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*** 7DFR-ss ***elNémo ID: 2404010752441758533Job options:ID = 2404010752441758533 JOBID = 7DFR-ss 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 7DFR-ss HEADER OXIDOREDUCTASE 21-OCT-88 7DFR TITLE CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. THE TITLE 2 NADP+ HOLOENZYME AND THE FOLATE(DOT)NADP+ TERNARY COMPLEX. SUBSTRATE TITLE 3 BINDING AND A MODEL FOR THE TRANSITION STATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE; COMPND 3 CHAIN: A; COMPND 4 EC: 1.5.1.3; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID KEYWDS OXIDO-REDUCTASE, OXIDOREDUCTASE EXPDTA X-RAY DIFFRACTION AUTHOR C.BYSTROFF,S.J.OATLEY,J.KRAUT REVDAT 6 29-NOV-17 7DFR 1 KEYWDS HELIX REVDAT 5 24-FEB-09 7DFR 1 VERSN REVDAT 4 01-APR-03 7DFR 1 JRNL REVDAT 3 15-JUL-92 7DFR 2 CONECT REVDAT 2 15-OCT-90 7DFR 1 JRNL REVDAT 1 15-JUL-90 7DFR 0 JRNL AUTH C.BYSTROFF,S.J.OATLEY,J.KRAUT JRNL TITL CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE JRNL TITL 2 REDUCTASE: THE NADP+ HOLOENZYME AND THE FOLATE.NADP+ TERNARY JRNL TITL 3 COMPLEX. SUBSTRATE BINDING AND A MODEL FOR THE TRANSITION JRNL TITL 4 STATE. JRNL REF BIOCHEMISTRY V. 29 3263 1990 JRNL REFN ISSN 0006-2960 JRNL PMID 2185835 JRNL DOI 10.1021/BI00465A018 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.BYSTROFF,J.KRAUT REMARK 1 TITL CRYSTAL STRUCTURE OF UNLIGANDED ESCHERICHIA COLI REMARK 1 TITL 2 DIHYDROFOLATE REDUCTASE. LIGAND-INDUCED CONFORMATIONAL REMARK 1 TITL 3 CHANGES AND COOPERATIVITY IN BINDING REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 1 REFERENCE 2 REMARK 1 AUTH J.T.BOLIN,D.J.FILMAN,D.A.MATTHEWS,R.C.HAMLIN,J.KRAUT REMARK 1 TITL CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS REMARK 1 TITL 2 CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 ANGSTROMS REMARK 1 TITL 3 RESOLUTION. I. GENERAL FEATURES AND BINDING OF METHOTREXATE REMARK 1 REF J.BIOL.CHEM. V. 257 13650 1982 REMARK 1 REFN ISSN 0021-9258 REMARK 1 REFERENCE 3 REMARK 1 AUTH K.M.PERRY,J.J.ONUFFER,N.A.TOUCHETTE,C.S.HERNDON, REMARK 1 AUTH 2 M.S.GITTELMAN,C.R.MATTHEWS,J.-T.CHEN,R.J.MAYER,K.TAIRA, REMARK 1 AUTH 3 S.J.BENKOVIC,E.E.HOWELL,J.KRAUT REMARK 1 TITL EFFECT OF SINGLE AMINO ACID REPLACEMENTS ON THE FOLDING AND REMARK 1 TITL 2 STABILITY OF DIHYDROFOLATE REDUCTASE FROM ESCHERICHIA COLI REMARK 1 REF BIOCHEMISTRY V. 26 2674 1987 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 4 REMARK 1 AUTH D.J.FILMAN,J.T.BOLIN,D.A.MATTHEWS,J.KRAUT REMARK 1 TITL CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS REMARK 1 TITL 2 CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 ANGSTROMS REMARK 1 TITL 3 RESOLUTION. II. ENVIRONMENT OF BOUND NADPH AND IMPLICATIONS REMARK 1 TITL 4 FOR CATALYSIS REMARK 1 REF J.BIOL.CHEM. V. 257 13663 1982 REMARK 1 REFN ISSN 0021-9258 REMARK 1 REFERENCE 5 REMARK 1 AUTH K.W.VOLZ,D.A.MATTHEWS,R.A.ALDEN,S.T.FREER,C.HANSCH, REMARK 1 AUTH 2 B.T.KAUFMAN,J.KRAUT REMARK 1 TITL CRYSTAL STRUCTURE OF AVIAN DIHYDROFOLATE REDUCTASE REMARK 1 TITL 2 CONTAINING PHENYLTRIAZINE AND NADPH REMARK 1 REF J.BIOL.CHEM. V. 257 2528 1982 REMARK 1 REFN ISSN 0021-9258 REMARK 1 REFERENCE 6 REMARK 1 AUTH D.A.MATTHEWS REMARK 1 TITL INTERPRETATION OF NUCLEAR MAGNETIC RESONANCE SPECTRA FOR REMARK 1 TITL 2 LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE BASED ON THE REMARK 1 TITL 3 X-RAY STRUCTURE OF THE ENZYME-METHOTREXATE-NADPH COMPLEX REMARK 1 REF BIOCHEMISTRY V. 18 1602 1979 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 7 REMARK 1 AUTH D.A.MATTHEWS,R.A.ALDEN,S.T.FREER,N.-H.XUONG,J.KRAUT REMARK 1 TITL DIHYDROFOLATE REDUCTASE FROM LACTOBACILLUS CASEI. REMARK 1 TITL 2 STEREOCHEMISTRY OF NADPH BINDING REMARK 1 REF J.BIOL.CHEM. V. 254 4144 1979 REMARK 1 REFN ISSN 0021-9258 REMARK 1 REFERENCE 8 REMARK 1 AUTH M.POE,K.HOOGSTEEN,D.A.MATTHEWS REMARK 1 TITL PROTON MAGNETIC RESONANCE STUDIES ON ESCHERICHIA COLI REMARK 1 TITL 2 DIHYDROFOLATE REDUCTASE. ASSIGNMENT OF HISTIDINE C-2 PROTONS REMARK 1 TITL 3 IN BINARY COMPLEXES WITH FOLATES ON THE BASIS OF THE CRYSTAL REMARK 1 TITL 4 STRUCTURE WITH METHOTREXATE AND ON CHEMICAL MODIFICATIONS REMARK 1 REF J.BIOL.CHEM. V. 254 8143 1979 REMARK 1 REFN ISSN 0021-9258 REMARK 1 REFERENCE 9 REMARK 1 AUTH D.A.MATTHEWS,R.A.ALDEN,J.T.BOLIN,D.J.FILMAN,S.T.FREER, REMARK 1 AUTH 2 R.HAMLIN,W.G.J.HOL,R.L.KISLIUK,E.J.PASTORE,L.T.PLANTE, REMARK 1 AUTH 3 N.-H.XUONG,J.KRAUT REMARK 1 TITL DIHYDROFOLATE REDUCTASE FROM LACTOBACILLUS CASEI. X-RAY REMARK 1 TITL 2 STRUCTURE OF THE ENZYME-METHOTREXATE-NADPH COMPLEX REMARK 1 REF J.BIOL.CHEM. V. 253 6946 1978 REMARK 1 REFN ISSN 0021-9258 REMARK 1 REFERENCE 10 REMARK 1 AUTH C.D.BENNETT,J.A.RODKEY,J.M.SONDEY,R.HIRSCHMANN REMARK 1 TITL DIHYDROFOLATE REDUCTASE. THE AMINO ACID SEQUENCE OF THE REMARK 1 TITL 2 ENZYME FROM A METHOTREXATE-RESISTANT MUTANT OF ESCHERICHIA REMARK 1 TITL 3 COLI REMARK 1 REF BIOCHEMISTRY V. 17 1328 1978 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 11 REMARK 1 AUTH D.A.MATTHEWS,R.A.ALDEN,J.T.BOLIN,S.T.FREER,R.HAMLIN,N.XUONG, REMARK 1 AUTH 2 J.KRAUT,M.POE,M.WILLIAMS,K.HOOGSTEEN REMARK 1 TITL DIHYDROFOLATE REDUCTASE. X-RAY STRUCTURE OF THE BINARY REMARK 1 TITL 2 COMPLEX WITH METHOTREXATE REMARK 1 REF SCIENCE V. 197 452 1977 REMARK 1 REFN ISSN 0036-8075 REMARK 1 REFERENCE 12 REMARK 1 AUTH M.POE,N.J.GREENFIELD,J.M.HIRSHFIELD,M.N.WILLIAMS,K.HOOGSTEEN REMARK 1 TITL DIHYDROFOLATE REDUCTASE. PURIFICATION AND CHARACTERIZATION REMARK 1 TITL 2 OF THE ENZYME FROM AN AMETHOPTERIN-RESISTANT MUTANT OF REMARK 1 TITL 3 ESCHERICHIA COLI REMARK 1 REF BIOCHEMISTRY V. 11 1023 1972 REMARK 1 REFN ISSN 0006-2960 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PROLSQ REMARK 3 AUTHORS : KONNERT,HENDRICKSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : NULL REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : 0.245 REMARK 3 R VALUE (WORKING SET) : NULL REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA. REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL REMARK 3 FREE R VALUE (NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1229 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 80 REMARK 3 SOLVENT ATOMS : 55 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : 0.022 ; 0.020 REMARK 3 ANGLE DISTANCE (A) : 0.034 ; 0.025 REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.039 ; 0.035 REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : 0.022 ; 0.018 REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.232 ; 0.180 REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : 0.217 ; 0.300 REMARK 3 MULTIPLE TORSION (A) : 0.266 ; 0.300 REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : 0.273 ; 0.300 REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : 4.400 ; 5.000 REMARK 3 STAGGERED (DEGREES) : 23.600; 15.000 REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 2.595 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.847 ; 3.