 C
ATOM 244 CE1 HIS C 278 -20.863 -18.176 57.922 1.00 37.39 C
ATOM 245 NE2 HIS C 278 -21.538 -19.030 57.164 1.00 36.89 N
ATOM 246 N ASP C 279 -23.228 -13.425 53.813 1.00 23.02 N
ATOM 247 CA ASP C 279 -24.003 -12.629 52.911 1.00 22.25 C
ATOM 248 C ASP C 279 -23.419 -12.577 51.483 1.00 24.13 C
ATOM 249 O ASP C 279 -24.177 -12.344 50.515 1.00 22.02 O
ATOM 250 CB ASP C 279 -24.102 -11.233 53.448 1.00 25.50 C
ATOM 251 CG ASP C 279 -24.943 -11.170 54.725 1.00 28.82 C
ATOM 252 OD1 ASP C 279 -25.581 -12.191 55.069 1.00 30.43 O
ATOM 253 OD2 ASP C 279 -24.956 -10.103 55.366 1.00 30.47 O
ATOM 254 N SER C 280 -22.097 -12.719 51.345 1.00 21.89 N
ATOM 255 CA SER C 280 -21.502 -12.774 50.001 1.00 21.85 C
ATOM 256 C SER C 280 -21.957 -14.077 49.327 1.00 22.44 C
ATOM 257 O SER C 280 -22.295 -14.092 48.175 1.00 25.02 O
ATOM 258 CB SER C 280 -19.993 -12.715 50.067 1.00 21.18 C
ATOM 259 OG SER C 280 -19.534 -11.489 50.613 1.00 20.81 O
ATOM 260 N ILE C 281 -21.991 -15.164 50.071 1.00 23.74 N
ATOM 261 CA ILE C 281 -22.445 -16.397 49.536 1.00 23.24 C
ATOM 262 C ILE C 281 -23.895 -16.241 49.007 1.00 26.92 C
ATOM 263 O ILE C 281 -24.235 -16.699 47.893 1.00 24.07 O
ATOM 264 CB ILE C 281 -22.351 -17.493 50.610 1.00 25.14 C
ATOM 265 CG1 ILE C 281 -20.895 -17.880 50.686 1.00 28.26 C
ATOM 266 CG2 ILE C 281 -23.248 -18.694 50.297 1.00 23.84 C
ATOM 267 CD1 ILE C 281 -20.610 -18.989 51.613 1.00 33.07 C
ATOM 268 N THR C 282 -24.734 -15.591 49.801 1.00 23.92 N
ATOM 269 CA THR C 282 -26.109 -15.412 49.437 1.00 24.34 C
ATOM 270 C THR C 282 -26.219 -14.582 48.181 1.00 24.95 C
ATOM 271 O THR C 282 -27.013 -14.878 47.298 1.00 26.89 O
ATOM 272 CB THR C 282 -26.859 -14.670 50.547 1.00 26.06 C
ATOM 273 OG1 THR C 282 -26.824 -15.458 51.744 1.00 25.80 O
ATOM 274 CG2 THR C 282 -28.296 -14.424 50.122 1.00 28.17 C
ATOM 275 N ALA C 283 -25.466 -13.500 48.142 1.00 23.88 N
ATOM 276 CA ALA C 283 -25.519 -12.580 47.072 1.00 25.25 C
ATOM 277 C ALA C 283 -25.185 -13.317 45.761 1.00 25.16 C
ATOM 278 O ALA C 283 -25.874 -13.181 44.774 1.00 26.34 O
ATOM 279 CB ALA C 283 -24.549 -11.424 47.324 1.00 26.33 C
ATOM 280 N CYS C 284 -24.167 -14.140 45.790 1.00 24.46 N
ATOM 281 CA CYS C 284 -23.796 -14.945 44.613 1.00 25.87 C
ATOM 282 C CYS C 284 -24.931 -15.944 44.226 1.00 27.85 C
ATOM 283 O CYS C 284 -25.267 -16.029 43.046 1.00 24.37 O
ATOM 284 CB CYS C 284 -22.468 -15.669 44.847 1.00 24.79 C
ATOM 285 SG CYS C 284 -21.074 -14.532 44.912 1.00 24.03 S
ATOM 286 N LYS C 285 -25.536 -16.640 45.203 1.00 28.25 N
ATOM 287 CA LYS C 285 -26.614 -17.590 44.906 1.00 31.31 C
ATOM 288 C LYS C 285 -27.768 -16.930 44.152 1.00 29.57 C
ATOM 289 O LYS C 285 -28.268 -17.465 43.167 1.00 28.67 O
ATOM 290 CB LYS C 285 -27.145 -18.229 46.176 1.00 34.43 C
ATOM 291 CG LYS C 285 -26.268 -19.372 46.616 1.00 38.20 C
ATOM 292 CD LYS C 285 -26.676 -19.907 47.976 1.00 41.61 C
ATOM 293 CE LYS C 285 -25.765 -21.089 48.266 1.00 46.90 C
ATOM 294 NZ LYS C 285 -25.918 -21.605 49.647 1.00 52.01 N
ATOM 295 N GLU C 286 -28.124 -15.733 44.587 1.00 28.74 N
ATOM 296 CA GLU C 286 -29.258 -15.027 44.070 1.00 30.05 C
ATOM 297 C GLU C 286 -29.063 -14.568 42.623 1.00 30.43 C
ATOM 298 O GLU C 286 -30.048 -14.278 41.942 1.00 29.60 O
ATOM 299 CB GLU C 286 -29.633 -13.870 44.982 1.00 30.90 C
ATOM 300 CG GLU C 286 -30.276 -14.398 46.261 1.00 37.92 C
ATOM 301 CD GLU C 286 -30.690 -13.305 47.222 1.00 46.37 C
ATOM 302 OE1 GLU C 286 -30.462 -12.096 46.923 1.00 53.77 O
ATOM 303 OE2 GLU C 286 -31.229 -13.678 48.288 1.00 53.75 O
ATOM 304 N VAL C 287 -27.825 -14.546 42.135 1.00 29.20 N
ATOM 305 CA VAL C 287 -27.610 -14.284 40.689 1.00 28.29 C
ATOM 306 C VAL C 287 -27.181 -15.538 39.948 1.00 30.40 C
ATOM 307 O VAL C 287 -26.611 -15.466 38.840 1.00 32.40 O
ATOM 308 CB VAL C 287 -26.624 -13.122 40.441 1.00 27.45 C
ATOM 309 CG1 VAL C 287 -27.199 -11.816 40.939 1.00 28.48 C
ATOM 310 CG2 VAL C 287 -25.287 -13.383 41.093 1.00 27.90 C
ATOM 311 N GLY C 288 -27.481 -16.687 40.552 1.00 29.44 N
ATOM 312 CA GLY C 288 -27.163 -17.976 39.980 1.00 27.20 C
ATOM 313 C GLY C 288 -25.693 -18.335 39.909 1.00 28.14 C
ATOM 314 O GLY C 288 -25.281 -19.081 39.040 1.00 28.00 O
ATOM 315 N ALA C 289 -24.901 -17.831 40.850 1.00 29.37 N
ATOM 316 CA ALA C 289 -23.463 -18.050 40.848 1.00 26.60 C
ATOM 317 C ALA C 289 -23.064 -18.538 42.199 1.00 27.59 C
ATOM 318 O ALA C 289 -23.921 -18.741 43.071 1.00 26.77 O
ATOM 319 CB ALA C 289 -22.736 -16.751 40.519 1.00 28.07 C
ATOM 320 N GLN C 290 -21.744 -18.666 42.382 1.00 27.93 N
ATOM 321 CA GLN C 290 -21.171 -19.137 43.606 1.00 28.20 C
ATOM 322 C GLN C 290 -19.959 -18.293 44.033 1.00 26.90 C
ATOM 323 O GLN C 290 -19.144 -17.904 43.190 1.00 22.81 O
ATOM 324 CB GLN C 290 -20.720 -20.544 43.352 1.00 29.64 C
ATOM 325 CG GLN C 290 -20.249 -21.285 44.572 1.00 32.18 C
ATOM 326 CD GLN C 290 -19.959 -22.732 44.226 1.00 36.13 C
ATOM 327 OE1 GLN C 290 -19.125 -23.030 43.328 1.00 38.61 O
ATOM 328 NE2 GLN C 290 -20.663 -23.636 44.892 1.00 30.74 N
ATOM 329 N LEU C 291 -19.854 -18.029 45.334 1.00 22.86 N
ATOM 330 CA LEU C 291 -18.697 -17.305 45.899 1.00 22.46 C
ATOM 331 C LEU C 291 -17.446 -18.070 45.468 1.00 20.88 C
ATOM 332 O LEU C 291 -17.352 -19.296 45.599 1.00 18.96 O
ATOM 333 CB LEU C 291 -18.810 -17.147 47.409 1.00 22.35 C
ATOM 334 CG LEU C 291 -17.685 -16.300 48.012 1.00 23.67 C
ATOM 335 CD1 LEU C 291 -17.846 -14.853 47.612 1.00 22.78 C
ATOM 336 CD2 LEU C 291 -17.695 -16.456 49.520 1.00 22.74 C
ATOM 337 N VAL C 292 -16.565 -17.355 44.800 1.00 20.75 N
ATOM 338 CA VAL C 292 -15.615 -17.967 43.911 1.00 21.57 C
ATOM 339 C VAL C 292 -14.777 -19.145 44.469 1.00 24.39 C
ATOM 340 O VAL C 292 -14.096 -19.047 45.506 1.00 23.59 O
ATOM 341 CB VAL C 292 -14.757 -16.910 43.200 1.00 22.22 C
ATOM 342 CG1 VAL C 292 -13.944 -16.096 44.172 1.00 22.41 C
ATOM 343 CG2 VAL C 292 -13.886 -17.577 42.115 1.00 22.08 C
ATOM 344 N VAL C 293 -14.848 -20.245 43.724 1.00 24.27 N
ATOM 345 CA VAL C 293 -14.068 -21.427 43.975 1.00 26.70 C
ATOM 346 C VAL C 293 -12.967 -21.529 42.933 1.00 26.08 C
ATOM 347 O VAL C 293 -13.247 -21.525 41.755 1.00 26.01 O
ATOM 348 CB VAL C 293 -14.956 -22.675 43.917 1.00 26.74 C
ATOM 349 CG1 VAL C 293 -14.129 -23.946 44.102 1.00 28.20 C
ATOM 350 CG2 VAL C 293 -16.040 -22.603 44.996 1.00 28.37 C
ATOM 351 N ILE C 294 -11.723 -21.645 43.376 1.00 25.81 N
ATOM 352 CA ILE C 294 -10.564 -21.596 42.478 1.00 26.46 C
ATOM 353 C ILE C 294 -10.133 -23.040 42.115 1.00 28.25 C
ATOM 354 O ILE C 294 -10.037 -23.914 42.986 1.00 28.14 O
ATOM 355 CB ILE C 294 -9.389 -20.828 43.126 1.00 27.60 C
ATOM 356 CG1 ILE C 294 -9.903 -19.471 43.672 1.00 28.48 C
ATOM 357 CG2 ILE C 294 -8.274 -20.583 42.115 1.00 27.19 C
ATOM 358 CD1 ILE C 294 -8.834 -18.621 44.313 1.00 27.76 C
ATOM 359 N LYS C 295 -9.916 -23.270 40.812 1.00 29.51 N
ATOM 360 CA LYS C 295 -9.578 -24.596 40.264 1.00 29.56 C
ATOM 361 C LYS C 295 -8.202 -24.676 39.601 1.00 33.28 C
ATOM 362 O LYS C 295 -7.692 -25.777 39.410 1.00 37.13 O
ATOM 363 CB LYS C 295 -10.591 -24.997 39.226 1.00 29.52 C
ATOM 364 CG LYS C 295 -12.015 -25.122 39.707 1.00 31.36 C
ATOM 365 CD LYS C 295 -12.238 -26.295 40.633 1.00 30.82 C
ATOM 366 CE LYS C 295 -13.737 -26.437 40.932 1.00 30.28 C
ATOM 367 NZ LYS C 295 -13.965 -27.013 42.264 1.00 30.80 N
ATOM 368 N SER C 296 -7.630 -23.534 39.207 1.00 29.81 N
ATOM 369 CA SER C 296 -6.297 -23.519 38.647 1.00 31.60 C
ATOM 370 C SER C 296 -5.463 -22.312 39.043 1.00 30.30 C
ATOM 371 O SER C 296 -5.934 -21.270 39.583 1.00 26.38 O
ATOM 372 CB SER C 296 -6.368 -23.587 37.112 1.00 31.91 C
ATOM 373 OG SER C 296 -6.962 -22.417 36.582 1.00 29.87 O
ATOM 374 N ALA C 297 -4.186 -22.496 38.787 1.00 32.19 N
ATOM 375 CA ALA C 297 -3.182 -21.510 39.077 1.00 33.54 C
ATOM 376 C ALA C 297 -3.460 -20.196 38.319 1.00 34.95 C
ATOM 377 O ALA C 297 -3.427 -19.101 38.932 1.00 36.91 O
ATOM 378 CB ALA C 297 -1.812 -22.067 38.720 1.00 35.37 C
