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*** bec_luci_A ***elNémo ID: 2404021201272023130Job options:ID = 2404021201272023130 JOBID = bec_luci_A 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 bec_luci_A
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 A 276 GLU A 286 1 11
HELIX 2 2 SER A 296 ASN A 311 1 16
HELIX 3 3 LEU A 336 TRP A 343 1 8
SHEET 1 1 1 THR A 261 PHE A 263 0
SHEET 2 2 1 ASN A 266 MET A 270 0
SHEET 3 3 1 GLN A 290 LEU A 291 0
SHEET 4 4 1 THR A 314 SER A 319 0
SHEET 5 5 1 GLN A 328 TRP A 329 0
SHEET 6 6 1 CYS A 356 SER A 360 0
SHEET 7 7 1 GLY A 363 ASP A 367 0
SHEET 8 8 1 PHE A 374 SER A 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 CYS A 253 -28.471 1.709 33.406 1.00 83.64 N
ATOM 2 CA CYS A 253 -27.226 2.492 33.116 1.00 86.10 C
ATOM 3 C CYS A 253 -25.968 1.659 33.376 1.00 74.44 C
ATOM 4 O CYS A 253 -25.479 1.575 34.513 1.00 68.79 O
ATOM 5 CB CYS A 253 -27.147 3.790 33.945 1.00 91.58 C
ATOM 6 SG CYS A 253 -25.738 4.864 33.497 1.00 96.83 S
ATOM 7 N HIS A 254 -25.454 1.063 32.306 1.00 59.58 N
ATOM 8 CA HIS A 254 -24.186 0.358 32.335 1.00 48.45 C
ATOM 9 C HIS A 254 -23.056 1.302 31.911 1.00 40.66 C
ATOM 10 O HIS A 254 -23.182 1.988 30.931 1.00 40.06 O
ATOM 11 CB HIS A 254 -24.274 -0.825 31.390 1.00 45.73 C
ATOM 12 CG HIS A 254 -25.386 -1.773 31.710 1.00 43.38 C
ATOM 13 ND1 HIS A 254 -25.329 -2.659 32.767 1.00 43.45 N
ATOM 14 CD2 HIS A 254 -26.564 -2.003 31.088 1.00 42.88 C
ATOM 15 CE1 HIS A 254 -26.435 -3.380 32.789 1.00 45.53 C
ATOM 16 NE2 HIS A 254 -27.192 -3.015 31.769 1.00 45.27 N
ATOM 17 N PRO A 255 -21.953 1.356 32.658 1.00 39.91 N
ATOM 18 CA PRO A 255 -20.904 2.290 32.224 1.00 39.31 C
ATOM 19 C PRO A 255 -20.341 1.971 30.813 1.00 39.47 C
ATOM 20 O PRO A 255 -19.856 2.850 30.130 1.00 39.36 O
ATOM 21 CB PRO A 255 -19.813 2.111 33.294 1.00 41.76 C
ATOM 22 CG PRO A 255 -20.523 1.591 34.509 1.00 42.79 C
ATOM 23 CD PRO A 255 -21.689 0.792 34.000 1.00 41.73 C
ATOM 24 N CYS A 256 -20.407 0.720 30.395 1.00 34.96 N
ATOM 25 CA CYS A 256 -19.863 0.330 29.128 1.00 35.47 C
ATOM 26 C CYS A 256 -20.828 -0.552 28.398 1.00 38.01 C
ATOM 27 O CYS A 256 -21.737 -1.145 29.010 1.00 38.18 O
ATOM 28 CB CYS A 256 -18.596 -0.477 29.327 1.00 34.75 C
ATOM 29 SG CYS A 256 -17.256 0.452 30.020 1.00 36.97 S
ATOM 30 N PRO A 257 -20.622 -0.669 27.080 1.00 35.78 N
ATOM 31 CA PRO A 257 -21.353 -1.650 26.295 1.00 33.86 C
ATOM 32 C PRO A 257 -21.035 -3.060 26.744 1.00 31.78 C
ATOM 33 O PRO A 257 -19.961 -3.324 27.233 1.00 31.47 O
ATOM 34 CB PRO A 257 -20.870 -1.428 24.844 1.00 36.01 C
ATOM 35 CG PRO A 257 -20.150 -0.095 24.855 1.00 39.44 C
ATOM 36 CD PRO A 257 -19.729 0.187 26.275 1.00 37.44 C
ATOM 37 N TRP A 258 -22.008 -3.936 26.590 1.00 31.63 N
ATOM 38 CA TRP A 258 -21.910 -5.332 26.931 1.00 35.24 C
ATOM 39 C TRP A 258 -20.646 -5.995 26.361 1.00 36.61 C
ATOM 40 O TRP A 258 -20.355 -5.926 25.159 1.00 41.16 O
ATOM 41 CB TRP A 258 -23.165 -6.058 26.386 1.00 37.62 C
ATOM 42 CG TRP A 258 -23.576 -7.333 27.115 1.00 38.69 C
ATOM 43 CD1 TRP A 258 -22.757 -8.285 27.659 1.00 40.83 C
ATOM 44 CD2 TRP A 258 -24.914 -7.776 27.349 1.00 38.53 C
ATOM 45 NE1 TRP A 258 -23.504 -9.288 28.221 1.00 39.24 N
ATOM 46 CE2 TRP A 258 -24.832 -8.999 28.050 1.00 38.29 C
ATOM 47 CE3 TRP A 258 -26.175 -7.248 27.046 1.00 37.58 C
ATOM 48 CZ2 TRP A 258 -25.963 -9.716 28.445 1.00 40.57 C
ATOM 49 CZ3 TRP A 258 -27.301 -7.958 27.436 1.00 42.28 C
ATOM 50 CH2 TRP A 258 -27.188 -9.192 28.123 1.00 42.19 C
ATOM 51 N GLU A 259 -19.902 -6.643 27.244 1.00 36.63 N
ATOM 52 CA GLU A 259 -18.721 -7.410 26.888 1.00 38.66 C
ATOM 53 C GLU A 259 -17.479 -6.573 26.871 1.00 37.90 C
ATOM 54 O GLU A 259 -16.417 -7.121 26.724 1.00 39.66 O
ATOM 55 CB GLU A 259 -18.860 -8.080 25.511 1.00 40.79 C
ATOM 56 CG GLU A 259 -20.057 -9.003 25.399 1.00 41.75 C
ATOM 57 CD GLU A 259 -19.844 -10.095 24.386 1.00 43.29 C
ATOM 58 OE1 GLU A 259 -18.685 -10.516 24.208 1.00 43.21 O
ATOM 59 OE2 GLU A 259 -20.844 -10.551 23.794 1.00 47.40 O
ATOM 60 N TRP A 260 -17.615 -5.255 26.985 1.00 35.20 N
ATOM 61 CA TRP A 260 -16.477 -4.359 27.139 1.00 34.25 C
ATOM 62 C TRP A 260 -16.080 -4.306 28.594 1.00 35.54 C
ATOM 63 O TRP A 260 -16.897 -4.528 29.485 1.00 36.75 O
ATOM 64 CB TRP A 260 -16.828 -2.951 26.679 1.00 33.97 C
ATOM 65 CG TRP A 260 -17.094 -2.814 25.213 1.00 36.45 C
ATOM 66 CD1 TRP A 260 -17.970 -3.548 24.459 1.00 34.99 C
ATOM 67 CD2 TRP A 260 -16.522 -1.838 24.325 1.00 33.32 C
ATOM 68 NE1 TRP A 260 -17.946 -3.111 23.176 1.00 33.55 N
ATOM 69 CE2 TRP A 260 -17.096 -2.043 23.064 1.00 33.65 C
ATOM 70 CE3 TRP A 260 -15.599 -0.812 24.485 1.00 33.59 C
ATOM 71 CZ2 TRP A 260 -16.753 -1.278 21.940 1.00 32.92 C
ATOM 72 CZ3 TRP A 260 -15.259 -0.048 23.369 1.00 36.22 C
ATOM 73 CH2 TRP A 260 -15.845 -0.286 22.117 1.00 33.27 C
ATOM 74 N THR A 261 -14.817 -3.985 28.816 1.00 34.49 N
ATOM 75 CA THR A 261 -14.199 -3.960 30.127 1.00 33.38 C
ATOM 76 C THR A 261 -14.097 -2.510 30.558 1.00 29.85 C
ATOM 77 O THR A 261 -13.548 -1.685 29.827 1.00 25.44 O
ATOM 78 CB THR A 261 -12.780 -4.554 30.079 1.00 36.92 C
ATOM 79 OG1 THR A 261 -12.846 -5.927 29.650 1.00 38.64 O
ATOM 80 CG2 THR A 261 -12.098 -4.480 31.463 1.00 38.39 C
ATOM 81 N PHE A 262 -14.667 -2.210 31.718 1.00 28.86 N
ATOM 82 CA PHE A 262 -14.498 -0.917 32.373 1.00 31.29 C
ATOM 83 C PHE A 262 -13.116 -0.842 33.037 1.00 30.45 C
ATOM 84 O PHE A 262 -12.701 -1.762 33.747 1.00 30.33 O
ATOM 85 CB PHE A 262 -15.581 -0.741 33.443 1.00 31.68 C
ATOM 86 CG PHE A 262 -15.531 0.586 34.141 1.00 30.63 C
ATOM 87 CD1 PHE A 262 -16.221 1.663 33.635 1.00 33.90 C
ATOM 88 CD2 PHE A 262 -14.754 0.766 35.268 1.00 32.98 C
ATOM 89 CE1 PHE A 262 -16.174 2.892 34.262 1.00 32.64 C
ATOM 90 CE2 PHE A 262 -14.704 1.990 35.916 1.00 33.80 C
ATOM 91 CZ PHE A 262 -15.401 3.060 35.396 1.00 33.67 C
ATOM 92 N PHE A 263 -12.396 0.246 32.812 1.00 30.86 N
ATOM 93 CA PHE A 263 -11.190 0.514 33.589 1.00 29.87 C
ATOM 94 C PHE A 263 -11.015 2.028 33.659 1.00 33.56 C
ATOM 95 O PHE A 263 -10.889 2.702 32.605 1.00 27.81 O
ATOM 96 CB PHE A 263 -9.996 -0.168 32.965 1.00 30.39 C
ATOM 97 CG PHE A 263 -8.680 0.175 33.606 1.00 31.37 C
ATOM 98 CD1 PHE A 263 -7.953 1.284 33.162 1.00 29.61 C
ATOM 99 CD2 PHE A 263 -8.153 -0.616 34.623 1.00 31.13 C
ATOM 100 CE1 PHE A 263 -6.748 1.614 33.731 1.00 30.34 C
ATOM 101 CE2 PHE A 263 -6.932 -0.295 35.193 1.00 35.35 C
ATOM 102 CZ PHE A 263 -6.225 0.826 34.739 1.00 33.34 C
ATOM 103 N GLN A 264 -11.074 2.535 34.902 1.00 32.46 N
ATOM 104 CA GLN A 264 -10.778 3.935 35.256 1.00 31.17 C
ATOM 105 C GLN A 264 -11.456 4.942 34.365 1.00 30.93 C
ATOM 106 O GLN A 264 -10.803 5.850 33.822 1.00 27.83 O
ATOM 107 CB GLN A 264 -9.263 4.211 35.305 1.00 30.45 C
ATOM 108 CG GLN A 264 -8.520 3.260 36.232 1.00 34.54 C
ATOM 109 CD GLN A 264 -7.195 3.812 36.718 1.00 35.07 C
ATOM 110 OE1 GLN A 264 -6.587 4.604 36.042 1.00 41.66 O
ATOM 111 NE2 GLN A 264 -6.762 3.406 37.881 1.00 36.12 N
ATOM 112 N GLY A 265 -12.765 4.770 34.204 1.00 29.97 N
ATOM 113 CA GLY A 265 -13.581 5.753 33.494 1.00 31.41 C
ATOM 114 C GLY A 265 -13.610 5.575 32.005 1.00 33.21 C
ATOM 115 O GLY A 265 -14.210 6.378 31.307 1.00 33.70 O
ATOM 116 N ASN A 266 -12.973 4.519 31.492 1.00 32.08 N
ATOM 117 CA ASN A 266 -13.110 4.190 30.066 1.00 32.26 C
ATOM 118 C ASN A 266 -13.496 2.721 29.873 1.00 31.88 C
ATOM 119 O ASN A 266 -13.340 1.899 30.773 1.00 33.54 O
ATOM 120 CB ASN A 266 -11.837 4.536 29.309 1.00 30.50 C
ATOM 121 CG ASN A 266 -11.510 6.023 29.362 1.00 29.62 C
ATOM 122 OD1 ASN A 266 -12.194 6.834 28.777 1.00 32.80 O
ATOM 123 ND2 ASN A 266 -10.426 6.354 29.982 1.00 29.45 N
ATOM 124 N CYS A 267 -13.996 2.442 28.682 1.00 30.80 N
ATOM 125 CA CYS A 267 -14.450 1.154 28.240 1.00 29.40 C
ATOM 126 C CYS A 267 -13.470 0.661 27.186 1.00 32.34 C
ATOM 127 O CYS A 267 -13.050 1.444 26.293 1.00 32.58 O
ATOM 128 CB CYS A 267 -15.809 1.324 27.585 1.00 32.35 C
ATOM 129 SG CYS A 267 -17.015 2.038 28.717 1.00 38.22 S
ATOM 130 N TYR A 268 -13.123 -0.621 27.275 1.00 29.03 N
ATOM 131 CA TYR A 268 -12.189 -1.242 26.358 1.00 30.43 C
ATOM 132 C TYR A 268 -12.762 -2.475 25.758 1.00 31.34 C
ATOM 133 O TYR A 268 -13.357 -3.304 26.447 1.00 29.76 O
ATOM 134 CB TYR A 268 -10.913 -1.645 27.084 1.00 28.98 C
ATOM 135 CG TYR A 268 -10.208 -0.456 27.653 1.00 28.35 C
ATOM 136 CD1 TYR A 268 -10.635 0.107 28.864 1.00 28.27 C
ATOM 137 CD2 TYR A 268 -9.185 0.161 26.965 1.00 25.78 C
ATOM 138 CE1 TYR A 268 -10.012 1.209 29.401 1.00 27.13 C
ATOM 139 CE2 TYR A 268 -8.536 1.279 27.492 1.00 26.57 C
ATOM 140 CZ TYR A 268 -8.960 1.810 28.711 1.00 29.06 C
ATOM 141 OH TYR A 268 -8.340 2.925 29.274 1.00 27.40 O
ATOM 142 N PHE A 269 -12.560 -2.619 24.460 1.00 30.36 N
ATOM 143 CA PHE A 269 -12.896 -3.842 23.789 1.00 30.34 C
ATOM 144 C PHE A 269 -11.650 -4.596 23.366 1.00 29.54 C
ATOM 145 O PHE A 269 -10.797 -4.037 22.689 1.00 24.37 O
ATOM 146 CB PHE A 269 -13.761 -3.510 22.574 1.00 36.36 C
ATOM 147 CG PHE A 269 -14.158 -4.705 21.792 1.00 38.75 C
ATOM 148 CD1 PHE A 269 -15.200 -5.524 22.239 1.00 39.90 C
ATOM 149 CD2 PHE A 269 -13.484 -5.028 20.615 1.00 39.95 C
ATOM 150 CE1 PHE A 269 -15.552 -6.669 21.553 1.00 38.62 C