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.649 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.966 ; 3.000 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 7DFR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000179892. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.37 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.35000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 35.17500 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 35.17500 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 70.35000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A 401 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 402 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 403 LIES ON A SPECIAL POSITION. REMARK 400 REMARK 400 COMPOUND REMARK 400 RESIDUES 16 - 19 FORM A TYPE I BETA TURN. THIS PART OF REMARK 400 THE STRUCTURE IS DENOTED AS THE MET 20 LOOP. REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A 17 CG CD OE1 OE2 REMARK 470 ARG A 44 NE CZ NH1 NH2 REMARK 470 GLU A 48 CG CD OE1 OE2 REMARK 470 ARG A 52 CD NE CZ NH1 NH2 REMARK 470 ARG A 98 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 106 CD CE NZ REMARK 470 ASP A 116 OD1 OD2 REMARK 470 GLU A 120 OE1 OE2 REMARK 470 GLU A 129 CB CG CD OE1 OE2 REMARK 470 ASP A 131 CB CG OD1 OD2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OG SER A 148 O HOH A 239 2.03 REMARK 500 O GLN A 65 O HOH A 310 2.09 REMARK 500 ND1 HIS A 45 O5B NAP A 164 2.11 REMARK 500 O ARG A 158 O HOH A 212 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 305 O HOH A 305 4556 1.45 REMARK 500 O HOH A 311 O HOH A 311 4556 1.89 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 THR A 113 N THR A 113 CA -0.127 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP A 11 CB - CG - OD1 ANGL. DEV. = 8.4 DEGREES REMARK 500 ARG A 12 CD - NE - CZ ANGL. DEV. = -8.9 DEGREES REMARK 500 ARG A 33 CA - CB - CG ANGL. DEV. = 14.1 DEGREES REMARK 500 MET A 42 CG - SD - CE ANGL. DEV. = -12.6 DEGREES REMARK 500 ASN A 59 CA - CB - CG ANGL. DEV. = 17.1 DEGREES REMARK 500 LEU A 62 CA - CB - CG ANGL. DEV. = 15.4 DEGREES REMARK 500 ASP A 87 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES REMARK 500 THR A 113 C - N - CA ANGL. DEV. = 18.0 DEGREES REMARK 500 GLU A 118 CA - CB - CG ANGL. DEV. = 13.3 DEGREES REMARK 500 PRO A 130 C - N - CA ANGL. DEV. = 9.9 DEGREES REMARK 500 TYR A 151 O - C - N ANGL. DEV. = 10.2 DEGREES REMARK 500 ARG A 158 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES REMARK 500 ARG A 158 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 ASP A 11 20.93 93.01 REMARK 500 GLU A 17 -129.76 33.79 REMARK 500 PRO A 21 22.23 -60.93 REMARK 500 LEU A 36 133.47 -27.11 REMARK 500 ARG A 52 148.94 -179.00 REMARK 500 ALA A 84 -8.05 -53.03 REMARK 500 TYR A 128 175.35 -56.33 REMARK 500 PRO A 130 -54.49 -26.91 REMARK 500 PHE A 137 142.91 178.18 REMARK 500 ASP A 144 -168.25 -167.04 REMARK 500 SER A 148 -14.64 -45.73 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 12 0.20 SIDE CHAIN REMARK 500 ARG A 33 0.10 SIDE CHAIN REMARK 500 ARG A 159 0.11 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 HIS A 114 10.08 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOL A 161 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 164 DBREF 7DFR A 1 159 UNP P0ABQ4 DYR_ECOLI 1 159 SEQADV 7DFR ASP A 37 UNP P0ABQ4 ASN 37 CONFLICT SEQRES 1 A 159 MET ILE SER LEU ILE ALA ALA LEU ALA VAL ASP ARG VAL SEQRES 2 A 159 ILE GLY MET GLU ASN ALA MET PRO TRP ASN LEU PRO ALA SEQRES 3 A 159 ASP LEU ALA TRP PHE LYS ARG ASN THR LEU ASP LYS PRO SEQRES 4 A 159 VAL ILE MET GLY ARG HIS THR TRP GLU SER ILE GLY ARG SEQRES 5 A 159 PRO LEU PRO GLY ARG LYS ASN ILE ILE LEU SER SER GLN SEQRES 6 A 159 PRO GLY THR ASP ASP ARG VAL THR TRP VAL LYS SER VAL SEQRES 7 A 159 ASP GLU ALA ILE ALA ALA CYS GLY ASP VAL PRO GLU ILE SEQRES 8 A 159 MET VAL ILE GLY GLY GLY ARG VAL TYR GLU GLN PHE LEU SEQRES 9 A 159 PRO LYS ALA GLN LYS LEU TYR LEU THR HIS ILE ASP ALA SEQRES 10 A 159 GLU VAL GLU GLY ASP THR HIS PHE PRO ASP TYR GLU PRO SEQRES 11 A 159 ASP ASP TRP GLU SER VAL PHE SER GLU PHE HIS ASP ALA SEQRES 12 A 159 ASP ALA GLN ASN SER HIS SER TYR CYS PHE GLU ILE LEU SEQRES 13 A 159 GLU ARG ARG HET FOL A 161 32 HET NAP A 164 48 HETNAM FOL FOLIC ACID HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE FORMUL 2 FOL C19 H19 N7 O6 FORMUL 3 NAP C21 H28 N7 O17 P3 FORMUL 4 HOH *55(H2 O) HELIX 1 HB LEU A 24 THR A 35 1 12 HELIX 2 HC GLY A 43 ILE A 50 1 8 HELIX 3 HE SER A 77 GLY A 86 1 10 HELIX 4 HF GLY A 96 LEU A 104 1 9 SHEET 1 S1 8 THR A 73 VAL A 75 0 SHEET 2 S1 8 LYS A 58 SER A 63 1 O ASN A 59 N THR A 73 SHEET 3 S1 8 PRO A 39 GLY A 43 1 N VAL A 40 O LYS A 58 SHEET 4 S1 8 ILE A 91 GLY A 95 1 N MET A 92 O PRO A 39 SHEET 5 S1 8 MET A 1 LEU A 8 1 O MET A 1 N ILE A 91 SHEET 6 S1 8 GLN A 108 ASP A 116 1 O LYS A 109 N LEU A 4 SHEET 7 S1 8 SER A 150 ARG A 159 -1 N ARG A 158 O GLN A 108 SHEET 8 S1 8 ASP A 132 HIS A 141 -1 N GLU A 134 O GLU A 157 SSBOND 1 CYS A 152 CYS A 152 1555 4556 2.56 CISPEP 1 GLY A 95 GLY A 96 0 -2.73 SITE 1 AC1 15 ILE A 5 ALA A 7 MET A 20 ASP A 27 SITE 2 AC1 15 LEU A 28 PHE A 31 LYS A 32 THR A 46 SITE 3 AC1 15 ILE A 50 ARG A 57 ILE A 94 THR A 113 SITE 4 AC1 15 NAP A 164 HOH A 206 HOH A 301 SITE 1 AC2 27 ALA A 6 ALA A 7 ILE A 14 MET A 16 SITE 2 AC2 27 ASN A 18 ALA A 19 MET A 20 TRP A 22 SITE 3 AC2 27 GLY A 43 ARG A 44 HIS A 45 THR A 46 SITE 4 AC2 27 SER A 49 LEU A 62 SER A 63 SER A 64 SITE 5 AC2 27 LYS A 76 ILE A 94 GLY A 96 GLY A 97 SITE 6 AC2 27 ARG A 98 VAL A 99 TYR A 100 GLN A 102 SITE 7 AC2 27 FOL A 161 HOH A 225 HOH A 237 CRYST1 62.207 62.207 105.525 90.00 90.00 120.00 P 32 2 1 6 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 0.016075 0.009281 0.000000 0.00000 SCALE2 0.000000 0.018562 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009476 0.00000 ATOM 1 N MET A 1 2.670 11.839 29.667 1.00 57.65 N ATOM 2 CA MET A 1 2.666 13.148 30.331 1.00 55.69 C ATOM 3 C MET A 1 4.018 13.829 30.165 1.00 52.87 C ATOM 4 O MET A 1 5.026 13.169 29.884 1.00 56.23 O ATOM 5 CB MET A 1 2.440 12.983 31.860 1.00 59.22 C ATOM 6 CG MET A 1 3.626 12.235 32.476 1.00 62.17 C ATOM 7 SD MET A 1 3.395 12.185 34.265 1.00 67.25 S ATOM 8 CE MET A 1 5.106 12.596 34.775 1.00 66.67 C ATOM 9 N ILE A 2 4.001 15.102 30.384 1.00 50.83 N ATOM 10 CA ILE A 2 5.158 16.012 30.412 1.00 48.49 C ATOM 11 C ILE A 2 5.438 16.382 31.892 1.00 47.79 C ATOM 12 O ILE A 2 4.491 