ATOM 379 N GLU C 298 -3.760 -20.315 37.016 1.00 33.67 N
ATOM 380 CA AGLU C 298 -4.056 -19.172 36.155 0.70 35.01 C
ATOM 381 CA BGLU C 298 -4.035 -19.134 36.186 0.30 33.10 C
ATOM 382 C GLU C 298 -5.284 -18.402 36.669 1.00 32.37 C
ATOM 383 O GLU C 298 -5.360 -17.209 36.548 1.00 27.39 O
ATOM 384 CB AGLU C 298 -4.371 -19.623 34.720 0.70 35.45 C
ATOM 385 CB BGLU C 298 -4.231 -19.479 34.703 0.30 32.67 C
ATOM 386 CG AGLU C 298 -3.270 -20.340 33.945 0.70 40.32 C
ATOM 387 CG BGLU C 298 -2.974 -19.832 33.928 0.30 34.11 C
ATOM 388 CD AGLU C 298 -2.988 -21.781 34.406 0.70 40.49 C
ATOM 389 CD BGLU C 298 -2.107 -18.646 33.564 0.30 34.17 C
ATOM 390 OE1AGLU C 298 -3.901 -22.494 34.870 0.70 36.51 O
ATOM 391 OE1BGLU C 298 -2.314 -17.537 34.105 0.30 35.42 O
ATOM 392 OE2AGLU C 298 -1.810 -22.194 34.312 0.70 42.47 O
ATOM 393 OE2BGLU C 298 -1.195 -18.844 32.729 0.30 35.92 O
ATOM 394 N GLU C 299 -6.278 -19.138 37.156 1.00 31.11 N
ATOM 395 CA GLU C 299 -7.469 -18.524 37.713 1.00 31.36 C
ATOM 396 C GLU C 299 -7.087 -17.807 39.005 1.00 31.66 C
ATOM 397 O GLU C 299 -7.528 -16.706 39.223 1.00 30.97 O
ATOM 398 CB GLU C 299 -8.537 -19.559 38.011 1.00 31.77 C
ATOM 399 CG GLU C 299 -9.961 -19.030 38.177 1.00 32.14 C
ATOM 400 CD GLU C 299 -10.920 -20.061 38.766 1.00 32.16 C
ATOM 401 OE1 GLU C 299 -12.068 -19.685 39.093 1.00 33.45 O
ATOM 402 OE2 GLU C 299 -10.557 -21.252 38.909 1.00 31.79 O
ATOM 403 N GLN C 300 -6.283 -18.459 39.855 1.00 30.37 N
ATOM 404 CA GLN C 300 -5.713 -17.837 41.056 1.00 26.59 C
ATOM 405 C GLN C 300 -5.007 -16.559 40.708 1.00 25.93 C
ATOM 406 O GLN C 300 -5.191 -15.568 41.401 1.00 22.16 O
ATOM 407 CB GLN C 300 -4.762 -18.790 41.794 1.00 24.95 C
ATOM 408 CG GLN C 300 -3.707 -18.160 42.700 1.00 24.83 C
ATOM 409 CD GLN C 300 -4.271 -17.249 43.802 1.00 27.61 C
ATOM 410 OE1 GLN C 300 -5.455 -17.330 44.176 1.00 28.43 O
ATOM 411 NE2 GLN C 300 -3.434 -16.322 44.273 1.00 25.01 N
ATOM 412 N ASN C 301 -4.210 -16.578 39.638 1.00 23.71 N
ATOM 413 CA ASN C 301 -3.475 -15.374 39.219 1.00 25.47 C
ATOM 414 C ASN C 301 -4.401 -14.247 38.749 1.00 23.96 C
ATOM 415 O ASN C 301 -4.149 -13.106 38.994 1.00 25.97 O
ATOM 416 CB ASN C 301 -2.423 -15.684 38.112 1.00 27.88 C
ATOM 417 CG ASN C 301 -1.278 -16.575 38.605 1.00 32.46 C
ATOM 418 OD1 ASN C 301 -1.088 -16.815 39.809 1.00 34.45 O
ATOM 419 ND2 ASN C 301 -0.516 -17.094 37.651 1.00 36.91 N
ATOM 420 N PHE C 302 -5.441 -14.567 38.015 1.00 25.16 N
ATOM 421 CA PHE C 302 -6.358 -13.574 37.564 1.00 25.50 C
ATOM 422 C PHE C 302 -7.107 -12.939 38.757 1.00 25.93 C
ATOM 423 O PHE C 302 -7.290 -11.704 38.833 1.00 25.49 O
ATOM 424 CB PHE C 302 -7.314 -14.272 36.607 1.00 27.92 C
ATOM 425 CG PHE C 302 -8.569 -13.528 36.344 1.00 28.49 C
ATOM 426 CD1 PHE C 302 -8.554 -12.367 35.593 1.00 31.47 C
ATOM 427 CD2 PHE C 302 -9.764 -14.012 36.813 1.00 30.84 C
ATOM 428 CE1 PHE C 302 -9.715 -11.693 35.319 1.00 29.80 C
ATOM 429 CE2 PHE C 302 -10.940 -13.341 36.538 1.00 32.07 C
ATOM 430 CZ PHE C 302 -10.902 -12.175 35.819 1.00 32.58 C
ATOM 431 N LEU C 303 -7.548 -13.787 39.672 1.00 22.13 N
ATOM 432 CA LEU C 303 -8.294 -13.339 40.837 1.00 23.53 C
ATOM 433 C LEU C 303 -7.477 -12.520 41.847 1.00 25.63 C
ATOM 434 O LEU C 303 -7.919 -11.444 42.296 1.00 24.52 O
ATOM 435 CB LEU C 303 -8.918 -14.549 41.522 1.00 23.34 C
ATOM 436 CG LEU C 303 -9.907 -15.353 40.696 1.00 22.21 C
ATOM 437 CD1 LEU C 303 -10.220 -16.612 41.456 1.00 24.78 C
ATOM 438 CD2 LEU C 303 -11.171 -14.551 40.397 1.00 23.66 C
ATOM 439 N GLN C 304 -6.278 -13.014 42.176 1.00 24.95 N
ATOM 440 CA GLN C 304 -5.383 -12.333 43.087 1.00 24.37 C
ATOM 441 C GLN C 304 -5.073 -10.923 42.608 1.00 27.55 C
ATOM 442 O GLN C 304 -4.992 -9.966 43.421 1.00 27.66 O
ATOM 443 CB GLN C 304 -4.080 -13.140 43.260 1.00 25.04 C
ATOM 444 CG GLN C 304 -3.160 -12.707 44.403 1.00 22.44 C
ATOM 445 CD GLN C 304 -3.795 -12.950 45.732 1.00 23.68 C
ATOM 446 OE1 GLN C 304 -4.136 -14.121 46.060 1.00 23.33 O
ATOM 447 NE2 GLN C 304 -3.980 -11.867 46.526 1.00 21.12 N
ATOM 448 N LEU C 305 -4.896 -10.793 41.297 1.00 27.17 N
ATOM 449 CA LEU C 305 -4.578 -9.533 40.695 1.00 28.17 C
ATOM 450 C LEU C 305 -5.665 -8.488 40.952 1.00 27.71 C
ATOM 451 O LEU C 305 -5.355 -7.338 41.100 1.00 31.43 O
ATOM 452 CB LEU C 305 -4.364 -9.696 39.174 1.00 29.89 C
ATOM 453 CG LEU C 305 -4.012 -8.382 38.480 1.00 33.98 C
ATOM 454 CD1 LEU C 305 -2.561 -7.981 38.757 1.00 33.34 C
ATOM 455 CD2 LEU C 305 -4.294 -8.434 36.981 1.00 36.97 C
ATOM 456 N GLN C 306 -6.933 -8.883 40.993 1.00 27.26 N
ATOM 457 CA GLN C 306 -8.006 -7.907 41.172 1.00 29.74 C
ATOM 458 C GLN C 306 -7.825 -7.251 42.523 1.00 29.66 C
ATOM 459 O GLN C 306 -8.025 -6.048 42.650 1.00 35.50 O
ATOM 460 CB GLN C 306 -9.416 -8.523 41.076 1.00 28.84 C
ATOM 461 CG GLN C 306 -9.628 -9.480 39.925 1.00 30.00 C
ATOM 462 CD GLN C 306 -9.328 -8.855 38.584 1.00 32.36 C
ATOM 463 OE1 GLN C 306 -9.880 -7.823 38.256 1.00 35.66 O
ATOM 464 NE2 GLN C 306 -8.462 -9.479 37.806 1.00 33.29 N
ATOM 465 N SER C 307 -7.386 -8.016 43.515 1.00 27.26 N
ATOM 466 CA SER C 307 -7.156 -7.448 44.833 1.00 28.02 C
ATOM 467 C SER C 307 -5.776 -6.807 45.021 1.00 28.51 C
ATOM 468 O SER C 307 -5.661 -5.799 45.733 1.00 28.71 O
ATOM 469 CB SER C 307 -7.397 -8.524 45.919 1.00 29.58 C
ATOM 470 OG SER C 307 -8.767 -8.922 45.871 1.00 29.91 O
ATOM 471 N SER C 308 -4.730 -7.383 44.444 1.00 27.07 N
ATOM 472 CA SER C 308 -3.387 -6.879 44.726 1.00 32.94 C
ATOM 473 C SER C 308 -3.237 -5.484 44.100 1.00 32.71 C
ATOM 474 O SER C 308 -2.652 -4.584 44.695 1.00 37.89 O
ATOM 475 CB SER C 308 -2.290 -7.793 44.184 1.00 31.34 C
ATOM 476 OG SER C 308 -2.408 -7.904 42.784 1.00 35.40 O
ATOM 477 N ARG C 309 -3.787 -5.346 42.915 1.00 31.21 N
ATOM 478 CA ARG C 309 -3.747 -4.110 42.157 1.00 37.26 C
ATOM 479 C ARG C 309 -4.688 -3.041 42.718 1.00 36.32 C
ATOM 480 O ARG C 309 -4.359 -1.878 42.712 1.00 33.15 O
ATOM 481 CB ARG C 309 -4.153 -4.426 40.746 1.00 39.48 C
ATOM 482 CG ARG C 309 -4.123 -3.280 39.784 1.00 44.71 C
ATOM 483 CD ARG C 309 -4.467 -3.817 38.402 1.00 49.17 C
ATOM 484 NE ARG C 309 -5.820 -4.375 38.345 1.00 51.20 N
ATOM 485 CZ ARG C 309 -6.305 -5.096 37.339 1.00 54.57 C
ATOM 486 NH1 ARG C 309 -5.552 -5.368 36.266 1.00 55.05 N
ATOM 487 NH2 ARG C 309 -7.559 -5.547 37.403 1.00 55.87 N
ATOM 488 N SER C 310 -5.869 -3.447 43.172 1.00 34.57 N
ATOM 489 CA SER C 310 -6.806 -2.515 43.759 1.00 33.77 C
ATOM 490 C SER C 310 -6.498 -2.164 45.221 1.00 34.75 C
ATOM 491 O SER C 310 -7.070 -1.215 45.755 1.00 33.43 O
ATOM 492 CB SER C 310 -8.221 -3.080 43.647 1.00 32.87 C
ATOM 493 OG SER C 310 -8.376 -4.172 44.521 1.00 30.14 O
ATOM 494 N ASN C 311 -5.605 -2.925 45.861 1.00 34.63 N
ATOM 495 CA ASN C 311 -5.348 -2.810 47.306 1.00 35.96 C
ATOM 496 C ASN C 311 -6.580 -3.101 48.200 1.00 34.32 C
ATOM 497 O ASN C 311 -6.613 -2.665 49.369 1.00 36.80 O
ATOM 498 CB ASN C 311 -4.784 -1.416 47.645 1.00 36.07 C
ATOM 499 CG ASN C 311 -3.605 -1.063 46.787 1.00 41.05 C
ATOM 500 OD1 ASN C 311 -2.558 -1.709 46.890 1.00 43.89 O
ATOM 501 ND2 ASN C 311 -3.770 -0.057 45.890 1.00 36.58 N
ATOM 502 N ARG C 312 -7.563 -3.812 47.651 1.00 29.38 N
ATOM 503 CA ARG C 312 -8.820 -4.142 48.306 1.00 29.77 C
ATOM 504 C ARG C 312 -8.819 -5.593 48.833 1.00 28.78 C
ATOM 505 O ARG C 312 -8.152 -6.425 48.262 1.00 30.09 O
ATOM 506 CB ARG C 312 -9.940 -4.076 47.265 1.00 31.82 C
ATOM 507 CG ARG C 312 -10.050 -2.759 46.540 1.00 36.46 C
ATOM 508 CD ARG C 312 -10.932 -1.766 47.233 1.00 36.51 C
ATOM 509 NE ARG C 312 -10.964 -0.424 46.599 1.00 36.17 N
ATOM 510 CZ ARG C 312 -11.099 0.710 47.294 1.00 35.94 C
ATOM 511 NH1 ARG C 312 -11.155 1.894 46.655 1.00 34.67 N
ATOM 512 NH2 ARG C 312 -11.170 0.660 48.649 1.00 32.29 N
ATOM 513 N PHE C 313 -9.631 -5.884 49.848 1.00 24.24 N
ATOM 514 CA PHE C 313 -9.714 -7.184 50.467 1.00 23.49 C
ATOM 515 C PHE C 313 -10.987 -7.833 49.980 1.00 24.76 C
ATOM 516 O PHE C 313 -12.073 -7.224 50.014 1.00 20.00 O