ATOM 151 CE2 PHE A 269 -13.851 -6.161 19.917 1.00 43.12 C
ATOM 152 CZ PHE A 269 -14.886 -6.984 20.397 1.00 40.88 C
ATOM 153 N MET A 270 -11.571 -5.878 23.725 1.00 30.47 N
ATOM 154 CA MET A 270 -10.424 -6.697 23.409 1.00 32.55 C
ATOM 155 C MET A 270 -10.888 -7.611 22.305 1.00 32.18 C
ATOM 156 O MET A 270 -11.827 -8.386 22.466 1.00 30.44 O
ATOM 157 CB MET A 270 -9.989 -7.544 24.598 1.00 39.59 C
ATOM 158 CG MET A 270 -10.139 -6.898 25.960 1.00 49.83 C
ATOM 159 SD MET A 270 -9.128 -5.447 26.243 1.00 51.03 S
ATOM 160 CE MET A 270 -9.776 -4.985 27.850 1.00 50.74 C
ATOM 161 N SER A 271 -10.282 -7.520 21.135 1.00 29.49 N
ATOM 162 CA SER A 271 -10.792 -8.316 20.048 1.00 26.91 C
ATOM 163 C SER A 271 -10.465 -9.779 20.307 1.00 26.55 C
ATOM 164 O SER A 271 -9.476 -10.094 20.993 1.00 26.15 O
ATOM 165 CB SER A 271 -10.177 -7.841 18.721 1.00 27.26 C
ATOM 166 OG SER A 271 -8.938 -8.436 18.534 1.00 23.86 O
ATOM 167 N ASN A 272 -11.293 -10.676 19.785 1.00 29.02 N
ATOM 168 CA AASN A 272 -10.964 -12.092 19.761 0.50 31.40 C
ATOM 169 CA BASN A 272 -10.912 -12.096 19.764 0.50 32.71 C
ATOM 170 C ASN A 272 -10.601 -12.570 18.344 1.00 32.11 C
ATOM 171 O ASN A 272 -10.615 -13.772 18.061 1.00 32.53 O
ATOM 172 CB AASN A 272 -12.100 -12.916 20.384 0.50 32.17 C
ATOM 173 CB BASN A 272 -11.944 -13.026 20.426 0.50 35.24 C
ATOM 174 CG AASN A 272 -12.149 -12.764 21.897 0.50 31.28 C
ATOM 175 CG BASN A 272 -11.324 -14.349 20.879 0.50 36.14 C
ATOM 176 OD1AASN A 272 -11.132 -12.894 22.565 0.50 30.71 O
ATOM 177 OD1BASN A 272 -10.403 -14.372 21.696 0.50 39.32 O
ATOM 178 ND2AASN A 272 -13.313 -12.438 22.429 0.50 31.10 N
ATOM 179 ND2BASN A 272 -11.817 -15.453 20.337 0.50 37.07 N
ATOM 180 N SER A 273 -10.262 -11.638 17.472 1.00 33.89 N
ATOM 181 CA SER A 273 -9.802 -11.970 16.107 1.00 36.56 C
ATOM 182 C SER A 273 -8.745 -10.980 15.646 1.00 34.99 C
ATOM 183 O SER A 273 -8.472 -9.967 16.316 1.00 29.35 O
ATOM 184 CB SER A 273 -10.973 -11.994 15.109 1.00 40.18 C
ATOM 185 OG SER A 273 -11.502 -10.697 14.892 1.00 45.00 O
ATOM 186 N GLN A 274 -8.154 -11.267 14.486 1.00 34.93 N
ATOM 187 CA GLN A 274 -6.973 -10.531 14.067 1.00 34.09 C
ATOM 188 C GLN A 274 -7.232 -9.755 12.793 1.00 32.35 C
ATOM 189 O GLN A 274 -7.962 -10.190 11.922 1.00 34.08 O
ATOM 190 CB GLN A 274 -5.781 -11.466 13.894 1.00 33.86 C
ATOM 191 CG GLN A 274 -5.542 -12.442 15.039 1.00 32.70 C
ATOM 192 CD GLN A 274 -4.885 -13.735 14.574 1.00 30.00 C
ATOM 193 OE1 GLN A 274 -3.689 -13.918 14.727 1.00 32.58 O
ATOM 194 NE2 GLN A 274 -5.655 -14.606 13.986 1.00 27.01 N
ATOM 195 N ARG A 275 -6.646 -8.568 12.742 1.00 31.83 N
ATOM 196 CA ARG A 275 -6.814 -7.606 11.664 1.00 30.89 C
ATOM 197 C ARG A 275 -5.542 -6.801 11.528 1.00 30.47 C
ATOM 198 O ARG A 275 -4.820 -6.617 12.519 1.00 29.79 O
ATOM 199 CB ARG A 275 -7.911 -6.642 12.001 1.00 33.05 C
ATOM 200 CG ARG A 275 -9.277 -7.246 11.795 1.00 36.10 C
ATOM 201 CD ARG A 275 -10.286 -6.157 11.959 1.00 38.40 C
ATOM 202 NE ARG A 275 -11.644 -6.630 11.716 1.00 41.82 N
ATOM 203 CZ ARG A 275 -12.582 -5.919 11.090 1.00 41.82 C
ATOM 204 NH1 ARG A 275 -12.335 -4.680 10.611 1.00 39.11 N
ATOM 205 NH2 ARG A 275 -13.775 -6.466 10.938 1.00 43.47 N
ATOM 206 N ASN A 276 -5.236 -6.348 10.315 1.00 28.68 N
ATOM 207 CA ASN A 276 -4.154 -5.420 10.165 1.00 29.23 C
ATOM 208 C ASN A 276 -4.560 -4.125 10.871 1.00 29.75 C
ATOM 209 O ASN A 276 -5.684 -3.993 11.369 1.00 24.56 O
ATOM 210 CB ASN A 276 -3.713 -5.209 8.690 1.00 34.22 C
ATOM 211 CG ASN A 276 -4.807 -4.672 7.793 1.00 32.97 C
ATOM 212 OD1 ASN A 276 -5.451 -3.671 8.094 1.00 35.56 O
ATOM 213 ND2 ASN A 276 -5.014 -5.342 6.669 1.00 38.65 N
ATOM 214 N TRP A 277 -3.599 -3.214 10.971 1.00 29.43 N
ATOM 215 CA TRP A 277 -3.732 -2.037 11.804 1.00 29.72 C
ATOM 216 C TRP A 277 -4.810 -1.096 11.233 1.00 29.66 C
ATOM 217 O TRP A 277 -5.641 -0.576 11.981 1.00 29.35 O
ATOM 218 CB TRP A 277 -2.352 -1.363 11.928 1.00 30.11 C
ATOM 219 CG TRP A 277 -2.269 -0.194 12.894 1.00 31.36 C
ATOM 220 CD1 TRP A 277 -2.006 -0.259 14.225 1.00 31.37 C
ATOM 221 CD2 TRP A 277 -2.405 1.207 12.588 1.00 31.92 C
ATOM 222 NE1 TRP A 277 -1.976 0.988 14.763 1.00 32.06 N
ATOM 223 CE2 TRP A 277 -2.230 1.909 13.793 1.00 31.77 C
ATOM 224 CE3 TRP A 277 -2.671 1.925 11.421 1.00 31.81 C
ATOM 225 CZ2 TRP A 277 -2.312 3.300 13.876 1.00 33.06 C
ATOM 226 CZ3 TRP A 277 -2.740 3.317 11.497 1.00 33.56 C
ATOM 227 CH2 TRP A 277 -2.558 3.987 12.711 1.00 32.89 C
ATOM 228 N HIS A 278 -4.791 -0.854 9.920 1.00 29.30 N
ATOM 229 CA HIS A 278 -5.771 0.051 9.315 1.00 27.39 C
ATOM 230 C HIS A 278 -7.152 -0.541 9.441 1.00 28.91 C
ATOM 231 O HIS A 278 -8.118 0.194 9.691 1.00 27.74 O
ATOM 232 CB HIS A 278 -5.485 0.318 7.840 1.00 30.61 C
ATOM 233 CG HIS A 278 -4.054 0.581 7.558 1.00 28.98 C
ATOM 234 ND1 HIS A 278 -3.514 1.843 7.615 1.00 30.40 N
ATOM 235 CD2 HIS A 278 -3.042 -0.261 7.248 1.00 33.63 C
ATOM 236 CE1 HIS A 278 -2.221 1.763 7.365 1.00 33.15 C
ATOM 237 NE2 HIS A 278 -1.914 0.502 7.120 1.00 33.09 N
ATOM 238 N ASP A 279 -7.294 -1.856 9.285 1.00 26.63 N
ATOM 239 CA ASP A 279 -8.667 -2.425 9.471 1.00 29.91 C
ATOM 240 C ASP A 279 -9.124 -2.456 10.962 1.00 30.69 C
ATOM 241 O ASP A 279 -10.345 -2.529 11.248 1.00 27.28 O
ATOM 242 CB ASP A 279 -8.807 -3.807 8.811 1.00 35.05 C
ATOM 243 CG ASP A 279 -8.744 -3.735 7.288 1.00 36.32 C
ATOM 244 OD1 ASP A 279 -8.972 -2.654 6.705 1.00 49.61 O
ATOM 245 OD2 ASP A 279 -8.502 -4.760 6.654 1.00 42.68 O
ATOM 246 N SER A 280 -8.147 -2.368 11.886 1.00 27.95 N
ATOM 247 CA SER A 280 -8.410 -2.316 13.344 1.00 29.48 C
ATOM 248 C SER A 280 -8.910 -0.907 13.742 1.00 32.15 C
ATOM 249 O SER A 280 -9.779 -0.754 14.641 1.00 31.58 O
ATOM 250 CB SER A 280 -7.149 -2.667 14.128 1.00 26.19 C
ATOM 251 OG SER A 280 -6.772 -4.014 13.940 1.00 23.89 O
ATOM 252 N ILE A 281 -8.350 0.100 13.067 1.00 32.01 N
ATOM 253 CA ILE A 281 -8.836 1.465 13.142 1.00 34.69 C
ATOM 254 C ILE A 281 -10.310 1.519 12.737 1.00 37.10 C
ATOM 255 O ILE A 281 -11.138 2.114 13.432 1.00 39.93 O
ATOM 256 CB ILE A 281 -8.097 2.449 12.199 1.00 35.78 C
ATOM 257 CG1 ILE A 281 -6.617 2.609 12.578 1.00 37.80 C
ATOM 258 CG2 ILE A 281 -8.783 3.821 12.221 1.00 32.72 C
ATOM 259 CD1 ILE A 281 -6.344 3.620 13.672 1.00 40.24 C
ATOM 260 N THR A 282 -10.607 0.937 11.593 1.00 34.76 N
ATOM 261 CA THR A 282 -11.972 0.877 11.073 1.00 35.30 C
ATOM 262 C THR A 282 -12.941 0.185 12.050 1.00 33.39 C
ATOM 263 O THR A 282 -14.006 0.714 12.326 1.00 37.22 O
ATOM 264 CB THR A 282 -11.991 0.204 9.678 1.00 37.69 C
ATOM 265 OG1 THR A 282 -11.420 1.100 8.726 1.00 38.86 O
ATOM 266 CG2 THR A 282 -13.391 -0.113 9.215 1.00 37.25 C
ATOM 267 N ALA A 283 -12.585 -0.997 12.535 1.00 29.22 N
ATOM 268 CA ALA A 283 -13.410 -1.719 13.483 1.00 29.64 C
ATOM 269 C ALA A 283 -13.746 -0.874 14.738 1.00 31.69 C
ATOM 270 O ALA A 283 -14.907 -0.803 15.143 1.00 34.09 O
ATOM 271 CB ALA A 283 -12.747 -3.024 13.884 1.00 27.15 C
ATOM 272 N CYS A 284 -12.757 -0.185 15.301 1.00 29.89 N
ATOM 273 CA CYS A 284 -12.979 0.615 16.478 1.00 31.76 C
ATOM 274 C CYS A 284 -13.959 1.738 16.190 1.00 36.91 C
ATOM 275 O CYS A 284 -14.899 1.918 16.972 1.00 33.72 O
ATOM 276 CB CYS A 284 -11.669 1.148 17.063 1.00 31.55 C
ATOM 277 SG CYS A 284 -10.663 -0.171 17.755 1.00 27.37 S
ATOM 278 N LYS A 285 -13.773 2.442 15.062 1.00 36.71 N
ATOM 279 CA LYS A 285 -14.707 3.508 14.620 1.00 42.42 C
ATOM 280 C LYS A 285 -16.132 3.080 14.290 1.00 39.03 C
ATOM 281 O LYS A 285 -17.033 3.857 14.442 1.00 48.48 O
ATOM 282 CB LYS A 285 -14.157 4.241 13.408 1.00 44.95 C
ATOM 283 CG LYS A 285 -13.220 5.386 13.735 1.00 45.99 C
ATOM 284 CD LYS A 285 -12.371 5.651 12.507 1.00 52.93 C
ATOM 285 CE LYS A 285 -11.644 6.976 12.564 1.00 53.14 C
ATOM 286 NZ LYS A 285 -10.728 7.000 11.388 1.00 56.56 N
ATOM 287 N GLU A 286 -16.328 1.849 13.854 1.00 44.02 N
ATOM 288 CA GLU A 286 -17.674 1.306 13.638 1.00 51.30 C
ATOM 289 C GLU A 286 -18.457 1.032 14.939 1.00 52.94 C
ATOM 290 O GLU A 286 -19.653 0.703 14.909 1.00 51.59 O
ATOM 291 CB GLU A 286 -17.603 0.046 12.769 1.00 56.15 C
ATOM 292 CG GLU A 286 -17.452 0.414 11.301 1.00 66.76 C
ATOM 293 CD GLU A 286 -17.137 -0.756 10.408 1.00 73.50 C
ATOM 294 OE1 GLU A 286 -17.068 -0.541 9.181 1.00 84.98 O
ATOM 295 OE2 GLU A 286 -16.935 -1.875 10.922 1.00 78.96 O
ATOM 296 N VAL A 287 -17.788 1.168 16.078 1.00 47.73 N
ATOM 297 CA VAL A 287 -18.455 1.017 17.370 1.00 43.24 C
ATOM 298 C VAL A 287 -18.253 2.260 18.221 1.00 40.18 C
ATOM 299 O VAL A 287 -18.301 2.186 19.423 1.00 40.99 O
ATOM 300 CB VAL A 287 -18.021 -0.288 18.096 1.00 42.83 C
ATOM 301 CG1 VAL A 287 -18.548 -1.499 17.351 1.00 41.95 C
ATOM 302 CG2 VAL A 287 -16.501 -0.402 18.253 1.00 42.01 C
ATOM 303 N GLY A 288 -18.045 3.406 17.570 1.00 37.85 N
ATOM 304 CA GLY A 288 -17.878 4.685 18.254 1.00 35.72 C
ATOM 305 C GLY A 288 -16.678 4.749 19.168 1.00 34.34 C
ATOM 306 O GLY A 288 -16.714 5.374 20.231 1.00 34.98 O
ATOM 307 N ALA A 289 -15.599 4.084 18.781 1.00 31.98 N
ATOM 308 CA ALA A 289 -14.407 4.045 19.628 1.00 29.37 C
ATOM 309 C ALA A 289 -13.140 4.316 18.820 1.00 30.06 C
ATOM 310 O ALA A 289 -13.178 4.496 17.601 1.00 33.53 O