16.578 32.695 1.00 46.73 O ATOM 13 CB ILE A 2 4.818 17.300 29.574 1.00 44.62 C ATOM 14 CG1 ILE A 2 4.416 16.868 28.153 1.00 48.44 C ATOM 15 CG2 ILE A 2 5.907 18.361 29.608 1.00 45.17 C ATOM 16 CD1 ILE A 2 4.628 17.969 27.049 1.00 48.16 C ATOM 17 N SER A 3 6.705 16.545 32.193 1.00 45.68 N ATOM 18 CA SER A 3 7.193 16.933 33.519 1.00 42.07 C ATOM 19 C SER A 3 8.277 17.993 33.392 1.00 42.60 C ATOM 20 O SER A 3 9.154 17.903 32.523 1.00 45.04 O ATOM 21 CB SER A 3 7.691 15.733 34.305 1.00 39.85 C ATOM 22 OG SER A 3 6.568 14.955 34.778 1.00 39.13 O ATOM 23 N LEU A 4 8.200 18.975 34.247 1.00 43.21 N ATOM 24 CA LEU A 4 9.269 20.008 34.399 1.00 44.23 C ATOM 25 C LEU A 4 10.140 19.541 35.615 1.00 40.41 C ATOM 26 O LEU A 4 9.622 18.912 36.560 1.00 44.22 O ATOM 27 CB LEU A 4 8.658 21.359 34.644 1.00 45.01 C ATOM 28 CG LEU A 4 8.199 22.300 33.584 1.00 46.79 C ATOM 29 CD1 LEU A 4 7.940 21.680 32.216 1.00 46.27 C ATOM 30 CD2 LEU A 4 6.882 22.937 34.066 1.00 50.25 C ATOM 31 N ILE A 5 11.394 19.807 35.531 1.00 34.88 N ATOM 32 CA ILE A 5 12.391 19.498 36.536 1.00 31.71 C ATOM 33 C ILE A 5 13.260 20.724 36.677 1.00 35.31 C ATOM 34 O ILE A 5 13.788 21.283 35.651 1.00 33.33 O ATOM 35 CB ILE A 5 13.006 18.093 36.286 1.00 35.24 C ATOM 36 CG1 ILE A 5 13.291 17.363 37.616 1.00 33.21 C ATOM 37 CG2 ILE A 5 14.167 18.000 35.253 1.00 32.24 C ATOM 38 CD1 ILE A 5 14.424 16.373 37.757 1.00 29.34 C ATOM 39 N ALA A 6 13.235 21.304 37.905 1.00 30.50 N ATOM 40 CA ALA A 6 14.080 22.434 38.227 1.00 29.24 C ATOM 41 C ALA A 6 14.464 22.400 39.758 1.00 30.69 C ATOM 42 O ALA A 6 13.917 21.654 40.555 1.00 28.86 O ATOM 43 CB ALA A 6 13.440 23.764 37.893 1.00 25.74 C ATOM 44 N ALA A 7 15.492 23.157 40.050 1.00 28.94 N ATOM 45 CA ALA A 7 16.117 23.519 41.260 1.00 29.77 C ATOM 46 C ALA A 7 16.010 25.052 41.412 1.00 33.00 C ATOM 47 O ALA A 7 16.715 25.814 40.710 1.00 34.24 O ATOM 48 CB ALA A 7 17.553 23.099 41.390 1.00 23.26 C ATOM 49 N LEU A 8 15.180 25.434 42.348 1.00 36.07 N ATOM 50 CA LEU A 8 14.949 26.878 42.618 1.00 35.42 C ATOM 51 C LEU A 8 15.655 27.284 43.919 1.00 33.09 C ATOM 52 O LEU A 8 15.472 26.584 44.893 1.00 32.86 O ATOM 53 CB LEU A 8 13.410 27.025 42.791 1.00 34.07 C ATOM 54 CG LEU A 8 12.584 26.900 41.539 1.00 34.73 C ATOM 55 CD1 LEU A 8 12.764 25.462 41.018 1.00 40.48 C ATOM 56 CD2 LEU A 8 11.090 27.116 41.798 1.00 32.29 C ATOM 57 N ALA A 9 16.356 28.368 43.876 1.00 33.73 N ATOM 58 CA ALA A 9 16.931 29.056 45.017 1.00 36.85 C ATOM 59 C ALA A 9 15.795 29.952 45.551 1.00 40.51 C ATOM 60 O ALA A 9 14.631 29.796 45.167 1.00 41.64 O ATOM 61 CB ALA A 9 18.147 29.863 44.647 1.00 33.79 C ATOM 62 N VAL A 10 16.161 30.946 46.355 1.00 46.75 N ATOM 63 CA VAL A 10 15.122 31.826 46.958 1.00 46.61 C ATOM 64 C VAL A 10 14.649 32.823 45.930 1.00 47.57 C ATOM 65 O VAL A 10 15.532 33.474 45.316 1.00 49.64 O ATOM 66 CB VAL A 10 15.598 32.388 48.304 1.00 46.06 C ATOM 67 CG1 VAL A 10 15.108 33.766 48.679 1.00 46.08 C ATOM 68 CG2 VAL A 10 15.116 31.454 49.450 1.00 46.89 C ATOM 69 N ASP A 11 13.334 32.912 45.799 1.00 47.15 N ATOM 70 CA ASP A 11 12.741 33.947 44.881 1.00 49.18 C ATOM 71 C ASP A 11 12.532 33.314 43.534 1.00 49.07 C ATOM 72 O ASP A 11 12.474 34.011 42.505 1.00 53.15 O ATOM 73 CB ASP A 11 13.654 35.145 44.965 1.00 54.74 C ATOM 74 CG ASP A 11 13.367 36.455 44.379 1.00 58.99 C ATOM 75 OD1 ASP A 11 13.357 37.547 44.970 1.00 57.89 O ATOM 76 OD2 ASP A 11 13.222 36.454 43.101 1.00 66.34 O ATOM 77 N ARG A 12 12.472 32.006 43.521 1.00 46.95 N ATOM 78 CA ARG A 12 12.272 31.203 42.306 1.00 45.82 C ATOM 79 C ARG A 12 13.401 31.342 41.314 1.00 43.83 C ATOM 80 O ARG A 12 13.266 31.012 40.122 1.00 46.30 O ATOM 81 CB ARG A 12 10.879 31.465 41.769 1.00 46.82 C ATOM 82 CG ARG A 12 9.809 30.833 42.693 1.00 47.68 C ATOM 83 CD ARG A 12 8.858 29.981 41.964 1.00 53.23 C ATOM 84 NE ARG A 12 7.553 30.652 41.712 1.00 55.26 N ATOM 85 CZ ARG A 12 7.647 31.873 41.144 1.00 56.78 C ATOM 86 NH1 ARG A 12 8.703 32.113 40.367 1.00 56.05 N ATOM 87 NH2 ARG A 12 6.820 32.836 41.527 1.00 58.51 N ATOM 88 N VAL A 13 14.578 31.703 41.793 1.00 37.25 N ATOM 89 CA VAL A 13 15.784 31.923 41.111 1.00 38.46 C ATOM 90 C VAL A 13 16.438 30.624 40.572 1.00 43.61 C ATOM 91 O VAL A 13 16.958 29.822 41.355 1.00 43.59 O ATOM 92 CB VAL A 13 16.842 32.701 41.950 1.00 34.38 C ATOM 93 CG1 VAL A 13 18.256 32.543 41.403 1.00 34.12 C ATOM 94 CG2 VAL A 13 16.516 34.153 42.090 1.00 34.96 C ATOM 95 N ILE A 14 16.586 30.619 39.235 1.00 41.60 N ATOM 96 CA ILE A 14 17.186 29.494 38.555 1.00 39.31 C ATOM 97 C ILE A 14 18.540 29.708 37.924 1.00 40.54 C ATOM 98 O ILE A 14 19.193 28.671 37.566 1.00 40.49 O ATOM 99 CB ILE A 14 16.158 28.748 37.691 1.00 38.52 C ATOM 100 CG1 ILE A 14 15.762 29.655 36.433 1.00 34.59 C ATOM 101 CG2 ILE A 14 14.895 28.201 38.368 1.00 33.07 C ATOM 102 CD1 ILE A 14 14.977 28.668 35.472 1.00 32.55 C ATOM 103 N GLY A 15 19.108 30.920 37.906 1.00 40.01 N ATOM 104 CA GLY A 15 20.449 31.074 37.367 1.00 36.77 C ATOM 105 C GLY A 15 20.892 32.518 37.187 1.00 37.50 C ATOM 106 O GLY A 15 20.091 33.428 37.324 1.00 31.44 O ATOM 107 N MET A 16 22.156 32.609 36.901 1.00 42.98 N ATOM 108 CA MET A 16 22.965 33.786 36.616 1.00 52.29 C ATOM 109 C MET A 16 23.915 33.468 35.449 1.00 56.60 C ATOM 110 O MET A 16 23.979 32.264 35.047 1.00 59.33 O ATOM 111 CB MET A 16 23.811 34.172 37.828 1.00 54.92 C ATOM 112 CG MET A 16 24.464 35.508 37.725 1.00 58.53 C ATOM 113 SD MET A 16 23.214 36.803 37.962 1.00 64.25 S ATOM 114 CE MET A 16 24.375 37.997 38.748 1.00 61.74 C ATOM 115 N GLU A 17 24.616 34.456 34.924 1.00 59.45 N ATOM 116 CA GLU A 17 25.420 34.202 33.666 1.00 61.56 C ATOM 117 C GLU A 17 24.529 33.171 32.921 1.00 62.91 C ATOM 118 O GLU A 17 23.267 33.366 32.928 1.00 64.21 O ATOM 119 CB GLU A 17 26.765 33.604 33.870 1.00 61.00 C ATOM 120 N ASN A 18 25.130 32.110 32.507 1.00 61.66 N ATOM 121 CA ASN A 18 24.345 30.938 31.964 1.00 62.01 C ATOM 122 C ASN A 18 24.830 29.814 32.921 1.00 61.57 C ATOM 123 O ASN A 18 25.361 28.798 32.473 1.00 64.33 O ATOM 124 CB ASN A 18 24.581 30.704 30.523 1.00 62.84 C ATOM 125 CG ASN A 18 23.664 29.895 29.696 1.00 64.98 C ATOM 126 OD1 ASN A 18 24.108 29.231 28.703 1.00 66.14 O ATOM 127 ND2 ASN A 18 22.359 29.864 30.012 1.00 64.57 N ATOM 128 N ALA A 19 24.762 30.167 34.198 1.00 59.74 N ATOM 129 CA ALA A 19 25.199 29.288 35.279 1.00 57.90 C ATOM 130 C ALA A 19 24.195 29.209 36.435 1.00 58.09 C ATOM 131 O ALA A 19 23.197 29.956 36.553 1.00 59.66 O ATOM 132 CB ALA A 19 26.579 29.641 35.754 1.00 57.00 C ATOM 133 N MET A 20 24.485 28.237 37.284 1.00 53.49 N ATOM 134 CA MET A 20 23.719 27.956 38.498 1.00 50.47 C ATOM 135 C MET A 20 24.588 28.394 39.689 1.00 48.74 C ATOM 136 O MET A 