ATOM 517 CB PHE C 313 -9.772 -7.053 51.981 1.00 27.42 C
ATOM 518 CG PHE C 313 -8.566 -6.390 52.594 1.00 27.78 C
ATOM 519 CD1 PHE C 313 -7.278 -6.724 52.201 1.00 28.13 C
ATOM 520 CD2 PHE C 313 -8.725 -5.465 53.625 1.00 26.26 C
ATOM 521 CE1 PHE C 313 -6.165 -6.092 52.797 1.00 28.30 C
ATOM 522 CE2 PHE C 313 -7.631 -4.904 54.255 1.00 27.28 C
ATOM 523 CZ PHE C 313 -6.353 -5.197 53.833 1.00 26.89 C
ATOM 524 N THR C 314 -10.849 -9.068 49.497 1.00 23.92 N
ATOM 525 CA THR C 314 -11.911 -9.714 48.783 1.00 23.59 C
ATOM 526 C THR C 314 -12.131 -11.182 49.220 1.00 23.36 C
ATOM 527 O THR C 314 -11.200 -11.997 49.280 1.00 20.54 O
ATOM 528 CB THR C 314 -11.583 -9.660 47.257 1.00 24.88 C
ATOM 529 OG1 THR C 314 -11.315 -8.290 46.853 1.00 25.34 O
ATOM 530 CG2 THR C 314 -12.724 -10.163 46.487 1.00 22.35 C
ATOM 531 N TRP C 315 -13.377 -11.564 49.442 1.00 23.92 N
ATOM 532 CA TRP C 315 -13.624 -12.935 49.897 1.00 24.85 C
ATOM 533 C TRP C 315 -13.577 -13.914 48.730 1.00 24.57 C
ATOM 534 O TRP C 315 -13.930 -13.557 47.613 1.00 22.34 O
ATOM 535 CB TRP C 315 -15.003 -13.124 50.503 1.00 25.76 C
ATOM 536 CG TRP C 315 -15.345 -12.436 51.799 1.00 24.55 C
ATOM 537 CD1 TRP C 315 -16.395 -11.578 52.009 1.00 26.08 C
ATOM 538 CD2 TRP C 315 -14.729 -12.617 53.062 1.00 25.28 C
ATOM 539 NE1 TRP C 315 -16.473 -11.221 53.319 1.00 23.58 N
ATOM 540 CE2 TRP C 315 -15.440 -11.833 53.986 1.00 24.25 C
ATOM 541 CE3 TRP C 315 -13.648 -13.371 53.506 1.00 24.07 C
ATOM 542 CZ2 TRP C 315 -15.103 -11.789 55.298 1.00 24.40 C
ATOM 543 CZ3 TRP C 315 -13.307 -13.312 54.792 1.00 28.34 C
ATOM 544 CH2 TRP C 315 -14.024 -12.537 55.701 1.00 25.87 C
ATOM 545 N MET C 316 -13.222 -15.162 49.045 1.00 22.33 N
ATOM 546 CA MET C 316 -13.363 -16.262 48.119 1.00 23.43 C
ATOM 547 C MET C 316 -14.220 -17.293 48.849 1.00 21.92 C
ATOM 548 O MET C 316 -14.435 -17.139 50.073 1.00 20.78 O
ATOM 549 CB MET C 316 -12.001 -16.776 47.715 1.00 23.80 C
ATOM 550 CG MET C 316 -11.246 -17.426 48.827 1.00 26.58 C
ATOM 551 SD MET C 316 -9.617 -18.025 48.373 1.00 26.92 S
ATOM 552 CE MET C 316 -8.662 -16.510 48.478 1.00 27.93 C
ATOM 553 N GLY C 317 -14.731 -18.291 48.115 1.00 21.35 N
ATOM 554 CA GLY C 317 -15.592 -19.351 48.685 1.00 22.95 C
ATOM 555 C GLY C 317 -14.788 -20.496 49.339 1.00 23.17 C
ATOM 556 O GLY C 317 -14.860 -21.665 48.882 1.00 27.26 O
ATOM 557 N LEU C 318 -13.969 -20.141 50.333 1.00 23.74 N
ATOM 558 CA LEU C 318 -13.063 -21.057 51.052 1.00 24.37 C
ATOM 559 C LEU C 318 -13.146 -20.744 52.535 1.00 24.82 C
ATOM 560 O LEU C 318 -12.984 -19.604 52.907 1.00 27.13 O
ATOM 561 CB LEU C 318 -11.661 -20.843 50.584 1.00 25.39 C
ATOM 562 CG LEU C 318 -10.571 -21.736 51.167 1.00 25.68 C
ATOM 563 CD1 LEU C 318 -10.720 -23.187 50.778 1.00 26.29 C
ATOM 564 CD2 LEU C 318 -9.217 -21.232 50.734 1.00 26.55 C
ATOM 565 N SER C 319 -13.451 -21.754 53.352 1.00 23.61 N
ATOM 566 CA SER C 319 -13.536 -21.634 54.772 1.00 26.21 C
ATOM 567 C SER C 319 -13.031 -22.891 55.526 1.00 28.54 C
ATOM 568 O SER C 319 -12.872 -23.987 54.940 1.00 29.57 O
ATOM 569 CB SER C 319 -14.967 -21.355 55.170 1.00 26.63 C
ATOM 570 OG SER C 319 -15.675 -22.570 55.212 1.00 28.31 O
ATOM 571 N ASP C 320 -12.756 -22.723 56.823 1.00 28.11 N
ATOM 572 CA ASP C 320 -12.512 -23.864 57.747 1.00 27.60 C
ATOM 573 C ASP C 320 -13.456 -23.796 58.922 1.00 30.71 C
ATOM 574 O ASP C 320 -13.110 -24.209 60.039 1.00 28.79 O
ATOM 575 CB ASP C 320 -11.063 -23.956 58.222 1.00 27.68 C
ATOM 576 CG ASP C 320 -10.653 -22.864 59.288 1.00 29.41 C
ATOM 577 OD1 ASP C 320 -11.376 -21.844 59.514 1.00 29.73 O
ATOM 578 OD2 ASP C 320 -9.541 -23.023 59.885 1.00 27.72 O
ATOM 579 N LEU C 321 -14.640 -23.257 58.658 1.00 28.09 N
ATOM 580 CA LEU C 321 -15.726 -23.229 59.620 1.00 29.60 C
ATOM 581 C LEU C 321 -16.134 -24.593 60.140 1.00 32.58 C
ATOM 582 O LEU C 321 -16.485 -24.711 61.316 1.00 34.65 O
ATOM 583 CB LEU C 321 -16.992 -22.625 58.982 1.00 29.76 C
ATOM 584 CG LEU C 321 -16.967 -21.093 58.822 1.00 31.85 C
ATOM 585 CD1 LEU C 321 -17.996 -20.610 57.798 1.00 31.56 C
ATOM 586 CD2 LEU C 321 -17.165 -20.466 60.188 1.00 32.45 C
ATOM 587 N ASN C 322 -16.155 -25.601 59.267 1.00 33.20 N
ATOM 588 CA AASN C 322 -16.649 -26.910 59.661 0.70 37.44 C
ATOM 589 CA BASN C 322 -16.647 -26.929 59.641 0.30 34.98 C
ATOM 590 C ASN C 322 -15.636 -27.661 60.498 1.00 37.55 C
ATOM 591 O ASN C 322 -15.993 -28.265 61.501 1.00 37.91 O
ATOM 592 CB AASN C 322 -17.019 -27.721 58.442 0.70 41.34 C
ATOM 593 CB BASN C 322 -16.952 -27.796 58.423 0.30 35.28 C
ATOM 594 CG AASN C 322 -18.262 -27.207 57.775 0.70 41.78 C
ATOM 595 CG BASN C 322 -17.313 -29.225 58.814 0.30 34.37 C
ATOM 596 OD1AASN C 322 -19.087 -26.530 58.404 0.70 45.68 O
ATOM 597 OD1BASN C 322 -18.111 -29.434 59.725 0.30 33.66 O
ATOM 598 ND2AASN C 322 -18.406 -27.512 56.495 0.70 42.59 N
ATOM 599 ND2BASN C 322 -16.708 -30.208 58.144 0.30 32.12 N
ATOM 600 N GLN C 323 -14.379 -27.601 60.088 1.00 34.32 N
ATOM 601 CA GLN C 323 -13.329 -28.313 60.785 1.00 34.45 C
ATOM 602 C GLN C 323 -12.094 -27.412 60.846 1.00 32.09 C
ATOM 603 O GLN C 323 -11.347 -27.235 59.836 1.00 32.08 O
ATOM 604 CB GLN C 323 -13.037 -29.621 60.059 1.00 31.93 C
ATOM 605 CG GLN C 323 -11.846 -30.392 60.601 1.00 34.69 C
ATOM 606 CD GLN C 323 -12.168 -31.144 61.882 1.00 40.35 C
ATOM 607 OE1 GLN C 323 -13.337 -31.362 62.217 1.00 46.47 O
ATOM 608 NE2 GLN C 323 -11.126 -31.562 62.600 1.00 42.33 N
ATOM 609 N GLU C 324 -11.895 -26.841 62.020 1.00 30.19 N
ATOM 610 CA GLU C 324 -10.814 -25.912 62.255 1.00 31.42 C
ATOM 611 C GLU C 324 -9.534 -26.458 61.696 1.00 30.28 C
ATOM 612 O GLU C 324 -9.182 -27.578 61.991 1.00 31.06 O
ATOM 613 CB GLU C 324 -10.658 -25.558 63.748 1.00 31.52 C
ATOM 614 CG GLU C 324 -9.465 -24.629 64.052 1.00 30.70 C
ATOM 615 CD GLU C 324 -9.477 -23.340 63.214 1.00 30.84 C
ATOM 616 OE1 GLU C 324 -10.576 -22.758 62.974 1.00 29.82 O
ATOM 617 OE2 GLU C 324 -8.378 -22.916 62.803 1.00 29.47 O
ATOM 618 N GLY C 325 -8.894 -25.694 60.806 1.00 30.15 N
ATOM 619 CA GLY C 325 -7.605 -26.090 60.197 1.00 29.79 C
ATOM 620 C GLY C 325 -7.728 -26.858 58.899 1.00 32.45 C
ATOM 621 O GLY C 325 -6.712 -27.061 58.178 1.00 32.02 O
ATOM 622 N THR C 326 -8.966 -27.276 58.568 1.00 31.50 N
ATOM 623 CA THR C 326 -9.219 -27.896 57.283 1.00 28.06 C
ATOM 624 C THR C 326 -10.045 -26.990 56.346 1.00 29.69 C
ATOM 625 O THR C 326 -11.250 -26.792 56.571 1.00 26.60 O
ATOM 626 CB THR C 326 -9.844 -29.294 57.440 1.00 29.84 C
ATOM 627 OG1 THR C 326 -8.867 -30.146 58.044 1.00 32.83 O
ATOM 628 CG2 THR C 326 -10.200 -29.881 56.080 1.00 27.69 C
ATOM 629 N TRP C 327 -9.386 -26.504 55.270 1.00 27.46 N
ATOM 630 CA TRP C 327 -10.009 -25.571 54.338 1.00 29.87 C
ATOM 631 C TRP C 327 -10.763 -26.261 53.220 1.00 28.64 C
ATOM 632 O TRP C 327 -10.262 -27.148 52.517 1.00 30.61 O
ATOM 633 CB TRP C 327 -8.993 -24.568 53.813 1.00 29.99 C
ATOM 634 CG TRP C 327 -8.522 -23.741 54.926 1.00 31.85 C
ATOM 635 CD1 TRP C 327 -7.531 -24.056 55.825 1.00 32.21 C
ATOM 636 CD2 TRP C 327 -9.062 -22.485 55.345 1.00 30.53 C
ATOM 637 NE1 TRP C 327 -7.413 -23.061 56.759 1.00 29.73 N
ATOM 638 CE2 TRP C 327 -8.329 -22.083 56.490 1.00 30.08 C
ATOM 639 CE3 TRP C 327 -10.087 -21.649 54.859 1.00 28.52 C
ATOM 640 CZ2 TRP C 327 -8.578 -20.882 57.157 1.00 28.98 C
ATOM 641 CZ3 TRP C 327 -10.323 -20.438 55.517 1.00 30.47 C
ATOM 642 CH2 TRP C 327 -9.573 -20.076 56.666 1.00 31.34 C
ATOM 643 N GLN C 328 -11.985 -25.806 53.055 1.00 29.24 N
ATOM 644 CA GLN C 328 -12.936 -26.392 52.146 1.00 29.88 C
ATOM 645 C GLN C 328 -13.577 -25.330 51.292 1.00 26.63 C
ATOM 646 O GLN C 328 -14.053 -24.323 51.791 1.00 26.36 O
ATOM 647 CB GLN C 328 -14.028 -27.089 52.949 1.00 36.09 C
ATOM 648 CG GLN C 328 -14.887 -28.005 52.099 1.00 43.50 C
ATOM 649 CD GLN C 328 -15.733 -28.977 52.928 1.00 50.91 C
ATOM 650 OE1 GLN C 328 -16.043 -30.078 52.467 1.00 57.48 O
ATOM 651 NE2 GLN C 328 -16.107 -28.576 54.148 1.00 56.30 N