ATOM 311 CB ALA A 289 -14.304 2.692 20.328 1.00 29.41 C
ATOM 312 N GLN A 290 -12.019 4.257 19.514 1.00 28.28 N
ATOM 313 CA AGLN A 290 -10.743 4.533 18.930 0.50 28.42 C
ATOM 314 CA BGLN A 290 -10.744 4.546 18.916 0.50 30.94 C
ATOM 315 C GLN A 290 -9.763 3.419 19.238 1.00 28.80 C
ATOM 316 O GLN A 290 -9.776 2.874 20.327 1.00 29.85 O
ATOM 317 CB AGLN A 290 -10.227 5.829 19.526 0.50 27.72 C
ATOM 318 CB BGLN A 290 -10.281 5.949 19.384 0.50 33.62 C
ATOM 319 CG AGLN A 290 -9.371 6.633 18.585 0.50 25.13 C
ATOM 320 CG BGLN A 290 -8.828 6.124 19.812 0.50 35.18 C
ATOM 321 CD AGLN A 290 -9.207 8.035 19.099 0.50 23.90 C
ATOM 322 CD BGLN A 290 -8.681 6.471 21.291 0.50 35.51 C
ATOM 323 OE1AGLN A 290 -8.779 8.238 20.222 0.50 22.59 O
ATOM 324 OE1BGLN A 290 -8.584 5.594 22.153 0.50 29.70 O
ATOM 325 NE2AGLN A 290 -9.558 9.002 18.286 0.50 24.07 N
ATOM 326 NE2BGLN A 290 -8.619 7.774 21.579 0.50 34.28 N
ATOM 327 N LEU A 291 -8.921 3.073 18.268 1.00 27.59 N
ATOM 328 CA LEU A 291 -7.882 2.092 18.474 1.00 27.99 C
ATOM 329 C LEU A 291 -7.023 2.684 19.582 1.00 28.47 C
ATOM 330 O LEU A 291 -6.686 3.872 19.544 1.00 26.52 O
ATOM 331 CB LEU A 291 -7.094 1.848 17.194 1.00 29.53 C
ATOM 332 CG LEU A 291 -5.971 0.799 17.257 1.00 28.19 C
ATOM 333 CD1 LEU A 291 -6.521 -0.576 17.533 1.00 27.00 C
ATOM 334 CD2 LEU A 291 -5.161 0.827 15.958 1.00 26.14 C
ATOM 335 N VAL A 292 -6.719 1.865 20.581 1.00 27.09 N
ATOM 336 CA VAL A 292 -6.429 2.386 21.922 1.00 31.08 C
ATOM 337 C VAL A 292 -5.233 3.361 22.053 1.00 30.34 C
ATOM 338 O VAL A 292 -4.082 3.039 21.750 1.00 29.65 O
ATOM 339 CB VAL A 292 -6.314 1.256 22.975 1.00 29.75 C
ATOM 340 CG1 VAL A 292 -5.131 0.357 22.709 1.00 27.50 C
ATOM 341 CG2 VAL A 292 -6.231 1.848 24.381 1.00 31.05 C
ATOM 342 N VAL A 293 -5.563 4.555 22.518 1.00 28.09 N
ATOM 343 CA VAL A 293 -4.611 5.608 22.805 1.00 27.59 C
ATOM 344 C VAL A 293 -4.379 5.586 24.314 1.00 28.88 C
ATOM 345 O VAL A 293 -5.333 5.671 25.108 1.00 25.07 O
ATOM 346 CB VAL A 293 -5.144 7.000 22.336 1.00 29.32 C
ATOM 347 CG1 VAL A 293 -4.145 8.121 22.644 1.00 29.96 C
ATOM 348 CG2 VAL A 293 -5.433 6.966 20.833 1.00 29.92 C
ATOM 349 N ILE A 294 -3.115 5.440 24.702 1.00 28.27 N
ATOM 350 CA ILE A 294 -2.760 5.363 26.087 1.00 30.35 C
ATOM 351 C ILE A 294 -2.376 6.731 26.642 1.00 35.61 C
ATOM 352 O ILE A 294 -1.528 7.421 26.074 1.00 31.12 O
ATOM 353 CB ILE A 294 -1.589 4.403 26.291 1.00 29.68 C
ATOM 354 CG1 ILE A 294 -1.925 3.064 25.650 1.00 27.74 C
ATOM 355 CG2 ILE A 294 -1.325 4.237 27.777 1.00 29.74 C
ATOM 356 CD1 ILE A 294 -0.798 2.091 25.637 1.00 27.22 C
ATOM 357 N LYS A 295 -3.001 7.083 27.769 1.00 38.52 N
ATOM 358 CA LYS A 295 -2.867 8.388 28.412 1.00 37.07 C
ATOM 359 C LYS A 295 -2.155 8.336 29.763 1.00 37.90 C
ATOM 360 O LYS A 295 -1.765 9.365 30.227 1.00 37.35 O
ATOM 361 CB LYS A 295 -4.256 9.027 28.632 1.00 38.95 C
ATOM 362 CG LYS A 295 -5.071 9.370 27.389 1.00 38.77 C
ATOM 363 CD LYS A 295 -4.310 10.342 26.516 1.00 42.42 C
ATOM 364 CE LYS A 295 -5.116 10.846 25.335 1.00 43.81 C
ATOM 365 NZ LYS A 295 -4.182 11.427 24.311 1.00 48.45 N
ATOM 366 N SER A 296 -2.006 7.169 30.409 1.00 36.33 N
ATOM 367 CA SER A 296 -1.362 7.103 31.724 1.00 35.30 C
ATOM 368 C SER A 296 -0.594 5.807 31.981 1.00 37.71 C
ATOM 369 O SER A 296 -0.852 4.786 31.334 1.00 37.68 O
ATOM 370 CB SER A 296 -2.413 7.279 32.814 1.00 35.57 C
ATOM 371 OG SER A 296 -3.243 6.138 32.888 1.00 33.31 O
ATOM 372 N ALA A 297 0.315 5.840 32.961 1.00 34.25 N
ATOM 373 CA ALA A 297 1.051 4.644 33.358 1.00 32.65 C
ATOM 374 C ALA A 297 0.156 3.521 33.821 1.00 32.84 C
ATOM 375 O ALA A 297 0.445 2.380 33.534 1.00 34.23 O
ATOM 376 CB ALA A 297 2.094 4.947 34.425 1.00 31.54 C
ATOM 377 N GLU A 298 -0.926 3.832 34.517 1.00 35.15 N
ATOM 378 CA AGLU A 298 -1.807 2.793 35.078 0.70 39.36 C
ATOM 379 CA BGLU A 298 -1.784 2.787 35.069 0.30 36.62 C
ATOM 380 C GLU A 298 -2.550 2.109 33.924 1.00 37.53 C
ATOM 381 O GLU A 298 -2.781 0.911 33.947 1.00 34.64 O
ATOM 382 CB AGLU A 298 -2.829 3.346 36.102 0.70 42.78 C
ATOM 383 CB BGLU A 298 -2.733 3.370 36.121 0.30 37.33 C
ATOM 384 CG AGLU A 298 -2.378 4.521 36.971 0.70 49.04 C
ATOM 385 CG BGLU A 298 -2.037 4.230 37.172 0.30 38.93 C
ATOM 386 CD AGLU A 298 -2.604 5.887 36.312 0.70 49.86 C
ATOM 387 CD BGLU A 298 -1.816 3.504 38.473 0.30 38.08 C
ATOM 388 OE1AGLU A 298 -1.601 6.649 36.214 0.70 45.63 O
ATOM 389 OE1BGLU A 298 -0.665 3.483 38.969 0.30 37.50 O
ATOM 390 OE2AGLU A 298 -3.766 6.175 35.873 0.70 45.58 O
ATOM 391 OE2BGLU A 298 -2.806 2.959 38.990 0.30 38.01 O
ATOM 392 N GLU A 299 -2.897 2.903 32.907 1.00 35.39 N
ATOM 393 CA GLU A 299 -3.606 2.424 31.753 1.00 35.83 C
ATOM 394 C GLU A 299 -2.699 1.507 30.923 1.00 33.41 C
ATOM 395 O GLU A 299 -3.079 0.385 30.577 1.00 28.00 O
ATOM 396 CB GLU A 299 -4.108 3.570 30.920 1.00 35.91 C
ATOM 397 CG GLU A 299 -5.065 3.102 29.832 1.00 37.11 C
ATOM 398 CD GLU A 299 -5.509 4.227 28.913 1.00 35.59 C
ATOM 399 OE1 GLU A 299 -6.475 4.037 28.149 1.00 37.55 O
ATOM 400 OE2 GLU A 299 -4.919 5.321 28.970 1.00 35.27 O
ATOM 401 N GLN A 300 -1.483 1.969 30.709 1.00 32.73 N
ATOM 402 CA GLN A 300 -0.452 1.168 30.050 1.00 34.25 C
ATOM 403 C GLN A 300 -0.246 -0.168 30.747 1.00 35.83 C
ATOM 404 O GLN A 300 -0.058 -1.194 30.090 1.00 36.63 O
ATOM 405 CB GLN A 300 0.844 1.933 30.016 1.00 32.00 C
ATOM 406 CG GLN A 300 2.106 1.101 29.955 1.00 32.84 C
ATOM 407 CD GLN A 300 2.228 0.224 28.743 1.00 31.25 C
ATOM 408 OE1 GLN A 300 1.448 0.299 27.796 1.00 30.85 O
ATOM 409 NE2 GLN A 300 3.210 -0.642 28.781 1.00 33.28 N
ATOM 410 N ASN A 301 -0.261 -0.149 32.074 1.00 35.76 N
ATOM 411 CA ASN A 301 0.010 -1.360 32.849 1.00 36.50 C
ATOM 412 C ASN A 301 -1.111 -2.373 32.659 1.00 34.40 C
ATOM 413 O ASN A 301 -0.843 -3.572 32.490 1.00 33.60 O
ATOM 414 CB ASN A 301 0.162 -1.053 34.329 1.00 38.81 C
ATOM 415 CG ASN A 301 1.486 -0.396 34.664 1.00 42.68 C
ATOM 416 OD1 ASN A 301 2.453 -0.425 33.892 1.00 41.66 O
ATOM 417 ND2 ASN A 301 1.526 0.218 35.834 1.00 41.40 N
ATOM 418 N PHE A 302 -2.342 -1.856 32.705 1.00 28.32 N
ATOM 419 CA PHE A 302 -3.530 -2.615 32.422 1.00 29.46 C
ATOM 420 C PHE A 302 -3.532 -3.233 31.007 1.00 30.77 C
ATOM 421 O PHE A 302 -3.800 -4.422 30.859 1.00 34.56 O
ATOM 422 CB PHE A 302 -4.734 -1.710 32.641 1.00 31.37 C
ATOM 423 CG PHE A 302 -6.017 -2.244 32.129 1.00 29.02 C
ATOM 424 CD1 PHE A 302 -6.643 -3.293 32.770 1.00 30.59 C
ATOM 425 CD2 PHE A 302 -6.624 -1.679 31.026 1.00 32.89 C
ATOM 426 CE1 PHE A 302 -7.862 -3.789 32.312 1.00 29.07 C
ATOM 427 CE2 PHE A 302 -7.842 -2.189 30.548 1.00 33.54 C
ATOM 428 CZ PHE A 302 -8.445 -3.256 31.200 1.00 29.35 C
ATOM 429 N LEU A 303 -3.242 -2.430 29.985 1.00 27.42 N
ATOM 430 CA LEU A 303 -3.304 -2.880 28.605 1.00 27.19 C
ATOM 431 C LEU A 303 -2.226 -3.928 28.336 1.00 24.48 C
ATOM 432 O LEU A 303 -2.503 -4.962 27.768 1.00 28.63 O
ATOM 433 CB LEU A 303 -3.233 -1.671 27.636 1.00 26.62 C
ATOM 434 CG LEU A 303 -4.434 -0.724 27.793 1.00 26.25 C
ATOM 435 CD1 LEU A 303 -4.100 0.638 27.235 1.00 27.63 C
ATOM 436 CD2 LEU A 303 -5.700 -1.266 27.147 1.00 27.56 C
ATOM 437 N GLN A 304 -1.003 -3.636 28.763 1.00 24.37 N
ATOM 438 CA GLN A 304 0.126 -4.510 28.608 1.00 23.29 C
ATOM 439 C GLN A 304 -0.123 -5.892 29.212 1.00 26.14 C
ATOM 440 O GLN A 304 0.261 -6.900 28.627 1.00 24.64 O
ATOM 441 CB GLN A 304 1.371 -3.912 29.232 1.00 21.89 C
ATOM 442 CG GLN A 304 2.612 -4.603 28.751 1.00 23.18 C
ATOM 443 CD GLN A 304 2.986 -4.281 27.306 1.00 25.53 C
ATOM 444 OE1 GLN A 304 3.032 -3.117 26.941 1.00 29.64 O
ATOM 445 NE2 GLN A 304 3.309 -5.310 26.494 1.00 25.15 N
ATOM 446 N LEU A 305 -0.751 -5.909 30.377 1.00 26.42 N
ATOM 447 CA LEU A 305 -1.109 -7.131 31.037 1.00 30.32 C
ATOM 448 C LEU A 305 -1.944 -8.045 30.178 1.00 30.56 C
ATOM 449 O LEU A 305 -1.643 -9.222 30.104 1.00 32.00 O
ATOM 450 CB LEU A 305 -1.904 -6.800 32.298 1.00 36.52 C
ATOM 451 CG LEU A 305 -2.420 -8.011 33.063 1.00 41.28 C
ATOM 452 CD1 LEU A 305 -1.243 -8.705 33.731 1.00 45.05 C
ATOM 453 CD2 LEU A 305 -3.466 -7.565 34.065 1.00 43.72 C
ATOM 454 N GLN A 306 -2.990 -7.490 29.546 1.00 32.43 N
ATOM 455 CA GLN A 306 -3.848 -8.222 28.625 1.00 34.37 C
ATOM 456 C GLN A 306 -3.052 -9.063 27.649 1.00 35.79 C
ATOM 457 O GLN A 306 -3.436 -10.194 27.390 1.00 28.99 O
ATOM 458 CB GLN A 306 -4.772 -7.317 27.791 1.00 36.18 C
ATOM 459 CG GLN A 306 -5.570 -6.283 28.559 1.00 38.50 C
ATOM 460 CD GLN A 306 -6.268 -6.868 29.764 1.00 41.30 C
ATOM 461 OE1 GLN A 306 -7.134 -7.697 29.617 1.00 40.21 O
ATOM 462 NE2 GLN A 306 -5.900 -6.420 30.962 1.00 45.44 N
ATOM 463 N SER A 307 -1.978 -8.481 27.091 1.00 34.80 N
ATOM 464 CA SER A 307 -1.151 -9.142 26.088 1.00 35.39 C
ATOM 465 C SER A 307 -0.049 -10.009 26.697 1.00 32.24 C
ATOM 466 O SER A 307 0.233 -11.072 26.207 1.00 31.87 O
ATOM 467 CB SER A 307 -0.499 -8.095 25.157 1.00 39.07 C
ATOM 468 OG SER A 307 -1.414 -7.696 24.157 1.00 46.44 O
ATOM 469 N SER A 308 0.595 -9.565 27.746 1.00 32.19 N
ATOM 470 CA SER A 308 1.668 -10.376 28.315 1.00 37.72 C
ATOM 471 C SER A 308 1.076 -11.686 28.863 1.00 37.81 C
ATOM 472 O SER A 308 1.669 -12.724 28.754 1.00 39.45 O
ATOM 473 CB SER A 308 2.450 -9.623 29.401 1.00 38.31 C