20 25.657 27.815 39.922 1.00 51.37 O ATOM 137 CB MET A 20 23.274 26.520 38.622 1.00 49.72 C ATOM 138 CG MET A 20 22.253 26.191 37.547 1.00 51.31 C ATOM 139 SD MET A 20 21.520 24.601 37.975 1.00 51.75 S ATOM 140 CE MET A 20 23.009 23.588 37.700 1.00 52.52 C ATOM 141 N PRO A 21 24.129 29.422 40.348 1.00 46.06 N ATOM 142 CA PRO A 21 24.814 30.057 41.435 1.00 48.25 C ATOM 143 C PRO A 21 25.095 29.188 42.654 1.00 48.40 C ATOM 144 O PRO A 21 25.372 29.738 43.754 1.00 48.81 O ATOM 145 CB PRO A 21 23.966 31.284 41.792 1.00 49.26 C ATOM 146 CG PRO A 21 22.714 31.241 40.996 1.00 47.22 C ATOM 147 CD PRO A 21 22.856 30.127 39.994 1.00 48.68 C ATOM 148 N TRP A 22 25.117 27.896 42.480 1.00 45.09 N ATOM 149 CA TRP A 22 25.332 26.913 43.539 1.00 41.23 C ATOM 150 C TRP A 22 25.964 25.659 42.919 1.00 43.55 C ATOM 151 O TRP A 22 25.917 25.512 41.701 1.00 44.41 O ATOM 152 CB TRP A 22 23.946 26.466 44.104 1.00 34.47 C ATOM 153 CG TRP A 22 22.963 25.953 43.134 1.00 30.19 C ATOM 154 CD1 TRP A 22 22.881 24.673 42.624 1.00 29.54 C ATOM 155 CD2 TRP A 22 21.827 26.635 42.582 1.00 27.57 C ATOM 156 NE1 TRP A 22 21.774 24.506 41.839 1.00 25.43 N ATOM 157 CE2 TRP A 22 21.132 25.730 41.761 1.00 25.83 C ATOM 158 CE3 TRP A 22 21.359 27.953 42.709 1.00 30.12 C ATOM 159 CZ2 TRP A 22 19.952 26.073 41.086 1.00 23.62 C ATOM 160 CZ3 TRP A 22 20.220 28.324 41.947 1.00 27.57 C ATOM 161 CH2 TRP A 22 19.485 27.369 41.247 1.00 22.32 C ATOM 162 N ASN A 23 26.422 24.834 43.813 1.00 46.46 N ATOM 163 CA ASN A 23 27.060 23.547 43.501 1.00 46.49 C ATOM 164 C ASN A 23 26.540 22.493 44.492 1.00 42.71 C ATOM 165 O ASN A 23 27.061 22.497 45.625 1.00 43.69 O ATOM 166 CB ASN A 23 28.573 23.759 43.683 1.00 51.26 C ATOM 167 CG ASN A 23 29.316 22.911 42.659 1.00 57.88 C ATOM 168 OD1 ASN A 23 29.245 21.678 42.696 1.00 60.73 O ATOM 169 ND2 ASN A 23 29.979 23.621 41.733 1.00 60.35 N ATOM 170 N LEU A 24 25.690 21.615 44.064 1.00 36.80 N ATOM 171 CA LEU A 24 25.014 20.591 44.764 1.00 32.19 C ATOM 172 C LEU A 24 24.966 19.246 44.072 1.00 32.08 C ATOM 173 O LEU A 24 23.876 18.767 43.628 1.00 32.21 O ATOM 174 CB LEU A 24 23.535 21.118 44.989 1.00 31.90 C ATOM 175 CG LEU A 24 23.400 22.466 45.646 1.00 30.85 C ATOM 176 CD1 LEU A 24 21.975 22.636 46.215 1.00 30.95 C ATOM 177 CD2 LEU A 24 24.339 22.531 46.889 1.00 27.75 C ATOM 178 N PRO A 25 26.107 18.566 44.038 1.00 29.38 N ATOM 179 CA PRO A 25 26.236 17.262 43.457 1.00 27.13 C ATOM 180 C PRO A 25 25.084 16.352 43.752 1.00 32.21 C ATOM 181 O PRO A 25 24.786 15.433 42.965 1.00 40.18 O ATOM 182 CB PRO A 25 27.556 16.731 44.025 1.00 28.68 C ATOM 183 CG PRO A 25 28.235 17.818 44.736 1.00 29.63 C ATOM 184 CD PRO A 25 27.420 19.103 44.471 1.00 32.06 C ATOM 185 N ALA A 26 24.461 16.449 44.919 1.00 31.57 N ATOM 186 CA ALA A 26 23.389 15.536 45.302 1.00 29.57 C ATOM 187 C ALA A 26 22.080 15.940 44.619 1.00 26.13 C ATOM 188 O ALA A 26 21.201 15.062 44.507 1.00 25.67 O ATOM 189 CB ALA A 26 23.278 15.498 46.856 1.00 31.33 C ATOM 190 N ASP A 27 21.969 17.166 44.226 1.00 24.19 N ATOM 191 CA ASP A 27 20.760 17.614 43.444 1.00 29.52 C ATOM 192 C ASP A 27 20.841 16.969 42.017 1.00 29.76 C ATOM 193 O ASP A 27 19.922 16.340 41.526 1.00 28.75 O ATOM 194 CB ASP A 27 20.652 19.114 43.406 1.00 29.31 C ATOM 195 CG ASP A 27 19.477 19.578 42.529 1.00 32.82 C ATOM 196 OD1 ASP A 27 18.370 19.070 42.708 1.00 28.38 O ATOM 197 OD2 ASP A 27 19.743 20.513 41.739 1.00 34.89 O ATOM 198 N LEU A 28 21.993 17.056 41.431 1.00 32.33 N ATOM 199 CA LEU A 28 22.305 16.512 40.109 1.00 34.74 C ATOM 200 C LEU A 28 22.086 15.026 40.076 1.00 37.89 C ATOM 201 O LEU A 28 21.677 14.508 38.985 1.00 40.61 O ATOM 202 CB LEU A 28 23.778 16.878 39.797 1.00 35.13 C ATOM 203 CG LEU A 28 23.937 18.407 39.564 1.00 31.81 C ATOM 204 CD1 LEU A 28 25.276 18.681 38.980 1.00 35.70 C ATOM 205 CD2 LEU A 28 22.820 18.743 38.575 1.00 33.47 C ATOM 206 N ALA A 29 22.374 14.421 41.195 1.00 34.63 N ATOM 207 CA ALA A 29 22.221 12.950 41.342 1.00 33.93 C ATOM 208 C ALA A 29 20.763 12.593 41.287 1.00 33.51 C ATOM 209 O ALA A 29 20.320 11.564 40.691 1.00 35.04 O ATOM 210 CB ALA A 29 22.763 12.623 42.782 1.00 36.62 C ATOM 211 N TRP A 30 20.030 13.511 41.894 1.00 32.66 N ATOM 212 CA TRP A 30 18.557 13.395 41.983 1.00 33.92 C ATOM 213 C TRP A 30 17.989 13.724 40.613 1.00 33.47 C ATOM 214 O TRP A 30 17.009 13.082 40.196 1.00 38.79 O ATOM 215 CB TRP A 30 17.956 14.231 43.072 1.00 29.04 C ATOM 216 CG TRP A 30 16.631 14.868 42.776 1.00 28.11 C ATOM 217 CD1 TRP A 30 16.366 16.081 42.201 1.00 26.02 C ATOM 218 CD2 TRP A 30 15.357 14.383 43.222 1.00 24.69 C ATOM 219 NE1 TRP A 30 15.004 16.313 42.184 1.00 23.73 N ATOM 220 CE2 TRP A 30 14.392 15.283 42.819 1.00 22.95 C ATOM 221 CE3 TRP A 30 14.978 13.216 43.879 1.00 26.89 C ATOM 222 CZ2 TRP A 30 13.043 15.123 43.131 1.00 25.41 C ATOM 223 CZ3 TRP A 30 13.646 13.060 44.160 1.00 26.66 C ATOM 224 CH2 TRP A 30 12.686 13.961 43.791 1.00 24.31 C ATOM 225 N PHE A 31 18.550 14.722 40.024 1.00 35.71 N ATOM 226 CA PHE A 31 18.149 15.161 38.635 1.00 38.52 C ATOM 227 C PHE A 31 18.280 13.915 37.720 1.00 38.99 C ATOM 228 O PHE A 31 17.300 13.353 37.271 1.00 41.55 O ATOM 229 CB PHE A 31 19.039 16.291 38.149 1.00 36.79 C ATOM 230 CG PHE A 31 19.067 16.481 36.663 1.00 39.33 C ATOM 231 CD1 PHE A 31 18.094 17.292 36.027 1.00 37.54 C ATOM 232 CD2 PHE A 31 19.965 15.760 35.892 1.00 40.10 C ATOM 233 CE1 PHE A 31 18.100 17.453 34.670 1.00 36.76 C ATOM 234 CE2 PHE A 31 20.002 15.930 34.486 1.00 41.84 C ATOM 235 CZ PHE A 31 19.095 16.806 33.877 1.00 38.14 C ATOM 236 N LYS A 32 19.484 13.444 37.623 1.00 38.75 N ATOM 237 CA LYS A 32 19.904 12.286 36.870 1.00 41.01 C ATOM 238 C LYS A 32 19.022 11.088 37.106 1.00 45.06 C ATOM 239 O LYS A 32 18.658 10.339 36.180 1.00 46.89 O ATOM 240 CB LYS A 32 21.349 11.929 37.205 1.00 41.82 C ATOM 241 CG LYS A 32 21.693 10.466 36.885 1.00 42.38 C ATOM 242 CD LYS A 32 23.194 10.363 36.680 1.00 43.06 C ATOM 243 CE LYS A 32 23.505 9.446 35.509 1.00 48.54 C ATOM 244 NZ LYS A 32 24.971 9.111 35.506 1.00 51.40 N ATOM 245 N ARG A 33 18.713 10.902 38.378 1.00 46.56 N ATOM 246 CA ARG A 33 17.885 9.694 38.762 1.00 44.65 C ATOM 247 C ARG A 33 16.514 9.874 38.222 1.00 45.01 C ATOM 248 O ARG A 33 15.805 8.889 37.892 1.00 46.36 O ATOM 249 CB ARG A 33 18.093 9.457 40.224 1.00 46.97 C ATOM 250 CG ARG A 33 17.062 9.230 41.251 1.00 48.91 C ATOM 251 CD ARG A 33 17.635 8.666 42.538 1.00 48.78 C ATOM 252 NE ARG A 33 17.403 9.552 43.694 1.00 47.12 N ATOM 253 CZ ARG A 33 18.457 10.185 44.245 1.00 48.96 C ATOM 254 NH1 ARG A 33 19.716 9.789 43.986 1.00 46.96 N ATOM 255 NH2 ARG A 33 18.255 11.251 45.020 1.00 47.52 N ATOM 256 N ASN A 34 16.055 11.139 38.098 1.00 43.72 N ATOM 