ATOM 652 N TRP C 329 -13.626 -25.583 49.988 1.00 26.72 N
ATOM 653 CA TRP C 329 -14.296 -24.715 49.067 1.00 24.07 C
ATOM 654 C TRP C 329 -15.771 -24.938 49.257 1.00 24.23 C
ATOM 655 O TRP C 329 -16.177 -26.009 49.701 1.00 24.39 O
ATOM 656 CB TRP C 329 -13.889 -25.010 47.628 1.00 25.15 C
ATOM 657 CG TRP C 329 -12.462 -24.770 47.311 1.00 23.63 C
ATOM 658 CD1 TRP C 329 -11.514 -25.691 47.210 1.00 24.31 C
ATOM 659 CD2 TRP C 329 -11.817 -23.494 47.084 1.00 24.81 C
ATOM 660 NE1 TRP C 329 -10.297 -25.108 46.910 1.00 25.80 N
ATOM 661 CE2 TRP C 329 -10.465 -23.754 46.824 1.00 23.28 C
ATOM 662 CE3 TRP C 329 -12.256 -22.162 47.107 1.00 25.19 C
ATOM 663 CZ2 TRP C 329 -9.542 -22.747 46.579 1.00 23.64 C
ATOM 664 CZ3 TRP C 329 -11.327 -21.150 46.861 1.00 23.77 C
ATOM 665 CH2 TRP C 329 -9.995 -21.448 46.600 1.00 23.95 C
ATOM 666 N VAL C 330 -16.574 -23.935 48.920 1.00 25.07 N
ATOM 667 CA VAL C 330 -18.039 -23.982 49.115 1.00 26.78 C
ATOM 668 C VAL C 330 -18.734 -24.978 48.217 1.00 28.03 C
ATOM 669 O VAL C 330 -19.860 -25.331 48.488 1.00 27.67 O
ATOM 670 CB VAL C 330 -18.742 -22.590 48.937 1.00 28.02 C
ATOM 671 CG1 VAL C 330 -18.348 -21.669 50.062 1.00 28.29 C
ATOM 672 CG2 VAL C 330 -18.375 -21.896 47.647 1.00 28.64 C
ATOM 673 N ASP C 331 -18.087 -25.391 47.121 1.00 29.12 N
ATOM 674 CA ASP C 331 -18.645 -26.428 46.280 1.00 29.82 C
ATOM 675 C ASP C 331 -18.334 -27.800 46.853 1.00 32.29 C
ATOM 676 O ASP C 331 -18.602 -28.790 46.190 1.00 34.16 O
ATOM 677 CB ASP C 331 -18.108 -26.369 44.837 1.00 28.81 C
ATOM 678 CG ASP C 331 -16.671 -26.743 44.753 1.00 29.06 C
ATOM 679 OD1 ASP C 331 -16.068 -26.898 45.818 1.00 30.05 O
ATOM 680 OD2 ASP C 331 -16.108 -26.851 43.649 1.00 34.76 O
ATOM 681 N GLY C 332 -17.711 -27.867 48.020 1.00 30.41 N
ATOM 682 CA GLY C 332 -17.430 -29.157 48.675 1.00 35.00 C
ATOM 683 C GLY C 332 -16.004 -29.693 48.444 1.00 35.09 C
ATOM 684 O GLY C 332 -15.544 -30.584 49.156 1.00 37.93 O
ATOM 685 N SER C 333 -15.301 -29.135 47.465 1.00 31.43 N
ATOM 686 CA SER C 333 -14.024 -29.662 47.055 1.00 31.48 C
ATOM 687 C SER C 333 -13.013 -29.237 48.104 1.00 32.91 C
ATOM 688 O SER C 333 -13.227 -28.246 48.821 1.00 33.00 O
ATOM 689 CB SER C 333 -13.629 -29.165 45.641 1.00 32.27 C
ATOM 690 OG SER C 333 -13.560 -27.743 45.582 1.00 36.38 O
ATOM 691 N PRO C 334 -11.919 -29.992 48.209 1.00 33.63 N
ATOM 692 CA PRO C 334 -10.908 -29.784 49.224 1.00 32.01 C
ATOM 693 C PRO C 334 -9.885 -28.781 48.763 1.00 33.49 C
ATOM 694 O PRO C 334 -9.677 -28.640 47.568 1.00 33.32 O
ATOM 695 CB PRO C 334 -10.252 -31.175 49.332 1.00 34.12 C
ATOM 696 CG PRO C 334 -10.376 -31.762 47.953 1.00 33.29 C
ATOM 697 CD PRO C 334 -11.676 -31.232 47.423 1.00 34.73 C
ATOM 698 N LEU C 335 -9.222 -28.107 49.695 1.00 34.10 N
ATOM 699 CA LEU C 335 -8.097 -27.303 49.313 1.00 33.04 C
ATOM 700 C LEU C 335 -6.917 -28.225 49.058 1.00 36.36 C
ATOM 701 O LEU C 335 -6.380 -28.822 49.993 1.00 38.42 O
ATOM 702 CB LEU C 335 -7.741 -26.309 50.398 1.00 34.14 C
ATOM 703 CG LEU C 335 -6.539 -25.406 50.035 1.00 33.91 C
ATOM 704 CD1 LEU C 335 -6.811 -24.475 48.849 1.00 31.59 C
ATOM 705 CD2 LEU C 335 -6.191 -24.605 51.272 1.00 33.61 C
ATOM 706 N LEU C 336 -6.476 -28.290 47.808 1.00 35.66 N
ATOM 707 CA LEU C 336 -5.397 -29.185 47.405 1.00 33.63 C
ATOM 708 C LEU C 336 -4.049 -28.688 47.922 1.00 35.03 C
ATOM 709 O LEU C 336 -3.841 -27.470 48.055 1.00 36.26 O
ATOM 710 CB LEU C 336 -5.355 -29.340 45.882 1.00 33.24 C
ATOM 711 CG LEU C 336 -6.598 -29.996 45.250 1.00 37.38 C
ATOM 712 CD1 LEU C 336 -6.496 -29.945 43.723 1.00 38.30 C
ATOM 713 CD2 LEU C 336 -6.805 -31.430 45.699 1.00 36.97 C
ATOM 714 N PRO C 337 -3.115 -29.620 48.200 1.00 35.94 N
ATOM 715 CA PRO C 337 -1.790 -29.227 48.713 1.00 37.73 C
ATOM 716 C PRO C 337 -1.037 -28.222 47.845 1.00 34.22 C
ATOM 717 O PRO C 337 -0.326 -27.381 48.383 1.00 33.04 O
ATOM 718 CB PRO C 337 -1.024 -30.563 48.771 1.00 40.37 C
ATOM 719 CG PRO C 337 -2.110 -31.603 48.968 1.00 39.13 C
ATOM 720 CD PRO C 337 -3.248 -31.092 48.120 1.00 39.53 C
ATOM 721 N SER C 338 -1.209 -28.302 46.528 1.00 34.87 N
ATOM 722 CA SER C 338 -0.563 -27.381 45.570 1.00 36.72 C
ATOM 723 C SER C 338 -1.050 -25.927 45.623 1.00 36.27 C
ATOM 724 O SER C 338 -0.473 -25.070 44.938 1.00 35.37 O
ATOM 725 CB SER C 338 -0.824 -27.882 44.154 1.00 38.58 C
ATOM 726 OG SER C 338 -2.225 -28.065 43.999 1.00 41.56 O
ATOM 727 N PHE C 339 -2.141 -25.685 46.368 1.00 34.54 N
ATOM 728 CA PHE C 339 -2.728 -24.340 46.583 1.00 34.79 C
ATOM 729 C PHE C 339 -2.291 -23.743 47.899 1.00 35.74 C
ATOM 730 O PHE C 339 -2.580 -22.587 48.160 1.00 34.68 O
ATOM 731 CB PHE C 339 -4.272 -24.381 46.522 1.00 34.41 C
ATOM 732 CG PHE C 339 -4.794 -24.548 45.129 1.00 38.40 C
ATOM 733 CD1 PHE C 339 -4.604 -25.731 44.448 1.00 40.18 C
ATOM 734 CD2 PHE C 339 -5.400 -23.491 44.458 1.00 43.31 C
ATOM 735 CE1 PHE C 339 -5.018 -25.883 43.131 1.00 41.33 C
ATOM 736 CE2 PHE C 339 -5.824 -23.637 43.136 1.00 45.82 C
ATOM 737 CZ PHE C 339 -5.628 -24.838 42.469 1.00 40.69 C
ATOM 738 N LYS C 340 -1.575 -24.506 48.727 1.00 33.98 N
ATOM 739 CA LYS C 340 -1.211 -24.006 50.041 1.00 35.97 C
ATOM 740 C LYS C 340 -0.156 -22.905 50.005 1.00 32.50 C
ATOM 741 O LYS C 340 -0.111 -22.040 50.874 1.00 31.99 O
ATOM 742 CB LYS C 340 -0.879 -25.158 50.943 1.00 39.77 C
ATOM 743 CG LYS C 340 -2.180 -25.808 51.322 1.00 44.24 C
ATOM 744 CD LYS C 340 -2.061 -27.115 52.077 1.00 47.59 C
ATOM 745 CE LYS C 340 -3.373 -27.372 52.807 1.00 51.09 C
ATOM 746 NZ LYS C 340 -3.910 -28.726 52.520 1.00 56.90 N
ATOM 747 N GLN C 341 0.592 -22.885 48.919 1.00 28.65 N
ATOM 748 CA GLN C 341 1.531 -21.842 48.597 1.00 30.11 C
ATOM 749 C GLN C 341 0.924 -20.451 48.434 1.00 29.89 C
ATOM 750 O GLN C 341 1.639 -19.464 48.489 1.00 28.88 O
ATOM 751 CB GLN C 341 2.242 -22.189 47.285 1.00 31.98 C
ATOM 752 CG GLN C 341 1.350 -22.219 46.062 1.00 32.34 C
ATOM 753 CD GLN C 341 2.112 -22.590 44.801 1.00 37.37 C
ATOM 754 OE1 GLN C 341 2.883 -21.800 44.280 1.00 36.65 O
ATOM 755 NE2 GLN C 341 1.862 -23.787 44.280 1.00 37.17 N
ATOM 756 N TYR C 342 -0.381 -20.352 48.205 1.00 27.10 N
ATOM 757 CA TYR C 342 -0.944 -19.045 47.932 1.00 29.03 C
ATOM 758 C TYR C 342 -1.239 -18.257 49.214 1.00 27.26 C
ATOM 759 O TYR C 342 -1.503 -17.059 49.145 1.00 29.50 O
ATOM 760 CB TYR C 342 -2.220 -19.155 47.011 1.00 27.93 C
ATOM 761 CG TYR C 342 -1.908 -19.697 45.635 1.00 26.40 C
ATOM 762 CD1 TYR C 342 -0.948 -19.116 44.860 1.00 26.60 C
ATOM 763 CD2 TYR C 342 -2.551 -20.838 45.142 1.00 28.76 C
ATOM 764 CE1 TYR C 342 -0.628 -19.621 43.618 1.00 28.13 C
ATOM 765 CE2 TYR C 342 -2.235 -21.353 43.889 1.00 27.47 C
ATOM 766 CZ TYR C 342 -1.278 -20.721 43.136 1.00 26.97 C
ATOM 767 OH TYR C 342 -0.965 -21.172 41.893 1.00 29.91 O
ATOM 768 N TRP C 343 -1.238 -18.923 50.358 1.00 29.89 N
ATOM 769 CA TRP C 343 -1.420 -18.246 51.646 1.00 30.48 C
ATOM 770 C TRP C 343 -0.262 -17.309 51.826 1.00 32.32 C
ATOM 771 O TRP C 343 0.849 -17.733 51.545 1.00 27.49 O
ATOM 772 CB TRP C 343 -1.343 -19.225 52.810 1.00 28.72 C
ATOM 773 CG TRP C 343 -2.504 -20.173 52.966 1.00 31.52 C
ATOM 774 CD1 TRP C 343 -2.476 -21.546 52.844 1.00 29.60 C
ATOM 775 CD2 TRP C 343 -3.842 -19.836 53.344 1.00 29.88 C
ATOM 776 NE1 TRP C 343 -3.717 -22.073 53.133 1.00 28.33 N
ATOM 777 CE2 TRP C 343 -4.568 -21.053 53.450 1.00 29.46 C
ATOM 778 CE3 TRP C 343 -4.494 -18.627 53.649 1.00 27.35 C
ATOM 779 CZ2 TRP C 343 -5.932 -21.091 53.793 1.00 30.72 C
ATOM 780 CZ3 TRP C 343 -5.854 -18.672 53.996 1.00 29.85 C
ATOM 781 CH2 TRP C 343 -6.567 -19.901 54.032 1.00 27.62 C
ATOM 782 N ASN C 344 -0.519 -16.082 52.296 1.00 29.31 N
ATOM 783 CA ASN C 344 0.540 -15.155 52.744 1.00 32.16 C
ATOM 784 C ASN C 344 1.412 -15.794 53.816 1.00 30.54 C
ATOM 785 O ASN C 344 0.932 -16.644 54.603 1.00 30.57 O
ATOM 786 CB ASN C 344 -0.066 -13.865 53.360 1.00 32.86 C
ATOM 787 CG ASN C 344 -0.866 -13.039 52.346 1.00 31.35 C