ATOM 474 OG SER A 308 1.635 -9.308 30.521 1.00 40.31 O
ATOM 475 N ARG A 309 -0.129 -11.626 29.396 1.00 39.52 N
ATOM 476 CA ARG A 309 -0.766 -12.793 30.011 1.00 42.16 C
ATOM 477 C ARG A 309 -1.410 -13.748 28.974 1.00 40.28 C
ATOM 478 O ARG A 309 -1.428 -14.953 29.138 1.00 41.20 O
ATOM 479 CB ARG A 309 -1.806 -12.287 31.005 1.00 43.10 C
ATOM 480 CG ARG A 309 -2.635 -13.346 31.678 1.00 46.37 C
ATOM 481 CD ARG A 309 -3.604 -12.690 32.652 1.00 49.33 C
ATOM 482 NE ARG A 309 -4.555 -11.814 31.965 1.00 50.16 N
ATOM 483 CZ ARG A 309 -5.431 -11.015 32.571 1.00 53.87 C
ATOM 484 NH1 ARG A 309 -5.486 -10.956 33.906 1.00 61.30 N
ATOM 485 NH2 ARG A 309 -6.246 -10.258 31.842 1.00 52.57 N
ATOM 486 N SER A 310 -1.975 -13.192 27.925 1.00 36.94 N
ATOM 487 CA SER A 310 -2.597 -13.974 26.921 1.00 33.64 C
ATOM 488 C SER A 310 -1.571 -14.442 25.879 1.00 34.08 C
ATOM 489 O SER A 310 -1.864 -15.314 25.118 1.00 31.57 O
ATOM 490 CB SER A 310 -3.609 -13.129 26.217 1.00 35.73 C
ATOM 491 OG SER A 310 -2.885 -12.197 25.463 1.00 38.20 O
ATOM 492 N ASN A 311 -0.368 -13.880 25.903 1.00 36.10 N
ATOM 493 CA ASN A 311 0.660 -14.094 24.880 1.00 37.77 C
ATOM 494 C ASN A 311 0.215 -13.730 23.469 1.00 34.19 C
ATOM 495 O ASN A 311 0.667 -14.363 22.505 1.00 38.17 O
ATOM 496 CB ASN A 311 1.148 -15.551 24.909 1.00 42.57 C
ATOM 497 CG ASN A 311 1.576 -15.994 26.286 1.00 44.23 C
ATOM 498 OD1 ASN A 311 2.623 -15.575 26.779 1.00 51.39 O
ATOM 499 ND2 ASN A 311 0.772 -16.868 26.920 1.00 50.21 N
ATOM 500 N ARG A 312 -0.671 -12.747 23.349 1.00 29.36 N
ATOM 501 CA ARG A 312 -1.136 -12.253 22.079 1.00 32.90 C
ATOM 502 C ARG A 312 -0.486 -10.909 21.643 1.00 31.33 C
ATOM 503 O ARG A 312 -0.237 -10.013 22.428 1.00 35.20 O
ATOM 504 CB ARG A 312 -2.658 -12.091 22.087 1.00 37.57 C
ATOM 505 CG ARG A 312 -3.497 -13.301 22.506 1.00 40.84 C
ATOM 506 CD ARG A 312 -3.295 -14.517 21.634 1.00 43.36 C
ATOM 507 NE ARG A 312 -4.095 -15.721 21.990 1.00 43.36 N
ATOM 508 CZ ARG A 312 -4.092 -16.845 21.263 1.00 40.52 C
ATOM 509 NH1 ARG A 312 -3.359 -16.886 20.142 1.00 36.29 N
ATOM 510 NH2 ARG A 312 -4.802 -17.928 21.652 1.00 40.14 N
ATOM 511 N PHE A 313 -0.198 -10.790 20.365 1.00 28.51 N
ATOM 512 CA PHE A 313 0.246 -9.533 19.798 1.00 25.87 C
ATOM 513 C PHE A 313 -0.976 -8.689 19.447 1.00 24.71 C
ATOM 514 O PHE A 313 -1.889 -9.156 18.762 1.00 26.69 O
ATOM 515 CB PHE A 313 1.055 -9.848 18.560 1.00 28.23 C
ATOM 516 CG PHE A 313 2.285 -10.668 18.849 1.00 29.16 C
ATOM 517 CD1 PHE A 313 3.061 -10.416 19.987 1.00 29.00 C
ATOM 518 CD2 PHE A 313 2.700 -11.662 17.963 1.00 30.76 C
ATOM 519 CE1 PHE A 313 4.209 -11.160 20.252 1.00 31.50 C
ATOM 520 CE2 PHE A 313 3.845 -12.404 18.223 1.00 30.07 C
ATOM 521 CZ PHE A 313 4.606 -12.156 19.363 1.00 30.24 C
ATOM 522 N THR A 314 -0.985 -7.451 19.929 1.00 23.25 N
ATOM 523 CA THR A 314 -2.161 -6.605 19.953 1.00 23.67 C
ATOM 524 C THR A 314 -1.828 -5.173 19.521 1.00 23.64 C
ATOM 525 O THR A 314 -0.888 -4.570 20.042 1.00 22.29 O
ATOM 526 CB THR A 314 -2.698 -6.563 21.405 1.00 24.65 C
ATOM 527 OG1 THR A 314 -2.841 -7.921 21.877 1.00 28.77 O
ATOM 528 CG2 THR A 314 -3.978 -5.788 21.499 1.00 23.14 C
ATOM 529 N TRP A 315 -2.579 -4.633 18.568 1.00 22.93 N
ATOM 530 CA TRP A 315 -2.288 -3.299 18.009 1.00 23.08 C
ATOM 531 C TRP A 315 -2.745 -2.269 19.012 1.00 25.97 C
ATOM 532 O TRP A 315 -3.764 -2.498 19.708 1.00 23.78 O
ATOM 533 CB TRP A 315 -3.116 -3.013 16.731 1.00 23.81 C
ATOM 534 CG TRP A 315 -2.692 -3.754 15.469 1.00 25.13 C
ATOM 535 CD1 TRP A 315 -3.455 -4.586 14.679 1.00 25.15 C
ATOM 536 CD2 TRP A 315 -1.418 -3.699 14.876 1.00 23.78 C
ATOM 537 NE1 TRP A 315 -2.686 -5.086 13.625 1.00 24.52 N
ATOM 538 CE2 TRP A 315 -1.444 -4.523 13.718 1.00 24.79 C
ATOM 539 CE3 TRP A 315 -0.220 -3.072 15.233 1.00 25.08 C
ATOM 540 CZ2 TRP A 315 -0.328 -4.691 12.914 1.00 24.98 C
ATOM 541 CZ3 TRP A 315 0.885 -3.235 14.425 1.00 24.67 C
ATOM 542 CH2 TRP A 315 0.821 -4.033 13.282 1.00 24.17 C
ATOM 543 N MET A 316 -2.049 -1.140 19.053 1.00 22.96 N
ATOM 544 CA MET A 316 -2.558 0.042 19.757 1.00 26.89 C
ATOM 545 C MET A 316 -2.605 1.164 18.727 1.00 26.57 C
ATOM 546 O MET A 316 -2.121 1.018 17.608 1.00 24.82 O
ATOM 547 CB MET A 316 -1.704 0.450 20.992 1.00 26.71 C
ATOM 548 CG MET A 316 -0.407 1.127 20.639 1.00 27.08 C
ATOM 549 SD MET A 316 0.870 1.244 21.912 1.00 27.55 S
ATOM 550 CE MET A 316 1.314 -0.464 22.188 1.00 29.47 C
ATOM 551 N GLY A 317 -3.188 2.288 19.127 1.00 26.53 N
ATOM 552 CA GLY A 317 -3.419 3.401 18.240 1.00 26.66 C
ATOM 553 C GLY A 317 -2.229 4.319 18.097 1.00 24.48 C
ATOM 554 O GLY A 317 -2.335 5.530 18.280 1.00 21.98 O
ATOM 555 N LEU A 318 -1.102 3.757 17.734 1.00 22.81 N
ATOM 556 CA LEU A 318 0.108 4.531 17.696 1.00 22.53 C
ATOM 557 C LEU A 318 0.849 4.172 16.418 1.00 23.01 C
ATOM 558 O LEU A 318 0.954 2.993 16.082 1.00 25.40 O
ATOM 559 CB LEU A 318 0.914 4.229 18.954 1.00 22.95 C
ATOM 560 CG LEU A 318 2.276 4.933 19.048 1.00 23.79 C
ATOM 561 CD1 LEU A 318 2.071 6.418 19.283 1.00 25.82 C
ATOM 562 CD2 LEU A 318 3.159 4.317 20.122 1.00 24.01 C
ATOM 563 N SER A 319 1.370 5.174 15.716 1.00 22.49 N
ATOM 564 CA SER A 319 2.043 4.969 14.424 1.00 25.69 C
ATOM 565 C SER A 319 3.004 6.071 14.049 1.00 25.74 C
ATOM 566 O SER A 319 3.025 7.154 14.651 1.00 24.68 O
ATOM 567 CB SER A 319 1.029 4.795 13.240 1.00 27.43 C
ATOM 568 OG SER A 319 0.691 6.045 12.696 1.00 29.05 O
ATOM 569 N ASP A 320 3.833 5.756 13.054 1.00 26.19 N
ATOM 570 CA ASP A 320 4.796 6.708 12.509 1.00 26.06 C
ATOM 571 C ASP A 320 4.749 6.591 11.007 1.00 29.97 C
ATOM 572 O ASP A 320 5.724 6.874 10.295 1.00 26.03 O
ATOM 573 CB ASP A 320 6.234 6.549 13.135 1.00 26.02 C
ATOM 574 CG ASP A 320 7.091 5.435 12.472 1.00 27.61 C
ATOM 575 OD1 ASP A 320 6.508 4.586 11.783 1.00 29.26 O
ATOM 576 OD2 ASP A 320 8.353 5.383 12.634 1.00 27.75 O
ATOM 577 N LEU A 321 3.562 6.189 10.545 1.00 32.94 N
ATOM 578 CA LEU A 321 3.226 6.139 9.150 1.00 32.82 C
ATOM 579 C LEU A 321 3.397 7.524 8.510 1.00 37.40 C
ATOM 580 O LEU A 321 3.895 7.641 7.384 1.00 35.52 O
ATOM 581 CB LEU A 321 1.762 5.752 8.983 1.00 30.87 C
ATOM 582 CG LEU A 321 1.383 4.287 8.963 1.00 30.75 C
ATOM 583 CD1 LEU A 321 -0.124 4.159 9.058 1.00 30.74 C
ATOM 584 CD2 LEU A 321 1.911 3.632 7.711 1.00 32.00 C
ATOM 585 N ASN A 322 2.934 8.567 9.181 1.00 33.78 N
ATOM 586 CA AASN A 322 2.939 9.886 8.564 0.70 37.22 C
ATOM 587 CA BASN A 322 2.937 9.868 8.538 0.30 35.94 C
ATOM 588 C ASN A 322 4.375 10.357 8.374 1.00 36.55 C
ATOM 589 O ASN A 322 4.754 10.781 7.310 1.00 36.68 O
ATOM 590 CB AASN A 322 2.154 10.910 9.392 0.70 35.71 C
ATOM 591 CB BASN A 322 2.035 10.862 9.273 0.30 34.71 C
ATOM 592 CG AASN A 322 1.991 12.238 8.671 0.70 37.60 C
ATOM 593 CG BASN A 322 0.563 10.623 8.978 0.30 34.84 C
ATOM 594 OD1AASN A 322 2.233 13.314 9.243 0.70 40.24 O
ATOM 595 OD1BASN A 322 0.208 9.684 8.263 0.30 34.80 O
ATOM 596 ND2AASN A 322 1.564 12.176 7.410 0.70 37.24 N
ATOM 597 ND2BASN A 322 -0.300 11.468 9.523 0.30 35.29 N
ATOM 598 N GLN A 323 5.176 10.259 9.419 1.00 37.01 N
ATOM 599 CA GLN A 323 6.550 10.726 9.338 1.00 39.77 C
ATOM 600 C GLN A 323 7.416 9.787 10.140 1.00 35.92 C
ATOM 601 O GLN A 323 7.265 9.656 11.384 1.00 36.23 O
ATOM 602 CB GLN A 323 6.679 12.174 9.851 1.00 39.80 C
ATOM 603 CG GLN A 323 8.112 12.726 9.957 1.00 45.23 C
ATOM 604 CD GLN A 323 8.947 12.659 8.656 1.00 54.46 C
ATOM 605 OE1 GLN A 323 8.503 13.075 7.563 1.00 55.98 O
ATOM 606 NE2 GLN A 323 10.180 12.141 8.782 1.00 55.90 N
ATOM 607 N GLU A 324 8.318 9.131 9.420 1.00 33.86 N
ATOM 608 CA GLU A 324 9.173 8.095 10.000 1.00 34.14 C
ATOM 609 C GLU A 324 9.929 8.624 11.205 1.00 32.87 C
ATOM 610 O GLU A 324 10.573 9.641 11.138 1.00 35.72 O
ATOM 611 CB GLU A 324 10.139 7.538 8.940 1.00 32.55 C
ATOM 612 CG GLU A 324 11.029 6.402 9.458 1.00 34.25 C
ATOM 613 CD GLU A 324 10.261 5.235 10.074 1.00 32.57 C
ATOM 614 OE1 GLU A 324 9.183 4.863 9.542 1.00 34.72 O
ATOM 615 OE2 GLU A 324 10.763 4.661 11.067 1.00 30.84 O
ATOM 616 N GLY A 325 9.826 7.948 12.331 1.00 32.56 N
ATOM 617 CA GLY A 325 10.486 8.431 13.524 1.00 30.65 C
ATOM 618 C GLY A 325 9.618 9.314 14.398 1.00 32.46 C
ATOM 619 O GLY A 325 9.947 9.558 15.562 1.00 38.18 O
ATOM 620 N THR A 326 8.504 9.791 13.877 1.00 30.76 N
ATOM 621 CA THR A 326 7.627 10.575 14.701 1.00 32.35 C
ATOM 622 C THR A 326 6.427 9.740 15.062 1.00 30.35 C
ATOM 623 O THR A 326 5.517 9.532 14.243 1.00 29.84 O
ATOM 624 CB THR A 326 7.132 11.866 13.997 1.00 35.16 C
ATOM 625 OG1 THR A 326 8.252 12.687 13.651 1.00 38.50 O
ATOM 626 CG2 THR A 326 6.205 12.643 14.924 1.00 33.60 C
ATOM 627 N TRP A 327 6.405 9.307 16.310 1.00 31.85 N
ATOM 628 CA TRP A 327 5.323 8.466 16.798 1.00 32.65 C
ATOM 629 C TRP A 327 4.175 9.313 17.297 1.00 31.86 C
ATOM 630 O TRP A 327 4.314 10.148 18.158 1.00 30.88 O
ATOM 631 CB TRP A 327 5.831 7.489 17.831 1.00 32.50 C
ATOM 632 CG TRP A 327 6.648 6.488 17.138 1.00 31.18 C
ATOM 633 CD1 TRP A 327 7.966 6.588 16.830 1.00 32.42 C
ATOM 634 CD2 TRP A 327 6.192 5.263 16.577 1.00 30.50 C
ATOM 635 NE1 TRP A 327 8.371 5.475 16.129 1.00 33.28 N
ATOM 636 CE2 TRP A 327 7.288 4.660 15.943 1.00 31.91 C
ATOM 637 CE3 TRP A 327 4.965 4.610 16.548 1.00 27.58 C