257 CA ASN A 34 14.686 11.394 37.636 1.00 41.40 C ATOM 258 C ASN A 34 14.497 11.348 36.147 1.00 40.18 C ATOM 259 O ASN A 34 13.330 11.073 35.714 1.00 41.89 O ATOM 260 CB ASN A 34 14.104 12.684 38.292 1.00 41.52 C ATOM 261 CG ASN A 34 13.642 12.206 39.692 1.00 43.80 C ATOM 262 OD1 ASN A 34 12.621 11.551 39.793 1.00 44.24 O ATOM 263 ND2 ASN A 34 14.480 12.476 40.674 1.00 45.06 N ATOM 264 N THR A 35 15.533 11.636 35.406 1.00 38.39 N ATOM 265 CA THR A 35 15.530 11.684 33.958 1.00 40.10 C ATOM 266 C THR A 35 16.012 10.466 33.219 1.00 39.28 C ATOM 267 O THR A 35 15.456 10.120 32.171 1.00 44.20 O ATOM 268 CB THR A 35 16.371 12.962 33.427 1.00 37.37 C ATOM 269 OG1 THR A 35 17.717 12.745 33.874 1.00 33.21 O ATOM 270 CG2 THR A 35 15.689 14.250 33.910 1.00 34.78 C ATOM 271 N LEU A 36 17.060 9.871 33.661 1.00 42.28 N ATOM 272 CA LEU A 36 17.695 8.706 33.060 1.00 41.79 C ATOM 273 C LEU A 36 16.644 7.893 32.284 1.00 41.54 C ATOM 274 O LEU A 36 15.559 7.657 32.762 1.00 40.33 O ATOM 275 CB LEU A 36 18.347 7.888 34.176 1.00 40.57 C ATOM 276 CG LEU A 36 19.499 7.019 33.644 1.00 44.74 C ATOM 277 CD1 LEU A 36 20.630 7.911 33.178 1.00 43.50 C ATOM 278 CD2 LEU A 36 19.917 6.039 34.745 1.00 40.81 C ATOM 279 N ASP A 37 17.065 7.537 31.070 1.00 42.43 N ATOM 280 CA ASP A 37 16.252 6.692 30.206 1.00 41.92 C ATOM 281 C ASP A 37 14.931 7.340 29.846 1.00 42.68 C ATOM 282 O ASP A 37 13.929 6.635 29.600 1.00 44.81 O ATOM 283 CB ASP A 37 16.220 5.283 30.810 1.00 42.69 C ATOM 284 CG ASP A 37 17.591 4.619 30.777 1.00 47.91 C ATOM 285 OD1 ASP A 37 18.527 5.031 30.021 1.00 49.73 O ATOM 286 OD2 ASP A 37 17.817 3.649 31.537 1.00 47.80 O ATOM 287 N LYS A 38 14.907 8.652 29.713 1.00 39.55 N ATOM 288 CA LYS A 38 13.775 9.453 29.321 1.00 39.47 C ATOM 289 C LYS A 38 14.352 10.612 28.444 1.00 39.62 C ATOM 290 O LYS A 38 15.516 10.979 28.610 1.00 40.58 O ATOM 291 CB LYS A 38 12.990 10.152 30.421 1.00 41.88 C ATOM 292 CG LYS A 38 12.556 9.284 31.599 1.00 44.60 C ATOM 293 CD LYS A 38 12.382 10.100 32.874 1.00 44.28 C ATOM 294 CE LYS A 38 12.073 9.145 34.019 1.00 46.91 C ATOM 295 NZ LYS A 38 10.916 9.612 34.795 1.00 51.13 N ATOM 296 N PRO A 39 13.501 11.092 27.587 1.00 37.78 N ATOM 297 CA PRO A 39 13.839 12.203 26.711 1.00 38.85 C ATOM 298 C PRO A 39 13.934 13.493 27.508 1.00 37.67 C ATOM 299 O PRO A 39 12.997 13.784 28.272 1.00 39.78 O ATOM 300 CB PRO A 39 12.664 12.269 25.728 1.00 37.73 C ATOM 301 CG PRO A 39 11.691 11.220 26.085 1.00 37.81 C ATOM 302 CD PRO A 39 12.106 10.607 27.382 1.00 39.09 C ATOM 303 N VAL A 40 14.932 14.319 27.262 1.00 37.10 N ATOM 304 CA VAL A 40 14.994 15.619 27.950 1.00 35.59 C ATOM 305 C VAL A 40 15.053 16.772 26.978 1.00 39.38 C ATOM 306 O VAL A 40 16.012 16.842 26.154 1.00 43.15 O ATOM 307 CB VAL A 40 16.129 15.659 28.993 1.00 33.26 C ATOM 308 CG1 VAL A 40 16.065 14.447 29.911 1.00 29.76 C ATOM 309 CG2 VAL A 40 17.510 15.891 28.451 1.00 31.02 C ATOM 310 N ILE A 41 14.092 17.686 27.119 1.00 37.50 N ATOM 311 CA ILE A 41 13.996 18.880 26.354 1.00 37.17 C ATOM 312 C ILE A 41 14.643 20.068 27.083 1.00 39.06 C ATOM 313 O ILE A 41 14.224 20.393 28.187 1.00 41.77 O ATOM 314 CB ILE A 41 12.515 19.317 26.017 1.00 36.94 C ATOM 315 CG1 ILE A 41 11.736 18.203 25.399 1.00 37.63 C ATOM 316 CG2 ILE A 41 12.545 20.623 25.128 1.00 38.56 C ATOM 317 CD1 ILE A 41 10.252 18.438 25.073 1.00 39.11 C ATOM 318 N MET A 42 15.534 20.726 26.415 1.00 40.56 N ATOM 319 CA MET A 42 16.270 21.884 26.866 1.00 40.28 C ATOM 320 C MET A 42 16.153 22.977 25.773 1.00 45.55 C ATOM 321 O MET A 42 15.499 22.659 24.758 1.00 52.10 O ATOM 322 CB MET A 42 17.740 21.643 27.051 1.00 39.48 C ATOM 323 CG MET A 42 18.269 20.307 27.199 1.00 37.11 C ATOM 324 SD MET A 42 20.150 20.471 27.023 1.00 39.33 S ATOM 325 CE MET A 42 20.188 18.680 26.580 1.00 37.48 C ATOM 326 N GLY A 43 16.871 24.043 25.955 1.00 43.62 N ATOM 327 CA GLY A 43 16.932 25.190 25.092 1.00 44.22 C ATOM 328 C GLY A 43 18.401 25.559 24.813 1.00 44.77 C ATOM 329 O GLY A 43 19.284 25.296 25.638 1.00 44.52 O ATOM 330 N ARG A 44 18.600 26.241 23.691 1.00 43.48 N ATOM 331 CA ARG A 44 19.997 26.507 23.277 1.00 45.14 C ATOM 332 C ARG A 44 20.818 26.881 24.469 1.00 43.01 C ATOM 333 O ARG A 44 21.895 26.250 24.584 1.00 48.71 O ATOM 334 CB ARG A 44 20.233 27.340 22.033 1.00 43.21 C ATOM 335 CG ARG A 44 21.627 27.926 21.802 1.00 41.23 C ATOM 336 CD ARG A 44 21.506 29.436 21.520 1.00 44.40 C ATOM 337 N HIS A 45 20.428 27.811 25.307 1.00 43.36 N ATOM 338 CA HIS A 45 21.322 28.236 26.418 1.00 43.39 C ATOM 339 C HIS A 45 21.578 27.169 27.469 1.00 37.62 C ATOM 340 O HIS A 45 22.721 27.130 27.921 1.00 37.87 O ATOM 341 CB HIS A 45 20.982 29.530 27.167 1.00 44.96 C ATOM 342 CG HIS A 45 20.333 30.545 26.302 1.00 49.42 C ATOM 343 ND1 HIS A 45 18.987 30.566 26.035 1.00 51.99 N ATOM 344 CD2 HIS A 45 20.897 31.560 25.582 1.00 50.46 C ATOM 345 CE1 HIS A 45 18.749 31.595 25.208 1.00 54.16 C ATOM 346 NE2 HIS A 45 19.892 32.213 24.930 1.00 51.30 N ATOM 347 N THR A 46 20.541 26.454 27.874 1.00 35.36 N ATOM 348 CA THR A 46 20.720 25.416 28.898 1.00 38.08 C ATOM 349 C THR A 46 21.783 24.444 28.348 1.00 39.94 C ATOM 350 O THR A 46 22.884 24.301 28.906 1.00 36.89 O ATOM 351 CB THR A 46 19.440 24.759 29.462 1.00 39.07 C ATOM 352 OG1 THR A 46 18.356 25.762 29.673 1.00 36.65 O ATOM 353 CG2 THR A 46 19.626 24.023 30.824 1.00 36.14 C ATOM 354 N TRP A 47 21.516 24.004 27.096 1.00 41.90 N ATOM 355 CA TRP A 47 22.360 23.091 26.371 1.00 41.17 C ATOM 356 C TRP A 47 23.812 23.543 26.386 1.00 41.87 C ATOM 357 O TRP A 47 24.752 22.731 26.581 1.00 43.78 O ATOM 358 CB TRP A 47 21.897 22.807 24.909 1.00 41.93 C ATOM 359 CG TRP A 47 23.078 22.427 24.069 1.00 37.97 C ATOM 360 CD1 TRP A 47 23.855 23.306 23.373 1.00 37.71 C ATOM 361 CD2 TRP A 47 23.722 21.150 24.002 1.00 38.70 C ATOM 362 NE1 TRP A 47 24.925 22.634 22.819 1.00 39.15 N ATOM 363 CE2 TRP A 47 24.827 21.306 23.117 1.00 39.23 C ATOM 364 CE3 TRP A 47 23.424 19.886 24.462 1.00 37.88 C ATOM 365 CZ2 TRP A 47 25.699 20.257 22.837 1.00 38.16 C ATOM 366 CZ3 TRP A 47 24.272 18.818 24.128 1.00 34.35 C ATOM 367 CH2 TRP A 47 25.358 19.007 23.331 1.00 33.98 C ATOM 368 N GLU A 48 23.989 24.809 26.158 1.00 41.73 N ATOM 369 CA GLU A 48 25.348 25.370 26.116 1.00 44.52 C ATOM 370 C GLU A 48 25.965 25.199 27.485 1.00 49.22 C ATOM 371 O GLU A 48 27.176 24.922 27.543 1.00 52.11 O ATOM 372 CB GLU A 48 25.415 26.815 25.700 1.00 44.69 C ATOM 373 N SER A 49 25.133 25.356 28.558 1.00 48.02 N ATOM 374 CA SER A 49 25.725 25.220 29.914 1.00 46.05 C ATOM 375 C SER A 49 26.134 23.773 30.186 1.00 45.49 C ATOM 376 O SER A 49 27.224 23.540 30.748 1.00 45.21 O ATOM 377 CB SER A 49 24.962 25.834 31.040 1.00 46.26 C ATOM 378 OG