ATOM 788 OD1 ASN C 344 -0.560 -13.074 51.169 1.00 27.58 O
ATOM 789 ND2 ASN C 344 -1.929 -12.340 52.804 1.00 27.72 N
ATOM 790 N ARG C 345 2.654 -15.328 53.918 1.00 33.66 N
ATOM 791 CA ARG C 345 3.578 -15.810 54.975 1.00 35.83 C
ATOM 792 C ARG C 345 2.857 -15.787 56.313 1.00 31.43 C
ATOM 793 O ARG C 345 2.215 -14.817 56.620 1.00 28.78 O
ATOM 794 CB ARG C 345 4.840 -14.953 55.078 1.00 43.76 C
ATOM 795 CG ARG C 345 5.967 -15.648 55.873 1.00 55.08 C
ATOM 796 CD ARG C 345 6.743 -14.776 56.888 1.00 62.02 C
ATOM 797 NE ARG C 345 5.905 -14.245 57.999 1.00 73.42 N
ATOM 798 CZ ARG C 345 5.515 -14.904 59.107 1.00 67.94 C
ATOM 799 NH1 ARG C 345 5.863 -16.174 59.347 1.00 68.08 N
ATOM 800 NH2 ARG C 345 4.750 -14.280 59.993 1.00 65.10 N
ATOM 801 N GLY C 346 2.897 -16.879 57.065 1.00 27.71 N
ATOM 802 CA GLY C 346 2.319 -16.918 58.385 1.00 27.21 C
ATOM 803 C GLY C 346 0.852 -17.256 58.417 1.00 28.20 C
ATOM 804 O GLY C 346 0.300 -17.436 59.497 1.00 29.94 O
ATOM 805 N GLU C 347 0.218 -17.357 57.246 1.00 30.07 N
ATOM 806 CA GLU C 347 -1.191 -17.708 57.176 1.00 30.63 C
ATOM 807 C GLU C 347 -1.380 -19.167 56.690 1.00 32.46 C
ATOM 808 O GLU C 347 -0.577 -19.640 55.891 1.00 32.56 O
ATOM 809 CB GLU C 347 -1.901 -16.715 56.254 1.00 31.03 C
ATOM 810 CG GLU C 347 -1.577 -15.216 56.515 1.00 31.97 C
ATOM 811 CD GLU C 347 -2.092 -14.705 57.860 1.00 33.19 C
ATOM 812 OE1 GLU C 347 -2.847 -15.474 58.527 1.00 33.41 O
ATOM 813 OE2 GLU C 347 -1.772 -13.520 58.237 1.00 31.34 O
ATOM 814 N PRO C 348 -2.460 -19.842 57.084 1.00 29.71 N
ATOM 815 CA PRO C 348 -3.532 -19.240 57.888 1.00 32.11 C
ATOM 816 C PRO C 348 -3.216 -19.405 59.363 1.00 32.42 C
ATOM 817 O PRO C 348 -2.594 -20.401 59.720 1.00 35.93 O
ATOM 818 CB PRO C 348 -4.769 -20.049 57.498 1.00 30.71 C
ATOM 819 CG PRO C 348 -4.226 -21.421 57.127 1.00 30.87 C
ATOM 820 CD PRO C 348 -2.789 -21.227 56.677 1.00 30.76 C
ATOM 821 N ASN C 349 -3.628 -18.469 60.220 1.00 28.85 N
ATOM 822 CA ASN C 349 -3.156 -18.531 61.611 1.00 30.65 C
ATOM 823 C ASN C 349 -4.295 -18.561 62.618 1.00 32.72 C
ATOM 824 O ASN C 349 -4.058 -18.717 63.815 1.00 33.07 O
ATOM 825 CB ASN C 349 -2.191 -17.373 61.934 1.00 28.51 C
ATOM 826 CG ASN C 349 -2.827 -15.999 61.699 1.00 27.80 C
ATOM 827 OD1 ASN C 349 -4.005 -15.915 61.343 1.00 25.42 O
ATOM 828 ND2 ASN C 349 -2.038 -14.926 61.840 1.00 26.69 N
ATOM 829 N ASN C 350 -5.513 -18.357 62.159 1.00 26.80 N
ATOM 830 CA ASN C 350 -6.660 -18.427 63.035 1.00 27.69 C
ATOM 831 C ASN C 350 -6.600 -17.454 64.191 1.00 28.45 C
ATOM 832 O ASN C 350 -7.180 -17.707 65.236 1.00 27.19 O
ATOM 833 CB ASN C 350 -6.853 -19.828 63.605 1.00 26.57 C
ATOM 834 CG ASN C 350 -8.264 -20.076 64.020 1.00 26.44 C
ATOM 835 OD1 ASN C 350 -9.230 -19.638 63.354 1.00 28.48 O
ATOM 836 ND2 ASN C 350 -8.426 -20.811 65.081 1.00 28.69 N
ATOM 837 N VAL C 351 -5.918 -16.337 63.990 1.00 28.11 N
ATOM 838 CA VAL C 351 -5.714 -15.435 65.083 1.00 32.27 C
ATOM 839 C VAL C 351 -7.008 -14.681 65.430 1.00 30.54 C
ATOM 840 O VAL C 351 -7.569 -13.969 64.598 1.00 30.20 O
ATOM 841 CB VAL C 351 -4.512 -14.516 64.833 1.00 32.26 C
ATOM 842 CG1 VAL C 351 -4.783 -13.542 63.705 1.00 33.73 C
ATOM 843 CG2 VAL C 351 -4.168 -13.793 66.129 1.00 34.15 C
ATOM 844 N GLY C 352 -7.498 -14.911 66.646 1.00 32.30 N
ATOM 845 CA GLY C 352 -8.789 -14.386 67.075 1.00 33.54 C
ATOM 846 C GLY C 352 -9.997 -15.123 66.483 1.00 36.13 C
ATOM 847 O GLY C 352 -11.109 -14.566 66.430 1.00 36.75 O
ATOM 848 N GLU C 353 -9.780 -16.355 66.015 1.00 34.12 N
ATOM 849 CA GLU C 353 -10.806 -17.146 65.276 1.00 34.87 C
ATOM 850 C GLU C 353 -11.084 -16.603 63.889 1.00 28.92 C
ATOM 851 O GLU C 353 -11.917 -15.727 63.691 1.00 26.00 O
ATOM 852 CB GLU C 353 -12.112 -17.271 66.052 1.00 39.26 C
ATOM 853 CG GLU C 353 -11.894 -17.762 67.472 1.00 47.91 C
ATOM 854 CD GLU C 353 -11.867 -19.276 67.598 1.00 59.42 C
ATOM 855 OE1 GLU C 353 -12.695 -19.773 68.392 1.00 70.48 O
ATOM 856 OE2 GLU C 353 -11.042 -19.966 66.926 1.00 66.69 O
ATOM 857 N GLU C 354 -10.365 -17.125 62.915 1.00 28.46 N
ATOM 858 CA GLU C 354 -10.498 -16.649 61.566 1.00 26.36 C
ATOM 859 C GLU C 354 -10.849 -17.813 60.690 1.00 26.15 C
ATOM 860 O GLU C 354 -10.015 -18.682 60.449 1.00 23.02 O
ATOM 861 CB GLU C 354 -9.185 -16.028 61.108 1.00 27.89 C
ATOM 862 CG GLU C 354 -8.826 -14.725 61.817 1.00 27.29 C
ATOM 863 CD GLU C 354 -7.577 -14.048 61.276 1.00 26.88 C
ATOM 864 OE1 GLU C 354 -6.551 -14.753 61.077 1.00 24.84 O
ATOM 865 OE2 GLU C 354 -7.606 -12.785 61.078 1.00 25.06 O
ATOM 866 N ASP C 355 -12.061 -17.830 60.152 1.00 27.71 N
ATOM 867 CA ASP C 355 -12.496 -19.032 59.406 1.00 26.77 C
ATOM 868 C ASP C 355 -12.822 -18.875 57.915 1.00 27.09 C
ATOM 869 O ASP C 355 -13.169 -19.848 57.280 1.00 27.47 O
ATOM 870 CB ASP C 355 -13.661 -19.699 60.118 1.00 26.00 C
ATOM 871 CG ASP C 355 -13.301 -20.172 61.513 1.00 26.34 C
ATOM 872 OD1 ASP C 355 -12.095 -20.226 61.831 1.00 28.36 O
ATOM 873 OD2 ASP C 355 -14.225 -20.489 62.291 1.00 28.30 O
ATOM 874 N CYS C 356 -12.659 -17.673 57.375 1.00 25.93 N
ATOM 875 CA CYS C 356 -12.958 -17.366 56.014 1.00 26.39 C
ATOM 876 C CYS C 356 -11.757 -16.761 55.270 1.00 26.71 C
ATOM 877 O CYS C 356 -11.085 -15.852 55.788 1.00 30.78 O
ATOM 878 CB CYS C 356 -14.138 -16.394 55.997 1.00 26.95 C
ATOM 879 SG CYS C 356 -15.647 -17.170 56.576 1.00 28.59 S
ATOM 880 N ALA C 357 -11.527 -17.220 54.040 1.00 25.21 N
ATOM 881 CA ALA C 357 -10.332 -16.857 53.297 1.00 23.22 C
ATOM 882 C ALA C 357 -10.588 -15.643 52.440 1.00 23.32 C
ATOM 883 O ALA C 357 -11.646 -15.517 51.815 1.00 25.17 O
ATOM 884 CB ALA C 357 -9.853 -18.023 52.439 1.00 22.14 C
ATOM 885 N GLU C 358 -9.636 -14.725 52.445 1.00 24.84 N
ATOM 886 CA GLU C 358 -9.693 -13.544 51.574 1.00 24.66 C
ATOM 887 C GLU C 358 -8.468 -13.451 50.711 1.00 23.74 C
ATOM 888 O GLU C 358 -7.428 -14.037 51.044 1.00 27.37 O
ATOM 889 CB GLU C 358 -9.821 -12.269 52.383 1.00 24.90 C
ATOM 890 CG GLU C 358 -8.637 -12.062 53.338 1.00 29.88 C
ATOM 891 CD GLU C 358 -8.587 -10.721 54.040 1.00 29.65 C
ATOM 892 OE1 GLU C 358 -7.736 -10.574 54.935 1.00 30.62 O
ATOM 893 OE2 GLU C 358 -9.327 -9.804 53.638 1.00 34.18 O
ATOM 894 N PHE C 359 -8.577 -12.702 49.614 1.00 20.75 N
ATOM 895 CA PHE C 359 -7.402 -12.256 48.903 1.00 22.94 C
ATOM 896 C PHE C 359 -6.934 -11.007 49.607 1.00 23.78 C
ATOM 897 O PHE C 359 -7.697 -10.070 49.760 1.00 26.83 O
ATOM 898 CB PHE C 359 -7.668 -11.932 47.421 1.00 22.12 C
ATOM 899 CG PHE C 359 -8.351 -13.024 46.649 1.00 21.90 C
ATOM 900 CD1 PHE C 359 -7.620 -14.015 46.006 1.00 21.98 C
ATOM 901 CD2 PHE C 359 -9.737 -13.010 46.472 1.00 22.47 C
ATOM 902 CE1 PHE C 359 -8.245 -14.988 45.264 1.00 22.02 C
ATOM 903 CE2 PHE C 359 -10.364 -13.999 45.756 1.00 22.78 C
ATOM 904 CZ PHE C 359 -9.613 -14.989 45.127 1.00 22.30 C
ATOM 905 N SER C 360 -5.678 -11.002 50.035 1.00 25.74 N
ATOM 906 CA SER C 360 -5.130 -9.923 50.820 1.00 28.24 C
ATOM 907 C SER C 360 -3.707 -9.616 50.390 1.00 29.49 C
ATOM 908 O SER C 360 -2.769 -10.333 50.717 1.00 31.90 O
ATOM 909 CB SER C 360 -5.215 -10.282 52.317 1.00 30.95 C
ATOM 910 OG SER C 360 -4.713 -9.251 53.110 1.00 30.83 O
ATOM 911 N GLY C 361 -3.570 -8.552 49.602 1.00 31.74 N
ATOM 912 CA GLY C 361 -2.315 -8.228 48.929 1.00 30.59 C
ATOM 913 C GLY C 361 -1.957 -9.253 47.861 1.00 29.71 C
ATOM 914 O GLY C 361 -2.669 -9.404 46.866 1.00 33.40 O
ATOM 915 N ASN C 362 -0.838 -9.951 48.054 1.00 29.71 N
ATOM 916 CA ASN C 362 -0.301 -10.853 47.022 1.00 30.66 C
ATOM 917 C ASN C 362 -0.727 -12.292 47.163 1.00 25.83 C
ATOM 918 O ASN C 362 -0.454 -13.086 46.305 1.00 25.58 O
ATOM 919 CB ASN C 362 1.235 -10.767 46.975 1.00 33.78 C
ATOM 920 CG ASN C 362 1.722 -9.380 46.548 1.00 39.81 C
ATOM 921 OD1 ASN C 362 2.779 -8.935 46.998 1.00 46.64 O
ATOM 922 ND2 ASN C 362 0.931 -8.673 45.716 1.00 36.61 N
ATOM 923 N GLY C 363 -1.410 -12.623 48.230 1.00 25.60 N
ATOM 924 CA GLY C 363 -1.844 -13.990 48.470 1.00 27.58 C