ATOM 638 CZ2 TRP A 327 7.183 3.447 15.311 1.00 31.93 C
ATOM 639 CZ3 TRP A 327 4.868 3.418 15.917 1.00 26.77 C
ATOM 640 CH2 TRP A 327 5.957 2.832 15.340 1.00 29.27 C
ATOM 641 N GLN A 328 3.021 9.050 16.729 1.00 33.54 N
ATOM 642 CA GLN A 328 1.872 9.885 16.937 1.00 34.00 C
ATOM 643 C GLN A 328 0.685 8.968 17.233 1.00 28.24 C
ATOM 644 O GLN A 328 0.487 8.012 16.529 1.00 26.63 O
ATOM 645 CB GLN A 328 1.665 10.675 15.662 1.00 32.99 C
ATOM 646 CG GLN A 328 0.661 11.796 15.798 1.00 39.80 C
ATOM 647 CD GLN A 328 0.570 12.638 14.546 1.00 41.24 C
ATOM 648 OE1 GLN A 328 1.425 12.544 13.657 1.00 42.54 O
ATOM 649 NE2 GLN A 328 -0.468 13.459 14.467 1.00 47.89 N
ATOM 650 N TRP A 329 -0.055 9.233 18.302 1.00 28.72 N
ATOM 651 CA TRP A 329 -1.311 8.502 18.598 1.00 26.90 C
ATOM 652 C TRP A 329 -2.369 8.884 17.540 1.00 27.08 C
ATOM 653 O TRP A 329 -2.288 9.946 16.956 1.00 23.80 O
ATOM 654 CB TRP A 329 -1.837 8.848 19.992 1.00 27.89 C
ATOM 655 CG TRP A 329 -0.900 8.490 21.057 1.00 29.95 C
ATOM 656 CD1 TRP A 329 -0.069 9.324 21.707 1.00 31.12 C
ATOM 657 CD2 TRP A 329 -0.684 7.187 21.619 1.00 30.62 C
ATOM 658 NE1 TRP A 329 0.678 8.635 22.614 1.00 31.52 N
ATOM 659 CE2 TRP A 329 0.306 7.321 22.598 1.00 30.50 C
ATOM 660 CE3 TRP A 329 -1.238 5.931 21.391 1.00 31.30 C
ATOM 661 CZ2 TRP A 329 0.771 6.245 23.354 1.00 30.08 C
ATOM 662 CZ3 TRP A 329 -0.772 4.854 22.137 1.00 32.00 C
ATOM 663 CH2 TRP A 329 0.226 5.022 23.104 1.00 31.88 C
ATOM 664 N VAL A 330 -3.338 8.013 17.291 1.00 25.07 N
ATOM 665 CA VAL A 330 -4.370 8.307 16.341 1.00 26.48 C
ATOM 666 C VAL A 330 -5.276 9.491 16.709 1.00 30.45 C
ATOM 667 O VAL A 330 -6.087 9.899 15.875 1.00 33.56 O
ATOM 668 CB VAL A 330 -5.293 7.097 16.069 1.00 27.23 C
ATOM 669 CG1 VAL A 330 -4.513 5.913 15.532 1.00 28.23 C
ATOM 670 CG2 VAL A 330 -6.096 6.714 17.316 1.00 25.81 C
ATOM 671 N ASP A 331 -5.182 10.022 17.927 1.00 29.93 N
ATOM 672 CA ASP A 331 -5.928 11.222 18.265 1.00 32.07 C
ATOM 673 C ASP A 331 -5.135 12.476 17.964 1.00 36.44 C
ATOM 674 O ASP A 331 -5.525 13.571 18.379 1.00 39.43 O
ATOM 675 CB ASP A 331 -6.430 11.215 19.732 1.00 31.95 C
ATOM 676 CG ASP A 331 -5.325 11.368 20.744 1.00 32.55 C
ATOM 677 OD1 ASP A 331 -4.133 11.447 20.370 1.00 35.35 O
ATOM 678 OD2 ASP A 331 -5.649 11.423 21.944 1.00 32.93 O
ATOM 679 N GLY A 332 -4.031 12.334 17.239 1.00 34.63 N
ATOM 680 CA GLY A 332 -3.224 13.474 16.848 1.00 34.31 C
ATOM 681 C GLY A 332 -2.090 13.804 17.800 1.00 35.59 C
ATOM 682 O GLY A 332 -1.154 14.491 17.434 1.00 36.92 O
ATOM 683 N SER A 333 -2.161 13.339 19.034 1.00 36.02 N
ATOM 684 CA SER A 333 -1.175 13.734 20.019 1.00 35.29 C
ATOM 685 C SER A 333 0.130 12.941 19.821 1.00 34.49 C
ATOM 686 O SER A 333 0.119 11.805 19.354 1.00 31.29 O
ATOM 687 CB SER A 333 -1.740 13.536 21.430 1.00 37.40 C
ATOM 688 OG SER A 333 -1.780 12.164 21.758 1.00 40.84 O
ATOM 689 N PRO A 334 1.264 13.562 20.145 1.00 36.10 N
ATOM 690 CA PRO A 334 2.561 12.923 20.027 1.00 34.15 C
ATOM 691 C PRO A 334 2.924 12.046 21.216 1.00 34.50 C
ATOM 692 O PRO A 334 2.411 12.215 22.321 1.00 32.77 O
ATOM 693 CB PRO A 334 3.524 14.103 19.938 1.00 36.53 C
ATOM 694 CG PRO A 334 2.827 15.214 20.656 1.00 36.50 C
ATOM 695 CD PRO A 334 1.377 15.014 20.390 1.00 34.73 C
ATOM 696 N LEU A 335 3.801 11.091 20.971 1.00 33.22 N
ATOM 697 CA LEU A 335 4.258 10.225 22.029 1.00 33.90 C
ATOM 698 C LEU A 335 5.108 11.011 23.002 1.00 32.89 C
ATOM 699 O LEU A 335 6.194 11.465 22.650 1.00 31.59 O
ATOM 700 CB LEU A 335 5.072 9.070 21.467 1.00 31.89 C
ATOM 701 CG LEU A 335 5.508 8.008 22.455 1.00 33.24 C
ATOM 702 CD1 LEU A 335 4.326 7.367 23.160 1.00 32.93 C
ATOM 703 CD2 LEU A 335 6.310 6.963 21.687 1.00 33.08 C
ATOM 704 N LEU A 336 4.631 11.126 24.238 1.00 32.84 N
ATOM 705 CA LEU A 336 5.374 11.835 25.268 1.00 33.89 C
ATOM 706 C LEU A 336 6.664 11.118 25.619 1.00 34.10 C
ATOM 707 O LEU A 336 6.688 9.883 25.650 1.00 33.75 O
ATOM 708 CB LEU A 336 4.530 11.978 26.539 1.00 35.47 C
ATOM 709 CG LEU A 336 3.207 12.728 26.427 1.00 37.74 C
ATOM 710 CD1 LEU A 336 2.496 12.758 27.774 1.00 37.38 C
ATOM 711 CD2 LEU A 336 3.428 14.148 25.930 1.00 41.30 C
ATOM 712 N PRO A 337 7.740 11.883 25.912 1.00 36.74 N
ATOM 713 CA PRO A 337 8.995 11.308 26.395 1.00 36.93 C
ATOM 714 C PRO A 337 8.862 10.352 27.571 1.00 36.19 C
ATOM 715 O PRO A 337 9.522 9.335 27.599 1.00 35.14 O
ATOM 716 CB PRO A 337 9.781 12.529 26.827 1.00 39.27 C
ATOM 717 CG PRO A 337 9.305 13.601 25.912 1.00 39.96 C
ATOM 718 CD PRO A 337 7.838 13.349 25.779 1.00 37.98 C
ATOM 719 N SER A 338 8.010 10.654 28.542 1.00 37.99 N
ATOM 720 CA SER A 338 7.845 9.740 29.660 1.00 39.19 C
ATOM 721 C SER A 338 7.353 8.339 29.267 1.00 43.12 C
ATOM 722 O SER A 338 7.443 7.414 30.093 1.00 47.05 O
ATOM 723 CB SER A 338 6.866 10.314 30.663 1.00 39.51 C
ATOM 724 OG SER A 338 5.595 10.410 30.052 1.00 42.42 O
ATOM 725 N PHE A 339 6.817 8.184 28.050 1.00 40.15 N
ATOM 726 CA PHE A 339 6.286 6.887 27.595 1.00 41.16 C
ATOM 727 C PHE A 339 7.264 6.029 26.795 1.00 39.17 C
ATOM 728 O PHE A 339 7.052 4.811 26.638 1.00 40.08 O
ATOM 729 CB PHE A 339 5.018 7.070 26.778 1.00 39.26 C
ATOM 730 CG PHE A 339 3.804 7.309 27.604 1.00 43.80 C
ATOM 731 CD1 PHE A 339 3.598 8.543 28.208 1.00 50.03 C
ATOM 732 CD2 PHE A 339 2.854 6.319 27.775 1.00 44.79 C
ATOM 733 CE1 PHE A 339 2.471 8.788 28.984 1.00 51.20 C
ATOM 734 CE2 PHE A 339 1.720 6.551 28.540 1.00 48.23 C
ATOM 735 CZ PHE A 339 1.528 7.786 29.156 1.00 49.99 C
ATOM 736 N LYS A 340 8.344 6.639 26.316 1.00 37.06 N
ATOM 737 CA LYS A 340 9.313 5.926 25.494 1.00 37.81 C
ATOM 738 C LYS A 340 9.956 4.757 26.258 1.00 33.73 C
ATOM 739 O LYS A 340 10.468 3.819 25.671 1.00 36.80 O
ATOM 740 CB LYS A 340 10.356 6.900 24.942 1.00 39.12 C
ATOM 741 CG LYS A 340 9.788 7.876 23.901 1.00 42.86 C
ATOM 742 CD LYS A 340 10.778 9.002 23.572 1.00 46.82 C
ATOM 743 CE LYS A 340 10.500 9.710 22.229 1.00 49.56 C
ATOM 744 NZ LYS A 340 9.309 10.600 22.275 1.00 50.88 N
ATOM 745 N GLN A 341 9.883 4.798 27.575 1.00 33.30 N
ATOM 746 CA GLN A 341 10.377 3.711 28.394 1.00 34.31 C
ATOM 747 C GLN A 341 9.669 2.377 28.093 1.00 33.94 C
ATOM 748 O GLN A 341 10.255 1.297 28.267 1.00 35.03 O
ATOM 749 CB GLN A 341 10.250 4.078 29.884 1.00 35.12 C
ATOM 750 CG GLN A 341 8.826 4.266 30.371 1.00 37.80 C
ATOM 751 CD GLN A 341 8.727 4.544 31.868 1.00 40.83 C
ATOM 752 OE1 GLN A 341 8.506 5.679 32.294 1.00 41.89 O
ATOM 753 NE2 GLN A 341 8.844 3.498 32.664 1.00 43.30 N
ATOM 754 N TYR A 342 8.415 2.447 27.646 1.00 32.43 N
ATOM 755 CA TYR A 342 7.655 1.225 27.390 1.00 31.23 C
ATOM 756 C TYR A 342 8.035 0.457 26.131 1.00 29.28 C
ATOM 757 O TYR A 342 7.667 -0.698 25.985 1.00 29.54 O
ATOM 758 CB TYR A 342 6.188 1.523 27.364 1.00 31.51 C
ATOM 759 CG TYR A 342 5.709 2.140 28.645 1.00 34.62 C
ATOM 760 CD1 TYR A 342 5.901 1.488 29.876 1.00 32.77 C
ATOM 761 CD2 TYR A 342 5.062 3.386 28.629 1.00 31.71 C
ATOM 762 CE1 TYR A 342 5.440 2.053 31.044 1.00 33.45 C
ATOM 763 CE2 TYR A 342 4.603 3.946 29.781 1.00 33.54 C
ATOM 764 CZ TYR A 342 4.795 3.289 30.985 1.00 34.26 C
ATOM 765 OH TYR A 342 4.309 3.890 32.118 1.00 35.24 O
ATOM 766 N TRP A 343 8.784 1.065 25.229 1.00 29.11 N
ATOM 767 CA TRP A 343 9.329 0.309 24.122 1.00 29.35 C
ATOM 768 C TRP A 343 10.101 -0.909 24.661 1.00 32.48 C
ATOM 769 O TRP A 343 10.809 -0.813 25.667 1.00 36.88 O
ATOM 770 CB TRP A 343 10.247 1.179 23.251 1.00 28.88 C
ATOM 771 CG TRP A 343 9.575 2.240 22.417 1.00 28.95 C
ATOM 772 CD1 TRP A 343 9.753 3.594 22.542 1.00 28.48 C
ATOM 773 CD2 TRP A 343 8.643 2.059 21.302 1.00 29.47 C
ATOM 774 NE1 TRP A 343 8.963 4.263 21.636 1.00 29.35 N
ATOM 775 CE2 TRP A 343 8.290 3.354 20.846 1.00 30.28 C
ATOM 776 CE3 TRP A 343 8.069 0.939 20.667 1.00 28.96 C
ATOM 777 CZ2 TRP A 343 7.412 3.563 19.743 1.00 28.18 C
ATOM 778 CZ3 TRP A 343 7.176 1.138 19.596 1.00 28.29 C
ATOM 779 CH2 TRP A 343 6.854 2.452 19.141 1.00 27.61 C
ATOM 780 N ASN A 344 9.979 -2.057 24.009 1.00 34.00 N
ATOM 781 CA ASN A 344 10.904 -3.152 24.300 1.00 34.34 C
ATOM 782 C ASN A 344 12.314 -2.685 23.983 1.00 35.24 C
ATOM 783 O ASN A 344 12.517 -1.730 23.220 1.00 32.68 O
ATOM 784 CB ASN A 344 10.601 -4.411 23.486 1.00 32.97 C
ATOM 785 CG ASN A 344 9.295 -5.080 23.898 1.00 34.67 C
ATOM 786 OD1 ASN A 344 8.873 -4.988 25.044 1.00 32.00 O
ATOM 787 ND2 ASN A 344 8.663 -5.766 22.965 1.00 31.86 N
ATOM 788 N ARG A 345 13.284 -3.374 24.569 1.00 39.92 N
ATOM 789 CA ARG A 345 14.702 -3.054 24.356 1.00 44.76 C
ATOM 790 C ARG A 345 15.038 -3.128 22.863 1.00 39.58 C
ATOM 791 O ARG A 345 14.618 -4.042 22.172 1.00 40.84 O
ATOM 792 CB ARG A 345 15.594 -3.982 25.204 1.00 52.60 C
ATOM 793 CG ARG A 345 16.983 -3.434 25.516 1.00 66.17 C
ATOM 794 CD ARG A 345 17.820 -4.391 26.378 1.00 81.64 C
ATOM 795 NE ARG A 345 18.360 -5.531 25.617 1.00 90.32 N
ATOM 796 CZ ARG A 345 17.785 -6.736 25.504 1.00 97.71 C
ATOM 797 NH1 ARG A 345 16.628 -7.022 26.108 1.00 95.44 N
ATOM 798 NH2 ARG A 345 18.380 -7.674 24.771 1.00 98.89 N
ATOM 799 N GLY A 346 15.754 -2.133 22.358 1.00 36.03 N
ATOM 800 CA GLY A 346 16.084 -2.052 20.914 1.00 34.85 C
ATOM 801 C GLY A 346 14.973 -1.509 20.017 1.00 37.92 C