SER A 49 23.595 25.516 31.141 1.00 47.37 O ATOM 379 N ILE A 50 25.253 22.836 29.803 1.00 42.10 N ATOM 380 CA ILE A 50 25.578 21.416 30.059 1.00 36.85 C ATOM 381 C ILE A 50 26.867 21.111 29.376 1.00 40.99 C ATOM 382 O ILE A 50 27.858 20.766 30.045 1.00 41.65 O ATOM 383 CB ILE A 50 24.375 20.473 29.793 1.00 32.78 C ATOM 384 CG1 ILE A 50 23.163 20.930 30.570 1.00 26.10 C ATOM 385 CG2 ILE A 50 24.799 18.991 30.066 1.00 34.64 C ATOM 386 CD1 ILE A 50 21.772 20.445 30.052 1.00 26.10 C ATOM 387 N GLY A 51 26.910 21.302 28.026 1.00 46.44 N ATOM 388 CA GLY A 51 28.167 21.194 27.249 1.00 40.99 C ATOM 389 C GLY A 51 28.454 19.862 26.660 1.00 44.11 C ATOM 390 O GLY A 51 29.580 19.634 26.103 1.00 48.20 O ATOM 391 N ARG A 52 27.547 18.925 26.753 1.00 43.01 N ATOM 392 CA ARG A 52 27.809 17.562 26.170 1.00 43.13 C ATOM 393 C ARG A 52 26.547 16.775 26.446 1.00 41.38 C ATOM 394 O ARG A 52 25.841 17.039 27.426 1.00 44.40 O ATOM 395 CB ARG A 52 29.040 16.987 26.843 1.00 47.77 C ATOM 396 CG ARG A 52 28.856 16.631 28.345 1.00 48.32 C ATOM 397 N PRO A 53 26.244 15.851 25.561 1.00 38.35 N ATOM 398 CA PRO A 53 24.978 15.091 25.703 1.00 35.41 C ATOM 399 C PRO A 53 24.923 14.498 27.078 1.00 35.03 C ATOM 400 O PRO A 53 25.955 14.288 27.711 1.00 36.15 O ATOM 401 CB PRO A 53 25.009 14.119 24.551 1.00 33.15 C ATOM 402 CG PRO A 53 26.421 14.092 24.067 1.00 31.74 C ATOM 403 CD PRO A 53 26.998 15.448 24.388 1.00 34.42 C ATOM 404 N LEU A 54 23.730 14.090 27.482 1.00 38.42 N ATOM 405 CA LEU A 54 23.493 13.382 28.736 1.00 36.29 C ATOM 406 C LEU A 54 23.305 11.909 28.411 1.00 35.68 C ATOM 407 O LEU A 54 22.278 11.546 27.807 1.00 43.50 O ATOM 408 CB LEU A 54 22.201 13.959 29.387 1.00 34.48 C ATOM 409 CG LEU A 54 22.339 15.369 29.964 1.00 36.05 C ATOM 410 CD1 LEU A 54 20.993 15.881 30.431 1.00 36.33 C ATOM 411 CD2 LEU A 54 23.393 15.413 31.052 1.00 32.14 C ATOM 412 N PRO A 55 24.203 11.098 28.854 1.00 37.57 N ATOM 413 CA PRO A 55 24.148 9.636 28.657 1.00 36.02 C ATOM 414 C PRO A 55 22.809 9.116 29.101 1.00 37.19 C ATOM 415 O PRO A 55 22.177 9.714 30.024 1.00 39.49 O ATOM 416 CB PRO A 55 25.288 9.124 29.485 1.00 39.57 C ATOM 417 CG PRO A 55 26.274 10.255 29.646 1.00 38.06 C ATOM 418 CD PRO A 55 25.462 11.533 29.549 1.00 40.36 C ATOM 419 N GLY A 56 22.311 8.062 28.504 1.00 35.08 N ATOM 420 CA GLY A 56 21.061 7.412 28.803 1.00 34.28 C ATOM 421 C GLY A 56 19.792 8.143 28.597 1.00 37.31 C ATOM 422 O GLY A 56 18.678 7.741 29.074 1.00 38.39 O ATOM 423 N ARG A 57 19.846 9.247 27.839 1.00 38.44 N ATOM 424 CA ARG A 57 18.590 9.990 27.546 1.00 38.65 C ATOM 425 C ARG A 57 18.738 10.611 26.153 1.00 37.51 C ATOM 426 O ARG A 57 19.864 10.993 25.777 1.00 41.16 O ATOM 427 CB ARG A 57 18.358 11.094 28.569 1.00 39.05 C ATOM 428 CG ARG A 57 18.249 10.688 30.048 1.00 37.57 C ATOM 429 CD ARG A 57 18.871 11.860 30.819 1.00 36.26 C ATOM 430 NE ARG A 57 20.225 11.445 31.184 1.00 34.07 N ATOM 431 CZ ARG A 57 20.877 11.847 32.224 1.00 36.10 C ATOM 432 NH1 ARG A 57 20.255 12.566 33.217 1.00 38.12 N ATOM 433 NH2 ARG A 57 22.194 11.641 32.266 1.00 34.49 N ATOM 434 N LYS A 58 17.642 10.795 25.543 1.00 37.88 N ATOM 435 CA LYS A 58 17.516 11.409 24.192 1.00 40.35 C ATOM 436 C LYS A 58 17.432 12.926 24.452 1.00 39.43 C ATOM 437 O LYS A 58 16.373 13.355 24.915 1.00 40.79 O ATOM 438 CB LYS A 58 16.181 10.995 23.522 1.00 40.09 C ATOM 439 CG LYS A 58 16.096 11.516 22.067 1.00 43.64 C ATOM 440 CD LYS A 58 15.001 10.822 21.292 1.00 47.39 C ATOM 441 CE LYS A 58 14.699 11.322 19.903 1.00 49.99 C ATOM 442 NZ LYS A 58 15.403 12.580 19.510 1.00 52.89 N ATOM 443 N ASN A 59 18.461 13.629 24.174 1.00 37.31 N ATOM 444 CA ASN A 59 18.694 14.994 24.315 1.00 40.71 C ATOM 445 C ASN A 59 18.248 15.767 23.027 1.00 43.85 C ATOM 446 O ASN A 59 18.944 15.711 22.001 1.00 47.21 O ATOM 447 CB ASN A 59 20.093 15.368 24.699 1.00 41.91 C ATOM 448 CG ASN A 59 21.011 14.761 25.675 1.00 41.34 C ATOM 449 OD1 ASN A 59 21.985 15.483 26.062 1.00 40.15 O ATOM 450 ND2 ASN A 59 20.933 13.499 26.069 1.00 38.65 N ATOM 451 N ILE A 60 17.238 16.561 23.227 1.00 40.72 N ATOM 452 CA ILE A 60 16.621 17.431 22.267 1.00 40.97 C ATOM 453 C ILE A 60 16.808 18.905 22.618 1.00 42.58 C ATOM 454 O ILE A 60 16.503 19.263 23.779 1.00 45.89 O ATOM 455 CB ILE A 60 15.074 17.094 22.253 1.00 39.38 C ATOM 456 CG1 ILE A 60 14.935 15.551 22.278 1.00 36.55 C ATOM 457 CG2 ILE A 60 14.333 17.796 21.129 1.00 38.71 C ATOM 458 CD1 ILE A 60 13.555 15.115 21.690 1.00 40.50 C ATOM 459 N ILE A 61 17.333 19.684 21.710 1.00 41.65 N ATOM 460 CA ILE A 61 17.608 21.089 21.845 1.00 40.41 C ATOM 461 C ILE A 61 16.597 21.956 21.067 1.00 45.56 C ATOM 462 O ILE A 61 15.890 21.484 20.156 1.00 49.63 O ATOM 463 CB ILE A 61 19.065 21.446 21.532 1.00 36.93 C ATOM 464 CG1 ILE A 61 20.055 20.305 21.836 1.00 39.08 C ATOM 465 CG2 ILE A 61 19.504 22.785 22.175 1.00 36.53 C ATOM 466 CD1 ILE A 61 19.741 19.441 23.108 1.00 41.73 C ATOM 467 N LEU A 62 16.412 23.177 21.526 1.00 46.49 N ATOM 468 CA LEU A 62 15.505 24.179 20.999 1.00 45.75 C ATOM 469 C LEU A 62 16.454 25.324 20.568 1.00 48.91 C ATOM 470 O LEU A 62 17.308 25.823 21.289 1.00 49.62 O ATOM 471 CB LEU A 62 14.401 24.595 21.865 1.00 47.35 C ATOM 472 CG LEU A 62 12.935 24.272 21.808 1.00 46.58 C ATOM 473 CD1 LEU A 62 12.217 25.007 20.686 1.00 49.61 C ATOM 474 CD2 LEU A 62 12.674 22.795 21.665 1.00 44.60 C ATOM 475 N SER A 63 16.358 25.501 19.260 1.00 50.82 N ATOM 476 CA SER A 63 17.119 26.519 18.550 1.00 51.45 C ATOM 477 C SER A 63 16.163 26.868 17.376 1.00 54.10 C ATOM 478 O SER A 63 15.416 25.951 16.973 1.00 54.80 O ATOM 479 CB SER A 63 18.466 26.091 18.076 1.00 50.99 C ATOM 480 OG SER A 63 19.326 27.249 17.914 1.00 50.40 O ATOM 481 N SER A 64 16.185 28.131 17.081 1.00 54.55 N ATOM 482 CA SER A 64 15.329 28.605 15.928 1.00 57.44 C ATOM 483 C SER A 64 16.253 28.265 14.717 1.00 59.03 C ATOM 484 O SER A 64 15.829 27.843 13.652 1.00 60.43 O ATOM 485 CB SER A 64 15.063 30.079 16.094 1.00 55.25 C ATOM 486 OG SER A 64 16.290 30.749 16.493 1.00 55.82 O ATOM 487 N GLN A 65 17.523 28.331 15.031 1.00 58.21 N ATOM 488 CA GLN A 65 18.694 28.095 14.273 1.00 59.11 C ATOM 489 C GLN A 65 19.155 26.648 14.155 1.00 60.93 C ATOM 490 O GLN A 65 18.661 25.748 14.850 1.00 61.10 O ATOM 491 CB GLN A 65 19.888 28.915 14.869 1.00 61.92 C ATOM 492 CG GLN A 65 19.587 30.402 14.550 1.00 66.14 C ATOM 493 CD GLN A 65 20.798 31.239 14.852 1.00 68.54 C ATOM 494 OE1 GLN A 65 21.358 31.175 15.943 1.00 71.14 O ATOM 495 NE2 GLN A 65 21.197 32.012 13.850 1.00 70.81 N ATOM 496 N PRO A 66 20.132 26.458 13.260 1.00 60.73 N ATOM 497 CA PRO A 66 20.688 25.154 12.933 1.00 60.79 C ATOM 498 C PRO A 66 21.592 24.558 14.016 1.00 60.27 C ATOM 499 O PRO A 66 