ATOM 925 C GLY C 363 -3.069 -14.024 49.365 1.00 28.97 C
ATOM 926 O GLY C 363 -3.819 -13.027 49.398 1.00 27.45 O
ATOM 927 N TRP C 364 -3.291 -15.156 50.058 1.00 27.53 N
ATOM 928 CA TRP C 364 -4.488 -15.319 50.869 1.00 26.98 C
ATOM 929 C TRP C 364 -4.263 -15.139 52.334 1.00 27.07 C
ATOM 930 O TRP C 364 -3.177 -15.373 52.847 1.00 29.10 O
ATOM 931 CB TRP C 364 -5.139 -16.676 50.711 1.00 26.80 C
ATOM 932 CG TRP C 364 -5.286 -17.189 49.318 1.00 28.17 C
ATOM 933 CD1 TRP C 364 -5.230 -16.484 48.157 1.00 27.16 C
ATOM 934 CD2 TRP C 364 -5.603 -18.520 48.965 1.00 28.90 C
ATOM 935 NE1 TRP C 364 -5.446 -17.299 47.104 1.00 25.83 N
ATOM 936 CE2 TRP C 364 -5.691 -18.563 47.563 1.00 27.93 C
ATOM 937 CE3 TRP C 364 -5.771 -19.709 49.702 1.00 30.54 C
ATOM 938 CZ2 TRP C 364 -5.954 -19.746 46.862 1.00 28.53 C
ATOM 939 CZ3 TRP C 364 -6.047 -20.889 49.010 1.00 32.19 C
ATOM 940 CH2 TRP C 364 -6.145 -20.892 47.596 1.00 29.39 C
ATOM 941 N ASN C 365 -5.339 -14.775 53.020 1.00 26.37 N
ATOM 942 CA ASN C 365 -5.319 -14.658 54.465 1.00 25.13 C
ATOM 943 C ASN C 365 -6.611 -15.213 54.989 1.00 25.63 C
ATOM 944 O ASN C 365 -7.654 -15.042 54.339 1.00 27.82 O
ATOM 945 CB ASN C 365 -5.143 -13.182 54.903 1.00 24.62 C
ATOM 946 CG ASN C 365 -5.198 -13.008 56.425 1.00 23.65 C
ATOM 947 OD1 ASN C 365 -4.524 -13.757 57.190 1.00 21.08 O
ATOM 948 ND2 ASN C 365 -6.046 -12.054 56.893 1.00 20.67 N
ATOM 949 N ASP C 366 -6.570 -15.875 56.145 1.00 25.10 N
ATOM 950 CA ASP C 366 -7.803 -16.109 56.906 1.00 24.66 C
ATOM 951 C ASP C 366 -8.141 -14.939 57.796 1.00 23.91 C
ATOM 952 O ASP C 366 -7.290 -14.467 58.567 1.00 23.24 O
ATOM 953 CB ASP C 366 -7.768 -17.376 57.766 1.00 25.29 C
ATOM 954 CG ASP C 366 -6.598 -17.423 58.735 1.00 25.52 C
ATOM 955 OD1 ASP C 366 -5.547 -16.774 58.512 1.00 24.51 O
ATOM 956 OD2 ASP C 366 -6.734 -18.188 59.692 1.00 30.51 O
ATOM 957 N ASP C 367 -9.412 -14.541 57.750 1.00 23.29 N
ATOM 958 CA ASP C 367 -9.914 -13.407 58.507 1.00 23.31 C
ATOM 959 C ASP C 367 -11.270 -13.747 59.073 1.00 24.66 C
ATOM 960 O ASP C 367 -11.777 -14.841 58.858 1.00 25.53 O
ATOM 961 CB ASP C 367 -9.994 -12.137 57.645 1.00 22.40 C
ATOM 962 CG ASP C 367 -9.870 -10.835 58.468 1.00 26.18 C
ATOM 963 OD1 ASP C 367 -9.873 -10.891 59.732 1.00 24.18 O
ATOM 964 OD2 ASP C 367 -9.777 -9.726 57.852 1.00 28.53 O
ATOM 965 N LYS C 368 -11.814 -12.825 59.862 1.00 24.79 N
ATOM 966 CA LYS C 368 -13.032 -13.067 60.585 1.00 27.98 C
ATOM 967 C LYS C 368 -14.195 -12.962 59.609 1.00 27.78 C
ATOM 968 O LYS C 368 -14.318 -11.984 58.831 1.00 27.53 O
ATOM 969 CB LYS C 368 -13.177 -12.109 61.785 1.00 31.10 C
ATOM 970 CG LYS C 368 -11.936 -12.010 62.652 1.00 35.95 C
ATOM 971 CD LYS C 368 -12.305 -11.644 64.085 1.00 43.96 C
ATOM 972 CE LYS C 368 -11.095 -11.180 64.897 1.00 51.46 C
ATOM 973 NZ LYS C 368 -10.814 -9.731 64.675 1.00 53.89 N
ATOM 974 N CYS C 369 -15.044 -13.988 59.651 1.00 26.87 N
ATOM 975 CA CYS C 369 -16.142 -14.164 58.716 1.00 25.73 C
ATOM 976 C CYS C 369 -17.193 -13.090 58.815 1.00 28.43 C
ATOM 977 O CYS C 369 -17.893 -12.842 57.850 1.00 29.33 O
ATOM 978 CB CYS C 369 -16.815 -15.519 58.927 1.00 29.66 C
ATOM 979 SG CYS C 369 -15.770 -16.952 58.559 1.00 31.71 S
ATOM 980 N ASN C 370 -17.327 -12.469 59.980 1.00 28.22 N
ATOM 981 CA ASN C 370 -18.368 -11.466 60.190 1.00 30.23 C
ATOM 982 C ASN C 370 -17.939 -10.082 59.677 1.00 28.52 C
ATOM 983 O ASN C 370 -18.712 -9.159 59.743 1.00 26.60 O
ATOM 984 CB ASN C 370 -18.814 -11.412 61.668 1.00 31.39 C
ATOM 985 CG ASN C 370 -17.673 -11.029 62.619 1.00 37.00 C
ATOM 986 OD1 ASN C 370 -16.491 -11.325 62.376 1.00 41.54 O
ATOM 987 ND2 ASN C 370 -18.023 -10.375 63.713 1.00 44.06 N
ATOM 988 N LEU C 371 -16.722 -9.957 59.169 1.00 26.98 N
ATOM 989 CA LEU C 371 -16.301 -8.723 58.576 1.00 26.50 C
ATOM 990 C LEU C 371 -16.732 -8.536 57.127 1.00 26.17 C
ATOM 991 O LEU C 371 -16.958 -9.493 56.414 1.00 28.68 O
ATOM 992 CB LEU C 371 -14.811 -8.593 58.675 1.00 27.00 C
ATOM 993 CG LEU C 371 -14.209 -8.502 60.063 1.00 29.44 C
ATOM 994 CD1 LEU C 371 -12.679 -8.458 59.966 1.00 29.70 C
ATOM 995 CD2 LEU C 371 -14.779 -7.371 60.927 1.00 28.84 C
ATOM 996 N ALA C 372 -16.829 -7.273 56.701 1.00 25.89 N
ATOM 997 CA ALA C 372 -17.321 -6.902 55.393 1.00 25.42 C
ATOM 998 C ALA C 372 -16.135 -6.691 54.433 1.00 26.03 C
ATOM 999 O ALA C 372 -15.197 -5.959 54.720 1.00 29.13 O
ATOM 1000 CB ALA C 372 -18.176 -5.647 55.484 1.00 25.11 C
ATOM 1001 N LYS C 373 -16.188 -7.359 53.297 1.00 25.36 N
ATOM 1002 CA LYS C 373 -15.153 -7.262 52.291 1.00 23.34 C
ATOM 1003 C LYS C 373 -15.822 -7.279 50.960 1.00 23.06 C
ATOM 1004 O LYS C 373 -17.011 -7.592 50.823 1.00 25.76 O
ATOM 1005 CB LYS C 373 -14.158 -8.424 52.399 1.00 24.74 C
ATOM 1006 CG LYS C 373 -13.574 -8.640 53.793 1.00 25.78 C
ATOM 1007 CD LYS C 373 -12.627 -9.813 53.780 1.00 27.18 C
ATOM 1008 CE LYS C 373 -11.928 -10.032 55.097 1.00 28.48 C
ATOM 1009 NZ LYS C 373 -11.020 -8.932 55.526 1.00 29.34 N
ATOM 1010 N PHE C 374 -15.055 -6.962 49.936 1.00 20.54 N
ATOM 1011 CA PHE C 374 -15.517 -7.183 48.606 1.00 20.62 C
ATOM 1012 C PHE C 374 -15.749 -8.687 48.343 1.00 19.71 C
ATOM 1013 O PHE C 374 -15.225 -9.477 49.044 1.00 21.44 O
ATOM 1014 CB PHE C 374 -14.527 -6.531 47.611 1.00 20.07 C
ATOM 1015 CG PHE C 374 -14.566 -5.031 47.694 1.00 21.01 C
ATOM 1016 CD1 PHE C 374 -13.752 -4.348 48.596 1.00 22.55 C
ATOM 1017 CD2 PHE C 374 -15.493 -4.323 46.984 1.00 20.48 C
ATOM 1018 CE1 PHE C 374 -13.831 -2.959 48.715 1.00 22.70 C
ATOM 1019 CE2 PHE C 374 -15.587 -2.965 47.106 1.00 22.68 C
ATOM 1020 CZ PHE C 374 -14.766 -2.289 47.983 1.00 21.85 C
ATOM 1021 N TRP C 375 -16.501 -9.048 47.301 1.00 22.72 N
ATOM 1022 CA TRP C 375 -16.676 -10.445 46.919 1.00 22.96 C
ATOM 1023 C TRP C 375 -16.629 -10.671 45.401 1.00 22.00 C
ATOM 1024 O TRP C 375 -16.759 -9.755 44.599 1.00 23.34 O
ATOM 1025 CB TRP C 375 -17.902 -11.073 47.558 1.00 22.87 C
ATOM 1026 CG TRP C 375 -19.202 -10.638 46.938 1.00 24.94 C
ATOM 1027 CD1 TRP C 375 -19.888 -11.273 45.953 1.00 25.94 C
ATOM 1028 CD2 TRP C 375 -19.972 -9.495 47.277 1.00 25.46 C
ATOM 1029 NE1 TRP C 375 -21.013 -10.580 45.615 1.00 25.03 N
ATOM 1030 CE2 TRP C 375 -21.111 -9.497 46.429 1.00 24.63 C
ATOM 1031 CE3 TRP C 375 -19.797 -8.442 48.189 1.00 26.17 C
ATOM 1032 CZ2 TRP C 375 -22.071 -8.521 46.467 1.00 25.34 C
ATOM 1033 CZ3 TRP C 375 -20.759 -7.461 48.233 1.00 27.71 C
ATOM 1034 CH2 TRP C 375 -21.902 -7.521 47.400 1.00 28.69 C
ATOM 1035 N ILE C 376 -16.326 -11.901 45.035 1.00 21.50 N
ATOM 1036 CA ILE C 376 -16.338 -12.299 43.687 1.00 25.01 C
ATOM 1037 C ILE C 376 -17.178 -13.557 43.548 1.00 24.55 C
ATOM 1038 O ILE C 376 -17.013 -14.489 44.307 1.00 26.89 O
ATOM 1039 CB ILE C 376 -14.945 -12.503 43.111 1.00 27.65 C
ATOM 1040 CG1 ILE C 376 -14.207 -11.168 43.073 1.00 28.05 C
ATOM 1041 CG2 ILE C 376 -15.057 -13.007 41.650 1.00 29.21 C
ATOM 1042 CD1 ILE C 376 -12.750 -11.318 42.668 1.00 30.63 C
ATOM 1043 N CYS C 377 -18.084 -13.519 42.578 1.00 22.66 N
ATOM 1044 CA CYS C 377 -18.949 -14.605 42.188 1.00 23.92 C
ATOM 1045 C CYS C 377 -18.426 -15.164 40.851 1.00 23.72 C
ATOM 1046 O CYS C 377 -17.845 -14.450 40.040 1.00 22.26 O
ATOM 1047 CB CYS C 377 -20.382 -14.133 41.921 1.00 24.88 C
ATOM 1048 SG CYS C 377 -21.258 -13.288 43.246 1.00 29.64 S
ATOM 1049 N LYS C 378 -18.697 -16.435 40.643 1.00 23.68 N
ATOM 1050 CA LYS C 378 -18.316 -17.160 39.430 1.00 24.79 C
ATOM 1051 C LYS C 378 -19.473 -18.062 39.025 1.00 26.50 C
ATOM 1052 O LYS C 378 -20.182 -18.647 39.888 1.00 22.48 O
ATOM 1053 CB LYS C 378 -17.137 -18.043 39.752 1.00 24.44 C
ATOM 1054 CG LYS C 378 -16.758 -19.074 38.708 1.00 25.70 C
ATOM 1055 CD LYS C 378 -15.529 -19.818 39.186 1.00 25.93 C
ATOM 1056 CE LYS C 378 -15.114 -20.936 38.242 1.00 27.37 C
ATOM 1057 NZ LYS C 378 -13.976 -21.728 38.779 1.00 27.06 N
ATOM 1058 N LYS C 379 -19.684 -18.134 37.722 1.00 26.61 N
ATOM 1059 CA LYS C 379 -20.586 -19.109 37.141 1.00 29.10 C