ATOM 802 O GLY A 346 15.172 -1.368 18.807 1.00 36.39 O
ATOM 803 N GLU A 347 13.797 -1.232 20.584 1.00 32.53 N
ATOM 804 CA GLU A 347 12.683 -0.771 19.779 1.00 36.19 C
ATOM 805 C GLU A 347 12.436 0.725 20.052 1.00 33.13 C
ATOM 806 O GLU A 347 12.773 1.191 21.137 1.00 34.23 O
ATOM 807 CB GLU A 347 11.428 -1.610 20.067 1.00 33.97 C
ATOM 808 CG GLU A 347 11.633 -3.101 19.932 1.00 35.58 C
ATOM 809 CD GLU A 347 11.861 -3.597 18.506 1.00 38.49 C
ATOM 810 OE1 GLU A 347 11.695 -2.806 17.514 1.00 34.71 O
ATOM 811 OE2 GLU A 347 12.160 -4.842 18.377 1.00 41.34 O
ATOM 812 N PRO A 348 11.857 1.466 19.095 1.00 32.38 N
ATOM 813 CA PRO A 348 11.393 0.931 17.805 1.00 31.62 C
ATOM 814 C PRO A 348 12.518 0.993 16.823 1.00 32.62 C
ATOM 815 O PRO A 348 13.273 1.921 16.874 1.00 30.10 O
ATOM 816 CB PRO A 348 10.358 1.953 17.366 1.00 30.96 C
ATOM 817 CG PRO A 348 10.843 3.276 17.960 1.00 32.27 C
ATOM 818 CD PRO A 348 11.721 2.947 19.141 1.00 32.65 C
ATOM 819 N ASN A 349 12.611 0.033 15.927 1.00 31.46 N
ATOM 820 CA ASN A 349 13.804 -0.108 15.112 1.00 32.59 C
ATOM 821 C ASN A 349 13.495 -0.048 13.620 1.00 34.05 C
ATOM 822 O ASN A 349 14.398 -0.093 12.823 1.00 35.30 O
ATOM 823 CB ASN A 349 14.512 -1.433 15.477 1.00 31.86 C
ATOM 824 CG ASN A 349 13.635 -2.672 15.226 1.00 28.36 C
ATOM 825 OD1 ASN A 349 12.491 -2.577 14.790 1.00 26.90 O
ATOM 826 ND2 ASN A 349 14.195 -3.828 15.468 1.00 28.01 N
ATOM 827 N ASN A 350 12.211 0.031 13.262 1.00 34.15 N
ATOM 828 CA ASN A 350 11.762 0.224 11.891 1.00 34.94 C
ATOM 829 C ASN A 350 12.264 -0.837 10.931 1.00 36.10 C
ATOM 830 O ASN A 350 12.297 -0.605 9.717 1.00 32.31 O
ATOM 831 CB ASN A 350 12.141 1.615 11.359 1.00 34.29 C
ATOM 832 CG ASN A 350 11.373 1.976 10.100 1.00 35.84 C
ATOM 833 OD1 ASN A 350 10.168 1.739 9.985 1.00 35.87 O
ATOM 834 ND2 ASN A 350 12.068 2.544 9.137 1.00 37.31 N
ATOM 835 N VAL A 351 12.599 -2.026 11.449 1.00 37.17 N
ATOM 836 CA VAL A 351 13.209 -3.051 10.575 1.00 36.54 C
ATOM 837 C VAL A 351 12.215 -3.606 9.549 1.00 36.09 C
ATOM 838 O VAL A 351 11.150 -4.151 9.892 1.00 34.70 O
ATOM 839 CB VAL A 351 13.899 -4.157 11.378 1.00 37.68 C
ATOM 840 CG1 VAL A 351 12.877 -5.049 12.113 1.00 40.14 C
ATOM 841 CG2 VAL A 351 14.805 -4.962 10.452 1.00 37.85 C
ATOM 842 N GLY A 352 12.557 -3.452 8.276 1.00 34.78 N
ATOM 843 CA GLY A 352 11.652 -3.841 7.205 1.00 35.78 C
ATOM 844 C GLY A 352 10.492 -2.876 6.993 1.00 38.04 C
ATOM 845 O GLY A 352 9.484 -3.234 6.342 1.00 36.38 O
ATOM 846 N GLU A 353 10.647 -1.656 7.532 1.00 38.32 N
ATOM 847 CA GLU A 353 9.580 -0.658 7.602 1.00 36.33 C
ATOM 848 C GLU A 353 8.417 -1.097 8.471 1.00 33.28 C
ATOM 849 O GLU A 353 7.511 -1.757 7.979 1.00 31.30 O
ATOM 850 CB GLU A 353 9.118 -0.263 6.206 1.00 37.43 C
ATOM 851 CG GLU A 353 10.337 0.195 5.423 1.00 44.39 C
ATOM 852 CD GLU A 353 10.025 1.181 4.340 1.00 48.55 C
ATOM 853 OE1 GLU A 353 8.914 1.117 3.772 1.00 51.91 O
ATOM 854 OE2 GLU A 353 10.899 2.031 4.073 1.00 59.01 O
ATOM 855 N GLU A 354 8.461 -0.669 9.741 1.00 30.73 N
ATOM 856 CA GLU A 354 7.472 -1.005 10.780 1.00 28.71 C
ATOM 857 C GLU A 354 6.989 0.335 11.292 1.00 25.26 C
ATOM 858 O GLU A 354 7.713 1.034 11.975 1.00 23.98 O
ATOM 859 CB GLU A 354 8.117 -1.806 11.924 1.00 29.70 C
ATOM 860 CG GLU A 354 8.748 -3.099 11.445 1.00 30.63 C
ATOM 861 CD GLU A 354 9.469 -3.861 12.506 1.00 32.81 C
ATOM 862 OE1 GLU A 354 10.312 -3.258 13.249 1.00 32.52 O
ATOM 863 OE2 GLU A 354 9.216 -5.107 12.569 1.00 37.11 O
ATOM 864 N ASP A 355 5.775 0.692 10.922 1.00 23.99 N
ATOM 865 CA ASP A 355 5.188 1.956 11.305 1.00 24.77 C
ATOM 866 C ASP A 355 3.974 1.849 12.244 1.00 28.07 C
ATOM 867 O ASP A 355 3.262 2.838 12.460 1.00 25.56 O
ATOM 868 CB ASP A 355 4.792 2.712 10.057 1.00 24.05 C
ATOM 869 CG ASP A 355 5.993 3.000 9.157 1.00 22.15 C
ATOM 870 OD1 ASP A 355 7.176 2.906 9.634 1.00 19.93 O
ATOM 871 OD2 ASP A 355 5.726 3.331 8.036 1.00 22.13 O
ATOM 872 N CYS A 356 3.745 0.666 12.795 1.00 28.70 N
ATOM 873 CA CYS A 356 2.600 0.485 13.698 1.00 29.44 C
ATOM 874 C CYS A 356 3.013 -0.172 14.993 1.00 28.28 C
ATOM 875 O CYS A 356 3.848 -1.067 15.011 1.00 26.38 O
ATOM 876 CB CYS A 356 1.526 -0.325 12.994 1.00 29.65 C
ATOM 877 SG CYS A 356 0.699 0.563 11.673 1.00 31.65 S
ATOM 878 N ALA A 357 2.438 0.302 16.089 1.00 28.96 N
ATOM 879 CA ALA A 357 2.860 -0.116 17.410 1.00 28.94 C
ATOM 880 C ALA A 357 1.934 -1.191 17.956 1.00 26.86 C
ATOM 881 O ALA A 357 0.730 -1.130 17.768 1.00 26.17 O
ATOM 882 CB ALA A 357 2.931 1.064 18.365 1.00 29.29 C
ATOM 883 N GLU A 358 2.524 -2.171 18.627 1.00 26.65 N
ATOM 884 CA GLU A 358 1.809 -3.308 19.157 1.00 25.47 C
ATOM 885 C GLU A 358 2.280 -3.597 20.569 1.00 24.90 C
ATOM 886 O GLU A 358 3.425 -3.331 20.943 1.00 25.18 O
ATOM 887 CB GLU A 358 2.050 -4.553 18.283 1.00 27.54 C
ATOM 888 CG GLU A 358 3.508 -5.020 18.351 1.00 30.28 C
ATOM 889 CD GLU A 358 3.797 -6.437 17.877 1.00 30.18 C
ATOM 890 OE1 GLU A 358 5.002 -6.722 17.694 1.00 31.28 O
ATOM 891 OE2 GLU A 358 2.880 -7.274 17.725 1.00 29.53 O
ATOM 892 N PHE A 359 1.409 -4.202 21.358 1.00 23.89 N
ATOM 893 CA PHE A 359 1.824 -4.795 22.587 1.00 22.99 C
ATOM 894 C PHE A 359 2.467 -6.124 22.267 1.00 25.22 C
ATOM 895 O PHE A 359 1.846 -6.983 21.625 1.00 26.29 O
ATOM 896 CB PHE A 359 0.609 -5.040 23.479 1.00 22.54 C
ATOM 897 CG PHE A 359 -0.107 -3.791 23.879 1.00 21.13 C
ATOM 898 CD1 PHE A 359 0.362 -3.005 24.895 1.00 23.40 C
ATOM 899 CD2 PHE A 359 -1.220 -3.373 23.190 1.00 22.72 C
ATOM 900 CE1 PHE A 359 -0.295 -1.841 25.269 1.00 21.70 C
ATOM 901 CE2 PHE A 359 -1.874 -2.220 23.563 1.00 23.94 C
ATOM 902 CZ PHE A 359 -1.409 -1.454 24.607 1.00 21.91 C
ATOM 903 N SER A 360 3.685 -6.318 22.777 1.00 27.30 N
ATOM 904 CA SER A 360 4.429 -7.502 22.508 1.00 30.03 C
ATOM 905 C SER A 360 5.364 -7.910 23.628 1.00 34.52 C
ATOM 906 O SER A 360 6.431 -7.315 23.793 1.00 34.92 O
ATOM 907 CB SER A 360 5.248 -7.250 21.283 1.00 32.98 C
ATOM 908 OG SER A 360 5.962 -8.419 20.978 1.00 40.68 O
ATOM 909 N GLY A 361 4.991 -8.972 24.349 1.00 35.88 N
ATOM 910 CA GLY A 361 5.689 -9.364 25.562 1.00 34.56 C
ATOM 911 C GLY A 361 5.371 -8.395 26.698 1.00 36.67 C
ATOM 912 O GLY A 361 4.215 -8.177 27.045 1.00 36.59 O
ATOM 913 N ASN A 362 6.411 -7.830 27.292 1.00 37.22 N
ATOM 914 CA ASN A 362 6.261 -6.886 28.397 1.00 38.63 C
ATOM 915 C ASN A 362 6.253 -5.413 27.982 1.00 35.07 C
ATOM 916 O ASN A 362 6.003 -4.545 28.798 1.00 34.05 O
ATOM 917 CB ASN A 362 7.400 -7.110 29.387 1.00 41.76 C
ATOM 918 CG ASN A 362 7.355 -8.498 30.007 1.00 48.28 C
ATOM 919 OD1 ASN A 362 6.278 -9.069 30.273 1.00 48.40 O
ATOM 920 ND2 ASN A 362 8.531 -9.061 30.222 1.00 55.91 N
ATOM 921 N GLY A 363 6.553 -5.139 26.725 1.00 35.30 N
ATOM 922 CA GLY A 363 6.527 -3.754 26.208 1.00 34.44 C
ATOM 923 C GLY A 363 5.913 -3.609 24.814 1.00 32.67 C
ATOM 924 O GLY A 363 5.101 -4.440 24.366 1.00 28.62 O
ATOM 925 N TRP A 364 6.323 -2.532 24.138 1.00 30.61 N
ATOM 926 CA TRP A 364 5.824 -2.183 22.844 1.00 27.30 C
ATOM 927 C TRP A 364 6.875 -2.509 21.811 1.00 27.44 C
ATOM 928 O TRP A 364 8.074 -2.461 22.075 1.00 26.70 O
ATOM 929 CB TRP A 364 5.510 -0.695 22.736 1.00 27.20 C
ATOM 930 CG TRP A 364 4.627 -0.131 23.737 1.00 27.02 C
ATOM 931 CD1 TRP A 364 3.886 -0.788 24.684 1.00 26.54 C
ATOM 932 CD2 TRP A 364 4.342 1.242 23.882 1.00 27.75 C
ATOM 933 NE1 TRP A 364 3.198 0.128 25.456 1.00 24.81 N
ATOM 934 CE2 TRP A 364 3.464 1.382 24.982 1.00 25.73 C
ATOM 935 CE3 TRP A 364 4.799 2.394 23.233 1.00 28.44 C
ATOM 936 CZ2 TRP A 364 2.979 2.631 25.405 1.00 26.27 C
ATOM 937 CZ3 TRP A 364 4.320 3.637 23.668 1.00 27.35 C
ATOM 938 CH2 TRP A 364 3.403 3.734 24.739 1.00 26.32 C
ATOM 939 N ASN A 365 6.403 -2.819 20.621 1.00 25.86 N
ATOM 940 CA ASN A 365 7.284 -3.037 19.484 1.00 27.73 C
ATOM 941 C ASN A 365 6.687 -2.353 18.258 1.00 26.46 C
ATOM 942 O ASN A 365 5.487 -2.239 18.141 1.00 28.42 O
ATOM 943 CB ASN A 365 7.446 -4.538 19.210 1.00 25.15 C
ATOM 944 CG ASN A 365 8.230 -4.801 17.915 1.00 27.41 C
ATOM 945 OD1 ASN A 365 9.296 -4.191 17.688 1.00 22.88 O
ATOM 946 ND2 ASN A 365 7.694 -5.671 17.049 1.00 22.61 N
ATOM 947 N ASP A 366 7.521 -1.898 17.342 1.00 28.82 N
ATOM 948 CA ASP A 366 7.017 -1.488 16.043 1.00 25.71 C
ATOM 949 C ASP A 366 7.025 -2.669 15.076 1.00 27.17 C
ATOM 950 O ASP A 366 8.004 -3.384 14.990 1.00 25.71 O
ATOM 951 CB ASP A 366 7.753 -0.272 15.492 1.00 28.37 C
ATOM 952 CG ASP A 366 9.221 -0.481 15.281 1.00 28.05 C
ATOM 953 OD1 ASP A 366 9.813 -1.344 15.948 1.00 27.12 O
ATOM 954 OD2 ASP A 366 9.784 0.275 14.457 1.00 32.28 O
ATOM 955 N ASP A 367 5.905 -2.914 14.403 1.00 26.56 N
ATOM 956 CA ASP A 367 5.806 -4.019 13.469 1.00 29.24 C
ATOM 957 C ASP A 367 5.167 -3.480 12.241 1.00 27.96 C
ATOM 958 O ASP A 367 4.806 -2.304 12.196 1.00 26.23 O
ATOM 959 CB ASP A 367 4.984 -5.187 14.024 1.00 30.43 C
ATOM 960 CG ASP A 367 5.426 -6.565 13.470 1.00 32.22 C
ATOM 961 OD1 ASP A 367 6.045 -6.661 12.378 1.00 31.15 O
ATOM 962 OD2 ASP A 367 5.142 -7.576 14.144 1.00 32.34 O
ATOM 963 N LYS A 368 5.056 -4.354 11.243 1.00 29.64 N
ATOM 964 CA LYS A 368 4.512 -4.022 9.938 1.00 32.05 C
ATOM 965 C LYS A 368 2.984 -3.990 9.990 1.00 30.08 C
ATOM 966 O LYS A 368 2.351 -4.912 10.480 1.00 25.31 O