22.447 25.228 14.614 1.00 59.54 O ATOM 500 CB PRO A 66 21.500 25.431 11.643 1.00 59.72 C ATOM 501 CG PRO A 66 21.969 26.862 11.857 1.00 58.32 C ATOM 502 CD PRO A 66 20.705 27.533 12.387 1.00 59.85 C ATOM 503 N GLY A 67 21.427 23.247 14.196 1.00 59.42 N ATOM 504 CA GLY A 67 22.158 22.505 15.243 1.00 59.68 C ATOM 505 C GLY A 67 23.630 22.428 14.949 1.00 59.13 C ATOM 506 O GLY A 67 24.048 22.368 13.767 1.00 63.83 O ATOM 507 N THR A 68 24.438 22.396 15.994 1.00 55.85 N ATOM 508 CA THR A 68 25.895 22.338 15.848 1.00 53.40 C ATOM 509 C THR A 68 26.534 21.186 16.617 1.00 47.80 C ATOM 510 O THR A 68 27.593 21.379 17.208 1.00 41.84 O ATOM 511 CB THR A 68 26.587 23.700 16.233 1.00 55.69 C ATOM 512 OG1 THR A 68 26.149 24.037 17.604 1.00 54.36 O ATOM 513 CG2 THR A 68 26.298 24.828 15.227 1.00 57.25 C ATOM 514 N ASP A 69 25.864 20.056 16.600 1.00 47.96 N ATOM 515 CA ASP A 69 26.386 18.826 17.296 1.00 45.72 C ATOM 516 C ASP A 69 25.506 17.702 16.767 1.00 45.21 C ATOM 517 O ASP A 69 24.285 17.815 16.991 1.00 46.17 O ATOM 518 CB ASP A 69 26.330 18.950 18.807 1.00 42.52 C ATOM 519 CG ASP A 69 26.976 17.782 19.535 1.00 42.09 C ATOM 520 OD1 ASP A 69 26.522 16.612 19.398 1.00 43.86 O ATOM 521 OD2 ASP A 69 27.944 18.019 20.290 1.00 37.46 O ATOM 522 N ASP A 70 26.133 16.709 16.157 1.00 46.53 N ATOM 523 CA ASP A 70 25.247 15.617 15.591 1.00 47.67 C ATOM 524 C ASP A 70 24.776 14.668 16.656 1.00 46.47 C ATOM 525 O ASP A 70 23.891 13.804 16.456 1.00 48.18 O ATOM 526 CB ASP A 70 26.051 14.982 14.438 1.00 50.55 C ATOM 527 CG ASP A 70 26.220 15.958 13.263 1.00 53.20 C ATOM 528 OD1 ASP A 70 25.195 16.514 12.786 1.00 55.60 O ATOM 529 OD2 ASP A 70 27.335 16.138 12.766 1.00 50.00 O ATOM 530 N ARG A 71 25.387 14.755 17.836 1.00 46.10 N ATOM 531 CA ARG A 71 25.104 13.794 18.915 1.00 42.71 C ATOM 532 C ARG A 71 23.697 13.973 19.400 1.00 40.40 C ATOM 533 O ARG A 71 23.007 12.996 19.735 1.00 39.68 O ATOM 534 CB ARG A 71 26.205 13.796 19.963 1.00 40.93 C ATOM 535 CG ARG A 71 27.531 13.228 19.438 1.00 36.47 C ATOM 536 CD ARG A 71 28.696 13.587 20.264 1.00 34.64 C ATOM 537 NE ARG A 71 28.743 14.988 20.677 1.00 34.37 N ATOM 538 CZ ARG A 71 29.681 15.454 21.506 1.00 37.83 C ATOM 539 NH1 ARG A 71 30.614 14.669 22.035 1.00 39.84 N ATOM 540 NH2 ARG A 71 29.753 16.755 21.867 1.00 38.22 N ATOM 541 N VAL A 72 23.199 15.182 19.300 1.00 41.76 N ATOM 542 CA VAL A 72 21.819 15.461 19.755 1.00 43.75 C ATOM 543 C VAL A 72 20.908 15.886 18.614 1.00 44.63 C ATOM 544 O VAL A 72 21.380 16.481 17.652 1.00 46.38 O ATOM 545 CB VAL A 72 21.819 16.539 20.891 1.00 43.31 C ATOM 546 CG1 VAL A 72 22.557 16.037 22.122 1.00 42.14 C ATOM 547 CG2 VAL A 72 22.340 17.888 20.435 1.00 38.14 C ATOM 548 N THR A 73 19.635 15.678 18.847 1.00 42.98 N ATOM 549 CA THR A 73 18.466 16.036 18.131 1.00 42.41 C ATOM 550 C THR A 73 18.032 17.493 18.273 1.00 46.95 C ATOM 551 O THR A 73 17.637 17.924 19.397 1.00 49.12 O ATOM 552 CB THR A 73 17.312 15.107 18.675 1.00 43.19 C ATOM 553 OG1 THR A 73 17.904 13.751 18.478 1.00 45.00 O ATOM 554 CG2 THR A 73 15.950 15.307 18.100 1.00 43.58 C ATOM 555 N TRP A 74 18.050 18.245 17.178 1.00 45.20 N ATOM 556 CA TRP A 74 17.691 19.683 17.178 1.00 43.50 C ATOM 557 C TRP A 74 16.259 19.951 16.817 1.00 44.58 C ATOM 558 O TRP A 74 15.627 19.122 16.129 1.00 47.25 O ATOM 559 CB TRP A 74 18.726 20.464 16.453 1.00 39.05 C ATOM 560 CG TRP A 74 20.121 20.355 16.999 1.00 38.23 C ATOM 561 CD1 TRP A 74 21.049 19.392 16.746 1.00 37.18 C ATOM 562 CD2 TRP A 74 20.777 21.302 17.862 1.00 37.88 C ATOM 563 NE1 TRP A 74 22.204 19.618 17.447 1.00 34.07 N ATOM 564 CE2 TRP A 74 22.070 20.788 18.138 1.00 34.63 C ATOM 565 CE3 TRP A 74 20.366 22.540 18.414 1.00 35.89 C ATOM 566 CZ2 TRP A 74 23.006 21.496 18.872 1.00 34.91 C ATOM 567 CZ3 TRP A 74 21.290 23.193 19.177 1.00 37.09 C ATOM 568 CH2 TRP A 74 22.603 22.709 19.394 1.00 35.00 C ATOM 569 N VAL A 75 15.663 21.038 17.323 1.00 44.19 N ATOM 570 CA VAL A 75 14.265 21.382 17.054 1.00 42.80 C ATOM 571 C VAL A 75 14.051 22.867 17.100 1.00 48.25 C ATOM 572 O VAL A 75 14.790 23.668 17.680 1.00 51.43 O ATOM 573 CB VAL A 75 13.252 20.408 17.549 1.00 41.63 C ATOM 574 CG1 VAL A 75 13.660 18.915 17.388 1.00 37.98 C ATOM 575 CG2 VAL A 75 12.759 20.560 19.004 1.00 41.96 C ATOM 576 N LYS A 76 13.073 23.306 16.290 1.00 54.72 N ATOM 577 CA LYS A 76 12.717 24.701 16.051 1.00 53.95 C ATOM 578 C LYS A 76 11.335 25.049 16.573 1.00 54.13 C ATOM 579 O LYS A 76 10.975 26.233 16.399 1.00 57.52 O ATOM 580 CB LYS A 76 12.575 24.978 14.528 1.00 56.66 C ATOM 581 CG LYS A 76 13.758 24.486 13.694 1.00 56.13 C ATOM 582 CD LYS A 76 14.071 25.504 12.596 1.00 54.67 C ATOM 583 CE LYS A 76 15.537 25.472 12.215 1.00 55.84 C ATOM 584 NZ LYS A 76 15.780 26.125 10.907 1.00 53.72 N ATOM 585 N SER A 77 10.648 24.083 17.132 1.00 52.40 N ATOM 586 CA SER A 77 9.329 24.312 17.715 1.00 51.17 C ATOM 587 C SER A 77 9.011 23.268 18.807 1.00 50.73 C ATOM 588 O SER A 77 9.442 22.105 18.804 1.00 51.95 O ATOM 589 CB SER A 77 8.233 24.352 16.682 1.00 51.02 C ATOM 590 OG SER A 77 7.733 23.009 16.452 1.00 53.71 O ATOM 591 N VAL A 78 8.197 23.729 19.715 1.00 49.05 N ATOM 592 CA VAL A 78 7.713 22.982 20.869 1.00 50.37 C ATOM 593 C VAL A 78 7.103 21.701 20.346 1.00 54.42 C ATOM 594 O VAL A 78 7.403 20.580 20.813 1.00 57.51 O ATOM 595 CB VAL A 78 6.778 23.948 21.652 1.00 50.82 C ATOM 596 CG1 VAL A 78 5.951 23.300 22.736 1.00 49.85 C ATOM 597 CG2 VAL A 78 7.574 25.162 22.147 1.00 46.24 C ATOM 598 N ASP A 79 6.293 21.871 19.308 1.00 56.50 N ATOM 599 CA ASP A 79 5.547 20.744 18.688 1.00 55.69 C ATOM 600 C ASP A 79 6.503 19.739 18.097 1.00 52.72 C ATOM 601 O ASP A 79 6.285 18.510 18.108 1.00 50.84 O ATOM 602 CB ASP A 79 4.531 21.319 17.692 1.00 59.44 C ATOM 603 CG ASP A 79 3.369 21.960 18.456 1.00 60.74 C ATOM 604 OD1 ASP A 79 2.992 21.453 19.511 1.00 60.12 O ATOM 605 OD2 ASP A 79 2.867 22.972 17.907 1.00 63.86 O ATOM 606 N GLU A 80 7.551 20.347 17.569 1.00 52.61 N ATOM 607 CA GLU A 80 8.629 19.510 16.932 1.00 51.98 C ATOM 608 C GLU A 80 9.098 18.597 18.093 1.00 49.12 C ATOM 609 O GLU A 80 8.884 17.385 18.127 1.00 43.22 O ATOM 610 CB GLU A 80 9.751 20.375 16.436 1.00 52.86 C ATOM 611 CG GLU A 80 9.851 20.693 14.945 1.00 54.74 C ATOM 612 CD GLU A 80 11.240 20.757 14.372 1.00 55.95 C ATOM 613 OE1 GLU A 80 11.911 19.734 14.117 1.00 52.80 O ATOM 614 OE2 GLU A 80 11.678 21.952 14.210 1.00 58.19 O ATOM 615 N ALA A 81 9.607 19.343 19.051 1.00 49.50 N ATOM 616 CA ALA A 81 10.149 18.909 20.336 1.00 47.39 C ATOM 617 C ALA A 81 9.396 17.742 20.910 1.00 44.26 C ATOM 618 O ALA A 81 9.909 16.648 21.152 1.00 45.07 O ATOM 619 CB ALA A 81 9.994 20.117 21.316 1.00 48.16 C ATOM 620 N ILE A 82 8.127 18.007 