ATOM 1060 C LYS C 379 -20.155 -19.396 35.714 1.00 29.88 C
ATOM 1061 O LYS C 379 -19.354 -18.651 35.135 1.00 26.70 O
ATOM 1062 CB LYS C 379 -22.016 -18.602 37.168 1.00 31.41 C
ATOM 1063 CG LYS C 379 -22.314 -17.484 36.212 1.00 32.85 C
ATOM 1064 CD LYS C 379 -23.627 -16.833 36.557 1.00 35.14 C
ATOM 1065 CE LYS C 379 -24.394 -16.367 35.344 1.00 41.35 C
ATOM 1066 NZ LYS C 379 -25.695 -15.791 35.816 1.00 44.50 N
ATOM 1067 N SER C 380 -20.726 -20.446 35.131 1.00 31.32 N
ATOM 1068 CA SER C 380 -20.370 -20.850 33.774 1.00 33.29 C
ATOM 1069 C SER C 380 -20.807 -19.869 32.710 1.00 30.71 C
ATOM 1070 O SER C 380 -21.869 -19.286 32.778 1.00 28.43 O
ATOM 1071 CB SER C 380 -20.977 -22.225 33.475 1.00 37.71 C
ATOM 1072 OG SER C 380 -20.307 -23.176 34.279 1.00 37.50 O
ATOM 1073 N ALA C 381 -19.969 -19.690 31.705 1.00 30.99 N
ATOM 1074 CA ALA C 381 -20.381 -18.925 30.532 1.00 29.22 C
ATOM 1075 C ALA C 381 -21.471 -19.669 29.750 1.00 28.40 C
ATOM 1076 O ALA C 381 -21.598 -20.895 29.834 1.00 23.49 O
ATOM 1077 CB ALA C 381 -19.193 -18.674 29.650 1.00 30.86 C
ATOM 1078 N ALA C 382 -22.308 -18.909 29.065 1.00 29.48 N
ATOM 1079 CA ALA C 382 -23.225 -19.469 28.114 1.00 31.42 C
ATOM 1080 C ALA C 382 -22.397 -19.742 26.875 1.00 36.68 C
ATOM 1081 O ALA C 382 -21.486 -18.983 26.575 1.00 37.45 O
ATOM 1082 CB ALA C 382 -24.285 -18.465 27.781 1.00 30.09 C
ATOM 1083 N SER C 383 -22.673 -20.827 26.171 1.00 40.08 N
ATOM 1084 CA SER C 383 -22.075 -21.017 24.848 1.00 44.28 C
ATOM 1085 C SER C 383 -22.958 -20.350 23.805 1.00 42.12 C
ATOM 1086 O SER C 383 -24.082 -20.781 23.587 1.00 40.50 O
ATOM 1087 CB SER C 383 -21.968 -22.511 24.516 1.00 50.38 C
ATOM 1088 OG SER C 383 -21.594 -23.273 25.653 1.00 57.90 O
ATOM 1089 N CYS C 384 -22.446 -19.349 23.104 1.00 45.94 N
ATOM 1090 CA CYS C 384 -23.263 -18.678 22.097 1.00 53.95 C
ATOM 1091 C CYS C 384 -23.067 -19.214 20.652 1.00 58.19 C
ATOM 1092 O CYS C 384 -21.946 -19.295 20.149 1.00 70.81 O
ATOM 1093 CB CYS C 384 -23.054 -17.171 22.212 1.00 53.80 C
ATOM 1094 SG CYS C 384 -23.567 -16.579 23.849 1.00 49.63 S
TER 1095 CYS C 384
HETATM 1096 C4 EZ8 C1001 -3.556 -11.621 60.094 1.00 23.84 C
HETATM 1097 C5 EZ8 C1001 -2.659 -10.777 61.001 1.00 26.26 C
HETATM 1098 C6 EZ8 C1001 -1.247 -11.121 60.648 1.00 28.48 C
HETATM 1099 N2 EZ8 C1001 -5.455 -9.410 59.222 1.00 24.47 N
HETATM 1100 C3 EZ8 C1001 -4.919 -11.473 60.547 1.00 23.91 C
HETATM 1101 CAP EZ8 C1001 -7.303 -3.775 65.435 1.00 46.41 C
HETATM 1102 CAL EZ8 C1001 -7.142 -2.584 64.691 1.00 45.35 C
HETATM 1103 CBM EZ8 C1001 -8.181 -2.082 63.906 1.00 47.00 C
HETATM 1104 CAV EZ8 C1001 -7.990 -0.925 63.148 1.00 50.46 C
HETATM 1105 OAE EZ8 C1001 -8.353 0.281 63.861 1.00 48.10 O
HETATM 1106 CAM EZ8 C1001 -9.392 -2.810 63.867 1.00 43.80 C
HETATM 1107 CAQ EZ8 C1001 -9.564 -3.999 64.599 1.00 44.89 C
HETATM 1108 CBO EZ8 C1001 -8.500 -4.510 65.398 1.00 43.65 C
HETATM 1109 CAZ EZ8 C1001 -8.653 -5.687 66.168 1.00 41.22 C
HETATM 1110 NBF EZ8 C1001 -7.565 -6.671 65.883 1.00 36.32 N
HETATM 1111 CBK EZ8 C1001 -7.539 -7.442 64.780 1.00 33.61 C
HETATM 1112 OAC EZ8 C1001 -8.374 -7.345 63.888 1.00 36.15 O
HETATM 1113 CBW EZ8 C1001 -6.333 -8.402 64.582 1.00 30.77 C
HETATM 1114 CBB EZ8 C1001 -5.285 -7.613 63.970 1.00 28.76 C
HETATM 1115 CBV EZ8 C1001 -5.875 -9.082 65.861 1.00 31.38 C
HETATM 1116 CBJ EZ8 C1001 -7.028 -9.899 66.472 1.00 33.02 C
HETATM 1117 OAB EZ8 C1001 -7.731 -10.586 65.747 1.00 37.23 O
HETATM 1118 NBE EZ8 C1001 -7.165 -9.823 67.801 1.00 32.68 N
HETATM 1119 CAY EZ8 C1001 -8.227 -10.486 68.623 1.00 32.47 C
HETATM 1120 CBN EZ8 C1001 -7.751 -11.643 69.316 1.00 29.97 C
HETATM 1121 CAN EZ8 C1001 -8.479 -12.224 70.369 1.00 31.10 C
HETATM 1122 CAJ EZ8 C1001 -8.002 -13.377 71.002 1.00 28.33 C
HETATM 1123 CBL EZ8 C1001 -6.807 -13.943 70.591 1.00 28.90 C
HETATM 1124 CAU EZ8 C1001 -6.267 -15.029 71.176 1.00 32.48 C
HETATM 1125 OAD EZ8 C1001 -7.276 -16.005 71.243 1.00 39.73 O
HETATM 1126 CAK EZ8 C1001 -6.091 -13.363 69.567 1.00 29.46 C
HETATM 1127 CAO EZ8 C1001 -6.555 -12.222 68.946 1.00 28.06 C
HETATM 1128 CBA EZ8 C1001 -4.831 -10.028 65.584 1.00 31.43 C
HETATM 1129 CBT EZ8 C1001 -3.669 -9.323 64.866 1.00 29.34 C
HETATM 1130 OBG EZ8 C1001 -2.974 -8.496 65.754 1.00 32.73 O
HETATM 1131 CAX EZ8 C1001 -1.621 -8.390 65.375 1.00 37.63 C
HETATM 1132 CAT EZ8 C1001 -1.070 -7.215 66.218 1.00 43.43 C
HETATM 1133 CL1 EZ8 C1001 -2.374 -5.979 66.637 1.00 53.34 Cl
HETATM 1134 CBU EZ8 C1001 -4.129 -8.547 63.660 1.00 29.95 C
HETATM 1135 O1 EZ8 C1001 -4.428 -9.517 62.669 1.00 25.08 O
HETATM 1136 C1 EZ8 C1001 -4.232 -9.143 61.315 1.00 24.82 C
HETATM 1137 O5 EZ8 C1001 -2.975 -9.368 60.800 1.00 25.11 O
HETATM 1138 O6 EZ8 C1001 -0.406 -10.106 61.172 1.00 31.40 O
HETATM 1139 O4 EZ8 C1001 -3.191 -12.987 60.093 1.00 24.38 O
HETATM 1140 O3 EZ8 C1001 -5.835 -12.193 59.689 1.00 23.89 O
HETATM 1141 C2 EZ8 C1001 -5.278 -9.972 60.518 1.00 23.87 C
HETATM 1142 CAR EZ8 C1001 -6.592 -8.921 58.753 1.00 25.12 C
HETATM 1143 NBD EZ8 C1001 -4.512 -9.239 58.288 1.00 24.43 N
HETATM 1144 NBC EZ8 C1001 -4.963 -8.694 57.349 1.00 24.41 N
HETATM 1145 CBP EZ8 C1001 -6.255 -8.463 57.550 1.00 26.90 C
HETATM 1146 CAS EZ8 C1001 -7.197 -7.776 56.578 1.00 27.46 C
HETATM 1147 NAA EZ8 C1001 -6.713 -7.953 55.218 1.00 30.03 N
HETATM 1148 CA CA C1002 -5.057 -14.525 59.344 1.00 25.73 Ca
HETATM 1149 CA CA C1003 -9.862 -20.970 61.350 1.00 27.95 Ca
HETATM 1150 CA CA C1004 -14.113 -21.919 63.758 1.00 51.36 Ca
HETATM 1151 CL CL C1005 -22.111 -4.897 44.537 1.00 60.06 Cl
HETATM 1152 CL CL C1006 -10.000 -15.788 28.746 1.00 58.86 Cl
HETATM 1153 O HOH C1101 -6.071 -23.422 63.013 1.00 38.74 O
HETATM 1154 O HOH C1102 -19.401 -1.470 51.134 1.00 28.21 O
HETATM 1155 O HOH C1103 -13.588 -27.224 57.235 1.00 25.45 O
HETATM 1156 O HOH C1104 -24.598 -5.755 48.877 1.00 53.62 O
HETATM 1157 O HOH C1105 -9.410 -16.537 70.090 1.00 45.76 O
HETATM 1158 O HOH C1106 -26.712 -13.529 36.235 1.00 48.45 O
HETATM 1159 O HOH C1107 -16.250 -23.490 52.698 1.00 33.61 O
HETATM 1160 O HOH C1108 -11.721 -7.517 63.860 1.00 49.58 O
HETATM 1161 O HOH C1109 -21.227 -8.899 59.509 1.00 34.03 O
HETATM 1162 O HOH C1110 -8.152 -27.783 40.904 1.00 33.14 O
HETATM 1163 O HOH C1111 -10.623 0.671 64.967 1.00 33.32 O
HETATM 1164 O HOH C1112 -13.047 -23.407 62.925 1.00 31.79 O
HETATM 1165 O HOH C1113 -1.883 -12.289 39.985 1.00 30.43 O
HETATM 1166 O HOH C1114 -6.586 -22.361 33.870 1.00 43.53 O
HETATM 1167 O HOH C1115 -22.978 -8.410 55.095 1.00 23.90 O
HETATM 1168 O HOH C1116 -9.668 -10.868 44.345 1.00 31.56 O
HETATM 1169 O HOH C1117 -12.338 -19.776 34.653 1.00 26.94 O
HETATM 1170 O HOH C1118 -23.997 -21.394 38.903 1.00 41.57 O
HETATM 1171 O HOH C1119 -10.746 -22.570 66.512 1.00 46.96 O
HETATM 1172 O HOH C1120 -16.039 -13.905 62.828 1.00 37.61 O
HETATM 1173 O HOH C1121 -7.943 -20.430 60.465 1.00 24.95 O
HETATM 1174 O HOH C1122 -25.230 -17.339 53.760 1.00 43.07 O
HETATM 1175 O HOH C1123 -14.530 1.018 45.230 1.00 55.04 O
HETATM 1176 O HOH C1124 -8.274 -11.125 63.067 1.00 28.39 O
HETATM 1177 O HOH C1125 -20.465 -14.387 57.842 1.00 35.13 O
HETATM 1178 O HOH C1126 -12.425 -21.049 64.373 1.00 31.90 O
HETATM 1179 O HOH C1127 -27.618 -13.981 53.868 1.00 39.44 O
HETATM 1180 O HOH C1128 -16.149 -22.756 63.159 1.00 34.62 O
HETATM 1181 O HOH C1129 -27.133 -10.791 44.547 1.00 42.64 O
HETATM 1182 O HOH C1130 -15.405 -20.675 64.728 1.00 37.80 O
HETATM 1183 O HOH C1131 1.492 -25.480 47.679 1.00 42.57 O
HETATM 1184 O HOH C1132 -25.399 -14.575 29.170 1.00 51.50 O
HETATM 1185 O HOH C1133 -5.048 -6.457 48.648 1.00 36.61 O
HETATM 1186 O HOH C1134 0.644 -9.826 50.355 1.00 46.15 O
HETATM 1187 O HOH C1135 0.302 -12.521 43.732 1.00 42.34 O
HETATM 1188 O HOH C1136 -8.184 -29.874 60.695 1.00 29.49 O
HETATM 1189 O HOH C1137 -6.926 -27.439 54.424 1.00 39.54 O
HETATM 1190 O HOH C1138 -12.030 -23.030 32.914 1.00 43.13 O