ATOM 967 CB LYS A 368 4.948 -5.041 8.883 1.00 36.44 C
ATOM 968 CG LYS A 368 6.381 -5.526 9.008 1.00 40.08 C
ATOM 969 CD LYS A 368 6.834 -6.158 7.712 1.00 48.43 C
ATOM 970 CE LYS A 368 8.260 -6.667 7.854 1.00 55.12 C
ATOM 971 NZ LYS A 368 8.315 -7.960 8.603 1.00 54.90 N
ATOM 972 N CYS A 369 2.442 -2.937 9.403 1.00 29.41 N
ATOM 973 CA CYS A 369 1.066 -2.528 9.582 1.00 28.75 C
ATOM 974 C CYS A 369 0.103 -3.426 8.899 1.00 28.97 C
ATOM 975 O CYS A 369 -1.068 -3.422 9.266 1.00 28.38 O
ATOM 976 CB CYS A 369 0.847 -1.096 9.059 1.00 29.62 C
ATOM 977 SG CYS A 369 1.787 0.196 9.916 1.00 30.26 S
ATOM 978 N ASN A 370 0.565 -4.165 7.882 1.00 28.00 N
ATOM 979 CA ASN A 370 -0.302 -5.047 7.130 1.00 30.72 C
ATOM 980 C ASN A 370 -0.407 -6.450 7.697 1.00 28.39 C
ATOM 981 O ASN A 370 -1.135 -7.250 7.161 1.00 31.03 O
ATOM 982 CB ASN A 370 0.136 -5.129 5.668 1.00 35.84 C
ATOM 983 CG ASN A 370 1.412 -5.909 5.468 1.00 39.28 C
ATOM 984 OD1 ASN A 370 2.407 -5.703 6.163 1.00 43.84 O
ATOM 985 ND2 ASN A 370 1.403 -6.790 4.466 1.00 49.44 N
ATOM 986 N LEU A 371 0.322 -6.750 8.764 1.00 29.49 N
ATOM 987 CA LEU A 371 0.133 -8.021 9.488 1.00 29.38 C
ATOM 988 C LEU A 371 -1.114 -7.978 10.323 1.00 30.08 C
ATOM 989 O LEU A 371 -1.583 -6.919 10.706 1.00 30.00 O
ATOM 990 CB LEU A 371 1.314 -8.369 10.406 1.00 27.70 C
ATOM 991 CG LEU A 371 2.658 -8.479 9.709 1.00 29.29 C
ATOM 992 CD1 LEU A 371 3.802 -8.734 10.678 1.00 27.68 C
ATOM 993 CD2 LEU A 371 2.558 -9.578 8.671 1.00 28.59 C
ATOM 994 N ALA A 372 -1.597 -9.172 10.634 1.00 30.55 N
ATOM 995 CA ALA A 372 -2.853 -9.402 11.310 1.00 29.64 C
ATOM 996 C ALA A 372 -2.555 -9.603 12.796 1.00 29.22 C
ATOM 997 O ALA A 372 -1.763 -10.458 13.164 1.00 29.43 O
ATOM 998 CB ALA A 372 -3.551 -10.626 10.705 1.00 31.84 C
ATOM 999 N LYS A 373 -3.148 -8.760 13.639 1.00 27.52 N
ATOM 1000 CA LYS A 373 -2.979 -8.856 15.078 1.00 25.70 C
ATOM 1001 C LYS A 373 -4.290 -8.651 15.776 1.00 23.97 C
ATOM 1002 O LYS A 373 -5.214 -8.104 15.196 1.00 25.16 O
ATOM 1003 CB LYS A 373 -2.014 -7.763 15.560 1.00 26.72 C
ATOM 1004 CG LYS A 373 -0.517 -8.045 15.308 1.00 27.78 C
ATOM 1005 CD LYS A 373 0.364 -6.855 15.648 1.00 28.23 C
ATOM 1006 CE LYS A 373 1.661 -6.801 14.864 1.00 31.74 C
ATOM 1007 NZ LYS A 373 2.577 -7.888 15.260 1.00 35.02 N
ATOM 1008 N PHE A 374 -4.360 -9.021 17.055 1.00 24.96 N
ATOM 1009 CA PHE A 374 -5.517 -8.638 17.872 1.00 24.48 C
ATOM 1010 C PHE A 374 -5.482 -7.137 18.087 1.00 24.47 C
ATOM 1011 O PHE A 374 -4.463 -6.490 17.819 1.00 24.62 O
ATOM 1012 CB PHE A 374 -5.527 -9.370 19.192 1.00 25.48 C
ATOM 1013 CG PHE A 374 -5.618 -10.850 19.047 1.00 28.75 C
ATOM 1014 CD1 PHE A 374 -6.845 -11.471 18.979 1.00 31.43 C
ATOM 1015 CD2 PHE A 374 -4.473 -11.623 18.947 1.00 30.41 C
ATOM 1016 CE1 PHE A 374 -6.940 -12.842 18.797 1.00 32.81 C
ATOM 1017 CE2 PHE A 374 -4.553 -12.987 18.801 1.00 32.23 C
ATOM 1018 CZ PHE A 374 -5.790 -13.607 18.708 1.00 31.97 C
ATOM 1019 N TRP A 375 -6.581 -6.571 18.563 1.00 25.25 N
ATOM 1020 CA TRP A 375 -6.657 -5.119 18.775 1.00 26.15 C
ATOM 1021 C TRP A 375 -7.570 -4.752 19.952 1.00 27.30 C
ATOM 1022 O TRP A 375 -8.383 -5.556 20.445 1.00 26.45 O
ATOM 1023 CB TRP A 375 -7.072 -4.363 17.490 1.00 26.62 C
ATOM 1024 CG TRP A 375 -8.558 -4.455 17.223 1.00 27.26 C
ATOM 1025 CD1 TRP A 375 -9.555 -3.606 17.702 1.00 27.41 C
ATOM 1026 CD2 TRP A 375 -9.218 -5.463 16.494 1.00 25.78 C
ATOM 1027 NE1 TRP A 375 -10.781 -4.036 17.285 1.00 27.87 N
ATOM 1028 CE2 TRP A 375 -10.608 -5.185 16.552 1.00 28.54 C
ATOM 1029 CE3 TRP A 375 -8.780 -6.549 15.758 1.00 27.43 C
ATOM 1030 CZ2 TRP A 375 -11.544 -5.984 15.925 1.00 27.32 C
ATOM 1031 CZ3 TRP A 375 -9.701 -7.351 15.169 1.00 29.85 C
ATOM 1032 CH2 TRP A 375 -11.064 -7.074 15.247 1.00 28.50 C
ATOM 1033 N ILE A 376 -7.405 -3.530 20.417 1.00 25.86 N
ATOM 1034 CA ILE A 376 -8.195 -3.019 21.546 1.00 27.97 C
ATOM 1035 C ILE A 376 -8.756 -1.646 21.205 1.00 27.75 C
ATOM 1036 O ILE A 376 -8.048 -0.742 20.786 1.00 26.08 O
ATOM 1037 CB ILE A 376 -7.369 -2.939 22.826 1.00 26.82 C
ATOM 1038 CG1 ILE A 376 -6.988 -4.359 23.269 1.00 28.88 C
ATOM 1039 CG2 ILE A 376 -8.149 -2.219 23.922 1.00 27.56 C
ATOM 1040 CD1 ILE A 376 -5.871 -4.420 24.281 1.00 30.49 C
ATOM 1041 N CYS A 377 -10.052 -1.523 21.331 1.00 28.89 N
ATOM 1042 CA CYS A 377 -10.686 -0.228 21.176 1.00 30.17 C
ATOM 1043 C CYS A 377 -10.943 0.378 22.544 1.00 29.24 C
ATOM 1044 O CYS A 377 -11.166 -0.341 23.540 1.00 26.96 O
ATOM 1045 CB CYS A 377 -12.036 -0.364 20.451 1.00 30.04 C
ATOM 1046 SG CYS A 377 -11.977 -1.263 18.909 1.00 33.93 S
ATOM 1047 N LYS A 378 -10.971 1.709 22.559 1.00 28.53 N
ATOM 1048 CA LYS A 378 -11.220 2.475 23.754 1.00 29.01 C
ATOM 1049 C LYS A 378 -12.276 3.549 23.479 1.00 29.40 C
ATOM 1050 O LYS A 378 -12.225 4.206 22.438 1.00 26.95 O
ATOM 1051 CB LYS A 378 -9.915 3.131 24.227 1.00 27.89 C
ATOM 1052 CG LYS A 378 -10.039 3.972 25.496 1.00 26.85 C
ATOM 1053 CD LYS A 378 -8.894 4.964 25.576 1.00 27.69 C
ATOM 1054 CE LYS A 378 -8.831 5.744 26.839 1.00 28.90 C
ATOM 1055 NZ LYS A 378 -7.439 6.268 27.094 1.00 29.95 N
ATOM 1056 N LYS A 379 -13.211 3.723 24.417 1.00 28.91 N
ATOM 1057 CA LYS A 379 -14.072 4.920 24.459 1.00 31.93 C
ATOM 1058 C LYS A 379 -14.538 5.228 25.883 1.00 32.47 C
ATOM 1059 O LYS A 379 -14.463 4.362 26.738 1.00 31.49 O
ATOM 1060 CB LYS A 379 -15.308 4.757 23.559 1.00 33.74 C
ATOM 1061 CG LYS A 379 -16.099 3.502 23.783 1.00 36.52 C
ATOM 1062 CD LYS A 379 -17.520 3.691 23.321 1.00 38.92 C
ATOM 1063 CE LYS A 379 -18.283 2.400 23.430 1.00 43.69 C
ATOM 1064 NZ LYS A 379 -19.211 2.316 22.267 1.00 45.84 N
ATOM 1065 N SER A 380 -15.064 6.442 26.105 1.00 32.60 N
ATOM 1066 CA SER A 380 -15.494 6.896 27.448 1.00 36.42 C
ATOM 1067 C SER A 380 -16.603 6.057 28.024 1.00 33.33 C
ATOM 1068 O SER A 380 -17.476 5.624 27.302 1.00 37.71 O
ATOM 1069 CB SER A 380 -15.987 8.331 27.417 1.00 36.01 C
ATOM 1070 OG SER A 380 -14.852 9.152 27.381 1.00 45.06 O
ATOM 1071 N ALA A 381 -16.552 5.808 29.316 1.00 36.30 N
ATOM 1072 CA ALA A 381 -17.699 5.228 29.986 1.00 39.03 C
ATOM 1073 C ALA A 381 -18.837 6.223 29.858 1.00 42.07 C
ATOM 1074 O ALA A 381 -18.622 7.400 29.569 1.00 42.80 O
ATOM 1075 CB ALA A 381 -17.383 4.936 31.436 1.00 41.28 C
ATOM 1076 N ALA A 382 -20.058 5.746 29.983 1.00 48.00 N
ATOM 1077 CA ALA A 382 -21.218 6.639 30.059 1.00 57.00 C
ATOM 1078 C ALA A 382 -21.327 7.062 31.513 1.00 58.08 C
ATOM 1079 O ALA A 382 -20.787 6.385 32.394 1.00 51.66 O
ATOM 1080 CB ALA A 382 -22.484 5.932 29.596 1.00 57.25 C
ATOM 1081 N SER A 383 -21.983 8.185 31.778 1.00 68.68 N
ATOM 1082 CA SER A 383 -22.168 8.589 33.183 1.00 78.14 C
ATOM 1083 C SER A 383 -23.357 7.879 33.837 1.00 79.21 C
ATOM 1084 O SER A 383 -24.414 7.713 33.205 1.00 70.13 O
ATOM 1085 CB SER A 383 -22.270 10.100 33.334 1.00 75.92 C
ATOM 1086 OG SER A 383 -21.002 10.598 33.735 1.00 76.03 O
ATOM 1087 N CYS A 384 -23.142 7.431 35.077 1.00 84.34 N
ATOM 1088 CA CYS A 384 -24.177 6.763 35.881 1.00 96.18 C
ATOM 1089 C CYS A 384 -24.277 7.407 37.279 1.00 98.40 C
ATOM 1090 O CYS A 384 -25.375 7.653 37.800 1.00 84.38 O
ATOM 1091 CB CYS A 384 -23.888 5.258 36.020 1.00 95.03 C
ATOM 1092 SG CYS A 384 -24.109 4.188 34.561 1.00100.23 S
TER 1093 CYS A 384
HETATM 1094 C4 EZ8 A1001 11.482 -6.710 15.963 1.00 30.75 C
HETATM 1095 C5 EZ8 A1001 12.563 -7.787 15.836 1.00 29.78 C
HETATM 1096 C6 EZ8 A1001 13.220 -7.891 17.157 1.00 31.49 C
HETATM 1097 N2 EZ8 A1001 9.219 -8.559 15.604 1.00 27.44 N
HETATM 1098 C3 EZ8 A1001 10.588 -6.752 14.722 1.00 29.48 C
HETATM 1099 CAP EZ8 A1001 8.674 -14.311 9.107 1.00 59.26 C
HETATM 1100 CAL EZ8 A1001 8.310 -15.457 9.809 1.00 53.05 C
HETATM 1101 CBM EZ8 A1001 9.235 -16.392 10.206 1.00 56.33 C
HETATM 1102 CAV EZ8 A1001 8.780 -17.491 10.927 1.00 60.31 C
HETATM 1103 OAE EZ8 A1001 9.327 -18.696 10.414 1.00 61.35 O
HETATM 1104 CAM EZ8 A1001 10.577 -16.152 9.906 1.00 57.92 C
HETATM 1105 CAQ EZ8 A1001 10.957 -15.000 9.195 1.00 58.75 C
HETATM 1106 CBO EZ8 A1001 10.009 -14.048 8.804 1.00 55.99 C
HETATM 1107 CAZ EZ8 A1001 10.331 -12.890 8.114 1.00 50.64 C
HETATM 1108 NBF EZ8 A1001 11.014 -11.937 9.031 1.00 48.22 N
HETATM 1109 CBK EZ8 A1001 10.430 -10.921 9.736 1.00 40.55 C
HETATM 1110 OAC EZ8 A1001 9.213 -10.667 9.703 1.00 41.94 O
HETATM 1111 CBW EZ8 A1001 11.398 -10.073 10.601 1.00 35.06 C
HETATM 1112 CBB EZ8 A1001 11.825 -10.843 11.767 1.00 35.72 C
HETATM 1113 CBV EZ8 A1001 12.647 -9.563 9.836 1.00 34.28 C
HETATM 1114 CBJ EZ8 A1001 12.197 -8.689 8.666 1.00 34.17 C
HETATM 1115 OAB EZ8 A1001 11.454 -7.742 8.898 1.00 31.54 O
HETATM 1116 NBE EZ8 A1001 12.707 -8.912 7.420 1.00 34.10 N
HETATM 1117 CAY EZ8 A1001 12.237 -8.092 6.260 1.00 33.18 C
HETATM 1118 CBN EZ8 A1001 13.079 -7.015 5.886 1.00 35.30 C
HETATM 1119 CAN EZ8 A1001 13.905 -6.366 6.804 1.00 38.14 C
HETATM 1120 CAJ EZ8 A1001 14.757 -5.324 6.419 1.00 34.68 C
HETATM 1121 CBL EZ8 A1001 14.797 -4.905 5.099 1.00 38.91 C
HETATM 1122 CAU EZ8 A1001 15.685 -3.880 4.725 1.00 41.47 C
HETATM 1123 OAD EZ8 A1001 14.949 -2.706 4.453 1.00 50.35 O
HETATM 1124 CAK EZ8 A1001 13.974 -5.559 4.158 1.00 36.39 C
HETATM 1125 CAO EZ8 A1001 13.127 -6.593 4.551 1.00 34.98 C
HETATM 1126 CBA EZ8 A1001 13.427 -8.661 10.677 1.00 33.09 C
HETATM 1127 CBT EZ8 A1001 13.875 -9.334 11.918 1.00 36.35 C
HETATM 1128 OBG EZ8 A1001 14.917 -10.360 11.664 1.00 39.68 O
HETATM 1129 CAX EZ8 A1001 15.801 -10.428 12.770 1.00 43.18 C
HETATM 1130 CAT EZ8 A1001 16.498 -11.792 12.723 1.00 48.49 C
HETATM 1131 CL1 EZ8 A1001 15.346 -13.117 12.262 1.00 57.77 Cl
HETATM 1132 CBU EZ8 A1001 12.643 -9.942 12.679 1.00 35.33 C
HETATM 1133 O1 EZ8 A1001 11.837 -8.873 13.152 1.00 33.49 O
HETATM 1134 C1 EZ8 A1001 11.133 -9.132 14.421 1.00 30.23 C
HETATM 1135 O5 EZ8 A1001 11.972 -9.064 15.583 1.00 26.40 O
HETATM 1136 O6 EZ8 A1001 14.442 -8.516 16.853 1.00 34.29 O
HETATM 1137 O4 EZ8 A1001 12.071 -5.425 16.084 1.00 30.09 O
HETATM 1138 O3 EZ8 A1001 9.595 -5.818 14.915 1.00 29.45 O
HETATM 1139 C2 EZ8 A1001 10.007 -8.157 14.524 1.00 28.12 C
HETATM 1140 CAR EZ8 A1001 8.001 -8.975 15.320 1.00 31.65 C
HETATM 1141 NBD EZ8 A1001 9.381 -8.644 16.917 1.00 29.99 N
HETATM 1142 NBC EZ8 A1001 8.272 -9.118 17.455 1.00 33.12 N
HETATM 1143 CBP EZ8 A1001 7.411 -9.316 16.456 1.00 35.09 C
HETATM 1144 CAS EZ8 A1001 5.986 -9.862 16.498 1.00 39.91 C
HETATM 1145 NAA EZ8 A1001 5.306 -9.362 17.690 1.00 43.58 N
HETATM 1146 CA CA A1002 10.340 -3.466 15.648 1.00 30.01 Ca
HETATM 1147 CA CA A1003 8.614 3.298 11.247 1.00 29.98 Ca
HETATM 1148 CA CA A1004 6.761 4.592 6.547 1.00 49.01 Ca
HETATM 1149 CL CL A1005 -13.513 -9.680 17.781 1.00 64.34 Cl
HETATM 1150 CL CL A1006 -7.495 -8.001 34.168 1.00 64.60 Cl
HETATM 1151 CL CL A1007 -11.156 0.395 37.832 1.00 65.39 Cl
HETATM 1152 O HOH A1101 -4.860 3.588 8.030 1.00 44.58 O
HETATM 1153 O HOH A1102 7.228 5.898 8.319 1.00 35.56 O
HETATM 1154 O HOH A1103 -5.142 -11.226 28.980 1.00 38.68 O
HETATM 1155 O HOH A1104 -12.199 -9.067 12.253 1.00 52.11 O
HETATM 1156 O HOH A1105 -1.698 1.095 40.354 1.00 49.11 O
HETATM 1157 O HOH A1106 -3.562 -6.995 5.338 1.00 42.01 O
HETATM 1158 O HOH A1107 -2.827 -5.664 24.875 1.00 44.63 O
HETATM 1159 O HOH A1108 9.516 -6.808 10.586 1.00 45.69 O
HETATM 1160 O HOH A1109 -4.454 4.287 40.482 1.00 40.12 O
HETATM 1161 O HOH A1110 3.482 15.233 8.028 1.00 38.14 O
HETATM 1162 O HOH A1111 13.086 5.135 12.131 1.00 37.47 O
HETATM 1163 O HOH A1112 14.435 -5.087 19.623 1.00 44.45 O
HETATM 1164 O HOH A1113 7.461 -18.432 8.614 1.00 34.42 O
HETATM 1165 O HOH A1114 4.065 10.143 12.159 1.00 33.95 O
HETATM 1166 O HOH A1115 -8.207 -14.162 13.643 1.00 36.26 O
HETATM 1167 O HOH A1116 -10.654 -0.511 6.812 1.00 44.98 O
HETATM 1168 O HOH A1117 -5.680 6.931 30.891 1.00 46.00 O
HETATM 1169 O HOH A1118 8.376 3.298 7.319 1.00 23.92 O
HETATM 1170 O HOH A1119 -1.045 7.185 14.538 1.00 32.98 O
HETATM 1171 O HOH A1120 10.332 7.296 29.139 1.00 38.22 O
HETATM 1172 O HOH A1121 -7.682 8.144 29.012 1.00 34.85 O
HETATM 1173 O HOH A1122 -13.634 -13.876 24.699 1.00 55.46 O
HETATM 1174 O HOH A1123 -20.184 -6.706 29.936 1.00 29.52 O
HETATM 1175 O HOH A1124 8.917 -8.214 26.300 1.00 46.26 O
HETATM 1176 O HOH A1125 -0.824 11.394 28.657 1.00 33.94 O
HETATM 1177 O HOH A1126 1.486 -4.821 33.198 1.00 34.55 O
HETATM 1178 O HOH A1127 -7.257 -6.694 8.142 1.00 31.39 O
HETATM 1179 O HOH A1128 7.048 12.461 20.238 1.00 38.27 O
HETATM 1180 O HOH A1129 9.617 2.743 12.981 1.00 30.03 O
HETATM 1181 O HOH A1130 -20.842 -1.545 31.916 1.00 36.52 O
HETATM 1182 O HOH A1131 -9.019 4.471 31.596 1.00 35.19 O
HETATM 1183 O HOH A1132 -17.566 -6.994 30.601 1.00 50.10 O
HETATM 1184 O HOH A1133 -9.540 4.081 15.735 1.00 36.17 O
HETATM 1185 O HOH A1134 -10.147 -11.933 11.601 1.00 46.58 O
HETATM 1186 O HOH A1135 9.103 0.708 32.312 1.00 51.94 O
HETATM 1187 O HOH A1136 2.065 9.730 24.858 1.00 31.32 O
HETATM 1188 O HOH A1137 1.944 8.523 11.870 1.00 27.47 O
HETATM 1189 O HOH A1138 0.581 8.402 34.287 1.00 45.07 O
HETATM 1190 O HOH A1139 6.604 3.167 5.276 1.00 37.95 O
HETATM 1191 O HOH A1140 -3.104 -0.790 36.278 1.00 34.26 O
HETATM 1192 O HOH A1141 4.764 -0.833 8.258 1.00 31.27 O
HETATM 1193 O HOH A1142 -3.826 -12.523 35.738 1.00 36.76 O
HETATM 1194 O HOH A1143 12.730 -5.395 26.647 1.00 46.84 O
HETATM 1195 O HOH A1144 11.392 4.060 6.677 1.00 32.02 O
HETATM 1196 O HOH A1145 8.414 9.936 18.406 1.00 38.65 O
HETATM 1197 O HOH A1146 -19.813 -3.643 30.184 1.00 37.80 O
HETATM 1198 O HOH A1147 10.762 4.998 14.370 1.00 40.96 O
HETATM 1199 O HOH A1148 -19.199 6.388 21.565 1.00 51.32 O
HETATM 1200 O HOH A1149 9.971 6.782 20.342 1.00 34.33 O
HETATM 1201 O HOH A1150 -7.783 8.333 24.904 1.00 32.22 O
HETATM 1202 O HOH A1151 -23.827 0.024 36.531 1.00 47.02 O
HETATM 1203 O HOH A1152 -10.075 -10.814 24.515 1.00 47.88 O
HETATM 1204 O HOH A1153 4.425 -1.505 31.793 1.00 40.62 O
HETATM 1205 O HOH A1154 6.622 13.363 29.049 1.00 42.79 O
HETATM 1206 O HOH A1155 2.330 -10.847 23.930 1.00 39.17 O
HETATM 1207 O AHOH A1156 -20.853 -12.793 21.665 0.50 22.53 O
HETATM 1208 O BHOH A1156 -18.973 -12.702 22.407 0.50 23.38 O
HETATM 1209 O HOH A1157 -1.739 16.849 15.520 1.00 53.69 O
HETATM 1210 O HOH A1158 10.331 -6.337 20.391 1.00 38.96 O
HETATM 1211 O HOH A1159 -30.342 -0.786 33.033 1.00 58.79 O
HETATM 1212 O HOH A1160 -8.012 7.475 9.827 1.00 54.15 O
HETATM 1213 O HOH A1161 14.526 -1.070 7.149 1.00 39.21 O
HETATM 1214 O HOH A1162 -1.183 -12.035 15.870 1.00 61.03 O
HETATM 1215 O HOH A1163 -24.275 -2.994 24.559 1.00 39.28 O
HETATM 1216 O HOH A1164 -23.009 1.611 27.765 1.00 54.27 O
HETATM 1217 O HOH A1165 -21.246 3.185 17.659 1.00 53.80 O
HETATM 1218 O HOH A1166 7.007 15.100 11.904 1.00 38.99 O
HETATM 1219 O HOH A1167 -17.616 -12.068 26.843 1.00 52.16 O
HETATM 1220 O HOH A1168 2.351 10.706 4.598 1.00 60.13 O
HETATM 1221 O HOH A1169 -0.014 -9.925 5.561 1.00 36.88 O
HETATM 1222 O HOH A1170 -12.912 7.328 21.544 1.00 49.46 O
HETATM 1223 O HOH A1171 6.679 8.875 5.345 1.00 57.45 O
HETATM 1224 O AHOH A1172 13.887 1.021 24.550 0.50 24.31 O
HETATM 1225 O BHOH A1172 13.601 3.091 25.085 0.50 25.68 O
HETATM 1226 O HOH A1173 -14.406 11.027 24.633 1.00 57.83 O
HETATM 1227 O HOH A1174 -11.718 -15.383 24.838 1.00 55.35 O
HETATM 1228 O HOH A1175 -10.630 -4.008 35.313 1.00 47.88 O
HETATM 1229 O HOH A1176 -11.960 4.571 8.957 1.00 39.40 O
HETATM 1230 O HOH A1177 -25.068 11.170 37.776 1.00 55.31 O
HETATM 1231 O HOH A1178 4.660 7.521 32.303 1.00 48.98 O
HETATM 1232 O HOH A1179 -1.239 -13.856 18.667 1.00 55.10 O
HETATM 1233 O HOH A1180 4.093 -2.517 36.449 1.00 52.16 O
HETATM 1234 O HOH A1181 2.035 -15.975 30.551 1.00 55.86 O
HETATM 1235 O HOH A1182 -0.759 -4.830 36.098 1.00 52.77 O
HETATM 1236 O HOH A1183 -20.839 -0.935 21.078 1.00 46.59 O
HETATM 1237 O HOH A1184 -21.139 3.241 26.511 1.00 50.36 O
HETATM 1238 O HOH A1185 -0.669 10.675 33.782 1.00 56.06 O
HETATM 1239 O HOH A1186 11.205 -3.485 2.733 1.00 44.32 O
HETATM 1240 O HOH A1187 -26.616 1.285 28.477 1.00 40.30 O
HETATM 1241 O HOH A1188 -8.936 6.509 14.997 1.00 38.32 O
HETATM 1242 O HOH A1189 -21.990 0.576 18.242 1.00 60.04 O
HETATM 1243 O HOH A1190 -6.225 -13.211 9.139 1.00 51.50 O
HETATM 1244 O HOH A1191 -24.686 -0.363 25.152 1.00 56.87 O
HETATM 1245 O HOH A1192 -13.820 -16.900 24.153 1.00 52.05 O
HETATM 1246 O HOH A1193 11.350 8.530 5.912 1.00 49.66 O
HETATM 1247 O HOH A1194 -29.032 -7.391 30.314 1.00 49.54 O
HETATM 1248 O HOH A1195 -28.187 0.672 26.501 1.00 39.72 O
CONECT 6 5 1092
CONECT 29 28 129
CONECT 129 29 128
CONECT 277 276 1046
CONECT 575 1147
CONECT 576 1147
CONECT 614 1147
CONECT 615 1147
CONECT 810 1146
CONECT 825 1146
CONECT 833 1147
CONECT 858 1147
CONECT 862 1146
CONECT 870 1147
CONECT 871 1148
CONECT 877 876 977
CONECT 945 1146
CONECT 950 1146
CONECT 953 1146
CONECT 977 877 976
CONECT 1046 277 1045
CONECT 1092 6 1091
CONECT 1134 1135 1133 1139
CONECT 1139 1097 1098 1134
CONECT 1098 1094 1138 1139
CONECT 1094 1095 1098 1137
CONECT 1095 1096 1094 1135
CONECT 1096 1095 1136
CONECT 1120 1121 1119
CONECT 1124 1121 1125
CONECT 1100 1101 1099
CONECT 1104 1101 1105
CONECT 1119 1120 1118
CONECT 1125 1124 1118
CONECT 1099 1100 1106
CONECT 1105 1104 1106
CONECT 1140 1097 1143
CONECT 1144 1145 1143
CONECT 1130 1131 1129
CONECT 1122 1121 1123
CONECT 1102 1101 1103
CONECT 1129 1128 1130
CONECT 1117 1118 1116
CONECT 1107 1106 1108
CONECT 1126 1113 1127
CONECT 1112 1111 1132
CONECT 1114 1113 1115 1116
CONECT 1109 1108 1110 1111
CONECT 1121 1120 1122 1124
CONECT 1101 1100 1102 1104
CONECT 1118 1117 1119 1125
CONECT 1106 1105 1107 1099
CONECT 1143 1140 1142 1144
CONECT 1127 1128 1126 1132
CONECT 1132 1112 1133 1127
CONECT 1113 1111 1126 1114
CONECT 1111 1109 1112 1113
CONECT 1131 1130
CONECT 1097 1140 1141 1139
CONECT 1145 1144
CONECT 1142 1141 1143
CONECT 1141 1097 1142
CONECT 1116 1114 1117
CONECT 1108 1107 1109
CONECT 1133 1134 1132
CONECT 1138 1098
CONECT 1138 1146
CONECT 1137 1094
CONECT 1137 1146
CONECT 1135 1095 1134
CONECT 1136 1096
CONECT 1115 1114
CONECT 1110 1109
CONECT 1123 1122
CONECT 1103 1102
CONECT 1128 1129 1127
CONECT 1146 945 950 953 1137
CONECT 1146 810 825 1138 862
CONECT 1147 1180 575 576 614
CONECT 1147 615 833 858 870
CONECT 1148 1169 1190 1153 871
CONECT 1153 1148
CONECT 1169 1148
CONECT 1180 1147
CONECT 1190 1148
END
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