HETATM 1191 O HOH C1139 -14.975 -7.169 43.917 1.00 31.87 O
HETATM 1192 O HOH C1140 -17.811 -7.609 37.641 1.00 46.86 O
HETATM 1193 O HOH C1141 -24.141 -20.012 34.236 1.00 40.11 O
HETATM 1194 O HOH C1142 -22.992 -4.267 50.149 1.00 44.56 O
HETATM 1195 O HOH C1143 -20.404 -9.508 29.818 1.00 28.59 O
HETATM 1196 O HOH C1144 -18.480 -22.255 37.030 1.00 44.55 O
HETATM 1197 O HOH C1145 -4.260 -15.258 34.857 1.00 43.79 O
HETATM 1198 O HOH C1146 3.585 -13.489 52.010 1.00 38.01 O
HETATM 1199 O HOH C1147 -11.767 -6.266 56.080 1.00 39.36 O
HETATM 1200 O HOH C1148 0.263 -22.215 55.092 1.00 34.72 O
HETATM 1201 O HOH C1149 -10.011 -21.084 34.488 1.00 39.15 O
HETATM 1202 O HOH C1150 -10.195 -29.736 44.999 1.00 43.16 O
HETATM 1203 O HOH C1151 -15.515 -23.542 40.339 1.00 31.92 O
HETATM 1204 O HOH C1152 -9.844 -22.721 36.578 1.00 32.23 O
HETATM 1205 O HOH C1153 -17.538 -20.953 42.186 1.00 42.19 O
HETATM 1206 O HOH C1154 -0.663 -5.882 41.781 1.00 37.98 O
HETATM 1207 O HOH C1155 -23.565 -16.545 31.658 1.00 41.92 O
HETATM 1208 O HOH C1156 -11.219 -3.795 51.018 1.00 41.10 O
HETATM 1209 O HOH C1157 -1.872 -11.930 55.846 1.00 42.38 O
HETATM 1210 O HOH C1158 -22.166 -18.676 46.928 1.00 30.65 O
HETATM 1211 O HOH C1159 -15.344 -9.813 29.854 1.00 37.10 O
HETATM 1212 O HOH C1160 -8.411 -4.423 40.296 1.00 40.70 O
HETATM 1213 O AHOH C1161 -13.796 -26.664 64.188 0.50 22.41 O
HETATM 1214 O BHOH C1161 -15.911 -26.495 63.751 0.50 23.87 O
HETATM 1215 O HOH C1162 -1.301 -10.372 41.732 1.00 40.84 O
HETATM 1216 O HOH C1163 -11.534 -26.074 44.246 1.00 36.65 O
HETATM 1217 O HOH C1164 -14.151 -16.285 61.474 1.00 22.60 O
HETATM 1218 O HOH C1165 -17.889 -10.319 29.607 1.00 47.89 O
HETATM 1219 O HOH C1166 -25.370 -21.282 43.314 1.00 49.89 O
HETATM 1220 O HOH C1167 -12.881 -23.476 36.688 1.00 45.26 O
HETATM 1221 O HOH C1168 -15.880 -18.060 62.467 1.00 42.05 O
HETATM 1222 O HOH C1169 -13.031 -4.408 53.448 1.00 33.94 O
HETATM 1223 O HOH C1170 -27.141 -9.146 31.720 1.00 29.22 O
HETATM 1224 O HOH C1171 -26.201 -8.032 34.312 1.00 41.70 O
HETATM 1225 O HOH C1172 -7.360 -29.344 52.730 1.00 36.66 O
HETATM 1226 O HOH C1173 -7.738 -26.646 45.695 1.00 27.12 O
HETATM 1227 O HOH C1174 -2.117 -4.732 47.625 1.00 37.58 O
HETATM 1228 O HOH C1175 1.605 -28.617 50.293 1.00 50.84 O
HETATM 1229 O HOH C1176 -11.046 -1.333 50.870 1.00 37.28 O
HETATM 1230 O HOH C1177 -0.925 -15.673 42.578 1.00 38.66 O
HETATM 1231 O HOH C1178 -20.353 -11.420 27.825 1.00 43.19 O
HETATM 1232 O HOH C1179 -3.261 -25.195 37.834 1.00 38.29 O
HETATM 1233 O HOH C1180 -4.129 -24.821 54.326 1.00 34.50 O
HETATM 1234 O HOH C1181 -14.205 -29.820 56.466 1.00 46.13 O
HETATM 1235 O HOH C1182 -23.400 -10.850 43.749 1.00 33.26 O
HETATM 1236 O HOH C1183 -6.497 -22.894 59.892 1.00 32.63 O
HETATM 1237 O HOH C1184 -22.807 -22.089 36.653 1.00 44.20 O
HETATM 1238 O HOH C1185 -15.588 -25.556 56.255 1.00 32.66 O
HETATM 1239 O HOH C1186 -1.068 -2.004 44.151 1.00 52.90 O
HETATM 1240 O HOH C1187 -5.943 -16.894 68.428 1.00 40.33 O
HETATM 1241 O HOH C1188 -21.344 -26.569 44.189 1.00 49.45 O
HETATM 1242 O HOH C1189 2.184 -20.817 52.583 1.00 46.08 O
HETATM 1243 O HOH C1190 -18.387 -6.893 61.864 1.00 37.09 O
HETATM 1244 O HOH C1191 -30.920 -12.629 39.430 1.00 48.64 O
HETATM 1245 O HOH C1192 -19.570 -21.712 39.728 1.00 46.75 O
HETATM 1246 O HOH C1193 -23.136 -23.054 49.645 1.00 49.47 O
HETATM 1247 O HOH C1194 -1.850 -27.802 40.890 1.00 40.17 O
HETATM 1248 O HOH C1195 -25.131 -12.261 58.396 1.00 50.02 O
HETATM 1249 O HOH C1196 -21.985 -21.824 58.634 1.00 54.80 O
HETATM 1250 O HOH C1197 -31.396 -18.096 43.145 1.00 41.73 O
HETATM 1251 O HOH C1198 -2.975 -3.598 35.622 1.00 44.29 O
HETATM 1252 O AHOH C1199 -5.839 -27.536 37.442 0.50 32.44 O
HETATM 1253 O BHOH C1199 -7.486 -26.812 36.388 0.50 36.43 O
HETATM 1254 O HOH C1200 -26.519 -8.214 53.210 1.00 53.79 O
HETATM 1255 O HOH C1201 -2.232 -31.197 45.020 1.00 47.50 O
HETATM 1256 O HOH C1202 -0.909 -25.118 41.645 1.00 50.61 O
HETATM 1257 O HOH C1203 -27.589 -12.802 26.389 1.00 43.16 O
HETATM 1258 O HOH C1204 1.240 -15.473 62.084 1.00 49.11 O
HETATM 1259 O HOH C1205 -4.056 -21.194 30.717 1.00 37.22 O
HETATM 1260 O HOH C1206 1.612 -5.837 44.080 1.00 49.81 O
HETATM 1261 O HOH C1207 -5.681 -21.840 66.729 1.00 47.19 O
HETATM 1262 O HOH C1208 -3.570 -5.199 50.175 1.00 50.77 O
HETATM 1263 O HOH C1209 1.905 -10.673 58.687 1.00 48.79 O
HETATM 1264 O HOH C1210 1.817 -16.018 48.608 1.00 46.59 O
HETATM 1265 O HOH C1211 -9.279 -27.204 43.788 1.00 41.30 O
HETATM 1266 O HOH C1212 1.211 -20.854 59.965 1.00 47.79 O
HETATM 1267 O HOH C1213 -32.561 -12.071 20.776 1.00 39.27 O
HETATM 1268 O HOH C1214 -23.769 -1.539 45.575 1.00 49.90 O
HETATM 1269 O HOH C1215 3.758 -24.932 49.502 1.00 39.97 O
HETATM 1270 O HOH C1216 -22.555 -21.584 47.531 1.00 43.61 O
HETATM 1271 O HOH C1217 -7.247 -24.942 33.683 1.00 38.53 O
HETATM 1272 O HOH C1218 -18.773 -25.142 52.439 1.00 50.99 O
HETATM 1273 O HOH C1219 -0.301 -15.438 65.276 1.00 50.45 O
HETATM 1274 O HOH C1220 -5.152 -29.710 60.903 1.00 45.01 O
HETATM 1275 O HOH C1221 -14.449 -23.098 65.517 1.00 33.95 O
HETATM 1276 O HOH C1222 -1.124 -24.385 55.548 1.00 48.01 O
HETATM 1277 O HOH C1223 -30.259 -17.599 49.634 1.00 49.11 O
HETATM 1278 O HOH C1224 -9.990 -25.487 35.762 1.00 43.23 O
HETATM 1279 O HOH C1225 -19.092 -17.087 61.366 1.00 53.67 O
HETATM 1280 O HOH C1226 -17.086 -20.474 26.973 1.00 39.93 O
HETATM 1281 O HOH C1227 -10.169 -29.271 40.672 1.00 37.44 O
HETATM 1282 O HOH C1228 -29.659 -16.028 55.272 1.00 60.71 O
HETATM 1283 O HOH C1229 -15.533 -4.618 37.378 1.00 51.93 O
HETATM 1284 O HOH C1230 1.772 -8.841 40.799 1.00 44.89 O
HETATM 1285 O HOH C1231 -17.240 1.706 37.600 1.00 55.38 O
HETATM 1286 O HOH C1232 -26.683 -4.632 24.425 1.00 44.76 O
HETATM 1287 O HOH C1233 -10.532 -25.322 67.138 1.00 61.18 O
HETATM 1288 O HOH C1234 -12.201 -10.414 26.962 1.00 49.22 O
HETATM 1289 O HOH C1235 -7.330 -25.567 67.189 1.00 57.65 O
CONECT 14 13 1094
CONECT 37 36 137
CONECT 137 37 136
CONECT 285 1048 284
CONECT 577 1149
CONECT 578 1149
CONECT 616 1149
CONECT 617 1149
CONECT 812 1148
CONECT 827 1148
CONECT 835 1149
CONECT 860 1149
CONECT 864 1148
CONECT 872 1149
CONECT 873 1150
CONECT 879 878 979
CONECT 947 1148
CONECT 952 1148
CONECT 955 1148
CONECT 979 879 978
CONECT 1048 1047 285
CONECT 1094 14 1093
CONECT 1136 1135 1137 1141
CONECT 1141 1099 1136 1100
CONECT 1100 1096 1140 1141
CONECT 1096 1139 1097 1100
CONECT 1097 1096 1098 1137
CONECT 1098 1097 1138
CONECT 1122 1121 1123
CONECT 1126 1123 1127
CONECT 1102 1103 1101
CONECT 1106 1103 1107
CONECT 1121 1122 1120
CONECT 1127 1126 1120
CONECT 1101 1102 1108
CONECT 1107 1106 1108
CONECT 1142 1099 1145
CONECT 1146 1145 1147
CONECT 1132 1131 1133
CONECT 1124 1125 1123
CONECT 1104 1105 1103
CONECT 1131 1130 1132
CONECT 1119 1118 1120
CONECT 1109 1110 1108
CONECT 1128 1129 1115
CONECT 1114 1134 1113
CONECT 1116 1115 1118 1117
CONECT 1111 1110 1112 1113
CONECT 1123 1124 1122 1126
CONECT 1103 1102 1106 1104
CONECT 1120 1121 1127 1119
CONECT 1108 1109 1107 1101
CONECT 1145 1146 1142 1144
CONECT 1129 1128 1134 1130
CONECT 1134 1129 1135 1114
CONECT 1115 1128 1116 1113
CONECT 1113 1115 1114 1111
CONECT 1133 1132
CONECT 1099 1141 1142 1143
CONECT 1147 1146
CONECT 1144 1145 1143
CONECT 1143 1099 1144
CONECT 1118 1116 1119
CONECT 1110 1109 1111
CONECT 1135 1134 1136
CONECT 1140 1100
CONECT 1140 1148
CONECT 1139 1096
CONECT 1139 1148
CONECT 1137 1097 1136
CONECT 1138 1098
CONECT 1117 1116
CONECT 1112 1111
CONECT 1125 1124
CONECT 1105 1104
CONECT 1130 1129 1131
CONECT 1148 812 827 1139 1140
CONECT 1148 864 947 952 955
CONECT 1149 835 860 872 577
CONECT 1149 578 616 1173 617
CONECT 1150 1178 1180 1182 1275
CONECT 1150 873 1164
CONECT 1164 1150
CONECT 1173 1149
CONECT 1178 1150
CONECT 1180 1150
CONECT 1182 1150
CONECT 1275 1150
END
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