21.115 1.00 46.15 N ATOM 621 CA ILE A 82 7.190 17.019 21.673 1.00 48.15 C ATOM 622 C ILE A 82 7.075 15.826 20.731 1.00 52.23 C ATOM 623 O ILE A 82 6.654 14.728 21.094 1.00 53.83 O ATOM 624 CB ILE A 82 5.767 17.708 21.725 1.00 49.38 C ATOM 625 CG1 ILE A 82 5.880 19.121 22.277 1.00 48.42 C ATOM 626 CG2 ILE A 82 4.758 16.739 22.415 1.00 49.41 C ATOM 627 CD1 ILE A 82 4.888 19.480 23.442 1.00 47.91 C ATOM 628 N ALA A 83 7.299 16.174 19.458 1.00 54.64 N ATOM 629 CA ALA A 83 7.231 15.212 18.354 1.00 54.18 C ATOM 630 C ALA A 83 8.484 14.347 18.388 1.00 52.99 C ATOM 631 O ALA A 83 8.373 13.102 18.415 1.00 53.87 O ATOM 632 CB ALA A 83 7.065 15.956 17.038 1.00 57.01 C ATOM 633 N ALA A 84 9.626 15.009 18.443 1.00 50.31 N ATOM 634 CA ALA A 84 10.908 14.298 18.500 1.00 49.59 C ATOM 635 C ALA A 84 11.034 13.261 19.591 1.00 52.13 C ATOM 636 O ALA A 84 12.129 12.606 19.592 1.00 53.50 O ATOM 637 CB ALA A 84 12.039 15.309 18.583 1.00 47.98 C ATOM 638 N CYS A 85 10.123 13.114 20.534 1.00 51.70 N ATOM 639 CA CYS A 85 10.262 12.123 21.610 1.00 54.31 C ATOM 640 C CYS A 85 9.598 10.814 21.125 1.00 57.49 C ATOM 641 O CYS A 85 10.203 9.743 21.231 1.00 61.31 O ATOM 642 CB CYS A 85 9.678 12.449 22.970 1.00 52.78 C ATOM 643 SG CYS A 85 10.055 14.039 23.710 1.00 53.62 S ATOM 644 N GLY A 86 8.391 10.990 20.649 1.00 57.65 N ATOM 645 CA GLY A 86 7.599 9.890 20.125 1.00 59.39 C ATOM 646 C GLY A 86 6.631 9.445 21.206 1.00 61.57 C ATOM 647 O GLY A 86 6.178 10.270 22.017 1.00 65.52 O ATOM 648 N ASP A 87 6.377 8.160 21.216 1.00 63.35 N ATOM 649 CA ASP A 87 5.467 7.567 22.202 1.00 64.70 C ATOM 650 C ASP A 87 6.086 6.998 23.445 1.00 63.77 C ATOM 651 O ASP A 87 6.365 5.791 23.603 1.00 63.51 O ATOM 652 CB ASP A 87 4.504 6.629 21.419 1.00 65.65 C ATOM 653 CG ASP A 87 3.109 7.255 21.657 1.00 66.61 C ATOM 654 OD1 ASP A 87 2.919 8.424 21.285 1.00 65.37 O ATOM 655 OD2 ASP A 87 2.383 6.532 22.365 1.00 69.45 O ATOM 656 N VAL A 88 6.282 7.908 24.411 1.00 63.87 N ATOM 657 CA VAL A 88 6.849 7.556 25.724 1.00 59.89 C ATOM 658 C VAL A 88 5.917 8.083 26.816 1.00 57.61 C ATOM 659 O VAL A 88 5.169 9.023 26.588 1.00 56.81 O ATOM 660 CB VAL A 88 8.278 8.033 25.920 1.00 60.81 C ATOM 661 CG1 VAL A 88 9.293 7.346 24.996 1.00 59.85 C ATOM 662 CG2 VAL A 88 8.371 9.551 25.825 1.00 62.54 C ATOM 663 N PRO A 89 6.052 7.413 27.960 1.00 56.23 N ATOM 664 CA PRO A 89 5.265 7.692 29.142 1.00 53.15 C ATOM 665 C PRO A 89 5.527 9.065 29.698 1.00 52.12 C ATOM 666 O PRO A 89 4.552 9.824 29.960 1.00 55.01 O ATOM 667 CB PRO A 89 5.634 6.584 30.140 1.00 54.49 C ATOM 668 CG PRO A 89 6.145 5.478 29.224 1.00 54.28 C ATOM 669 CD PRO A 89 6.969 6.260 28.190 1.00 53.59 C ATOM 670 N GLU A 90 6.814 9.389 29.857 1.00 48.10 N ATOM 671 CA GLU A 90 7.140 10.709 30.433 1.00 43.67 C ATOM 672 C GLU A 90 8.362 11.341 29.804 1.00 41.42 C ATOM 673 O GLU A 90 9.448 10.754 29.848 1.00 40.67 O ATOM 674 CB GLU A 90 7.375 10.594 31.945 1.00 43.42 C ATOM 675 CG GLU A 90 7.856 11.824 32.700 1.00 43.43 C ATOM 676 CD GLU A 90 8.078 11.558 34.197 1.00 45.88 C ATOM 677 OE1 GLU A 90 8.386 10.424 34.629 1.00 37.87 O ATOM 678 OE2 GLU A 90 7.823 12.637 34.829 1.00 43.92 O ATOM 679 N ILE A 91 8.148 12.546 29.341 1.00 38.22 N ATOM 680 CA ILE A 91 9.098 13.435 28.756 1.00 41.93 C ATOM 681 C ILE A 91 9.490 14.519 29.808 1.00 42.25 C ATOM 682 O ILE A 91 8.572 15.154 30.354 1.00 41.56 O ATOM 683 CB ILE A 91 8.441 14.205 27.514 1.00 41.87 C ATOM 684 CG1 ILE A 91 8.036 13.130 26.475 1.00 44.41 C ATOM 685 CG2 ILE A 91 9.311 15.321 26.960 1.00 39.48 C ATOM 686 CD1 ILE A 91 6.465 13.008 26.336 1.00 46.66 C ATOM 687 N MET A 92 10.788 14.728 29.922 1.00 38.31 N ATOM 688 CA MET A 92 11.353 15.649 30.860 1.00 39.53 C ATOM 689 C MET A 92 11.835 16.951 30.244 1.00 40.08 C ATOM 690 O MET A 92 12.798 16.968 29.485 1.00 41.83 O ATOM 691 CB MET A 92 12.548 15.052 31.681 1.00 39.34 C ATOM 692 CG MET A 92 12.230 13.707 32.226 1.00 38.36 C ATOM 693 SD MET A 92 11.037 13.763 33.575 1.00 41.68 S ATOM 694 CE MET A 92 11.823 15.040 34.606 1.00 35.18 C ATOM 695 N VAL A 93 11.208 18.027 30.721 1.00 39.39 N ATOM 696 CA VAL A 93 11.606 19.380 30.243 1.00 37.98 C ATOM 697 C VAL A 93 12.550 19.952 31.331 1.00 39.29 C ATOM 698 O VAL A 93 12.177 20.031 32.494 1.00 37.55 O ATOM 699 CB VAL A 93 10.312 20.171 30.005 1.00 35.78 C ATOM 700 CG1 VAL A 93 10.529 21.559 29.546 1.00 32.29 C ATOM 701 CG2 VAL A 93 9.303 19.389 29.160 1.00 32.86 C ATOM 702 N ILE A 94 13.768 20.226 30.921 1.00 37.10 N ATOM 703 CA ILE A 94 14.879 20.658 31.689 1.00 31.00 C ATOM 704 C ILE A 94 15.294 22.091 31.566 1.00 32.36 C ATOM 705 O ILE A 94 16.445 22.415 31.883 1.00 31.17 O ATOM 706 CB ILE A 94 16.056 19.623 31.593 1.00 33.64 C ATOM 707 CG1 ILE A 94 16.771 19.654 30.197 1.00 31.85 C ATOM 708 CG2 ILE A 94 15.724 18.133 31.904 1.00 28.55 C ATOM 709 CD1 ILE A 94 18.250 19.112 30.388 1.00 26.62 C ATOM 710 N GLY A 95 14.366 23.030 31.294 1.00 32.77 N ATOM 711 CA GLY A 95 14.645 24.472 31.225 1.00 29.05 C ATOM 712 C GLY A 95 15.420 24.880 29.967 1.00 33.19 C ATOM 713 O GLY A 95 15.620 24.048 29.029 1.00 32.91 O ATOM 714 N GLY A 96 16.014 26.072 29.939 1.00 29.75 N ATOM 715 CA GLY A 96 15.926 27.047 31.018 1.00 31.07 C ATOM 716 C GLY A 96 14.631 27.797 31.203 1.00 31.60 C ATOM 717 O GLY A 96 13.488 27.367 31.133 1.00 31.54 O ATOM 718 N GLY A 97 14.844 29.130 31.361 1.00 34.08 N ATOM 719 CA GLY A 97 13.739 30.042 31.666 1.00 36.29 C ATOM 720 C GLY A 97 12.603 29.881 30.667 1.00 36.82 C ATOM 721 O GLY A 97 11.576 29.227 30.915 1.00 37.78 O ATOM 722 N ARG A 98 12.904 30.508 29.519 1.00 37.89 N ATOM 723 CA ARG A 98 11.958 30.481 28.366 1.00 36.50 C ATOM 724 C ARG A 98 11.339 29.160 28.118 1.00 33.09 C ATOM 725 O ARG A 98 10.069 29.086 28.011 1.00 36.24 O ATOM 726 CB ARG A 98 12.737 31.057 27.180 1.00 40.38 C ATOM 727 N VAL A 99 12.082 28.077 28.104 1.00 33.57 N ATOM 728 CA VAL A 99 11.457 26.731 27.796 1.00 34.30 C ATOM 729 C VAL A 99 10.458 26.383 28.825 1.00 38.40 C ATOM 730 O VAL A 99 9.343 25.874 28.540 1.00 44.27 O ATOM 731 CB VAL A 99 12.575 25.659 27.626 1.00 36.49 C ATOM 732 CG1 VAL A 99 12.056 24.212 27.541 1.00 30.42 C ATOM 733 CG2 VAL A 99 13.569 26.086 26.601 1.00 30.52 C ATOM 734 N TYR A 100 10.919 26.598 30.076 1.00 40.70 N ATOM 735 CA TYR A 100 10.002 26.314 31.244 1.00 40.31 C ATOM 736 C TYR A 100 8.724 27.109 31.043 1.00 38.62 C ATOM 737 O TYR A 100 7.602 26.598 31.066 1.00 40.10 O ATOM 738 CB TYR A 100 10.773 26.771 32.522 1.00 38.97 C ATOM 739 CG TYR A 100 11.797 25.822 33.092 1.00 36.60 C ATOM 740 CD1 TYR A 100 11.593 24.439 33.091 1.00 36.46 C ATOM 741 CD2 TYR A 100 12.902 26.314 33.824 1.00 34.62 C ATOM 742 CE1 TYR A 100 12.535 23.585 33.681 1.00 32.36 C ATOM 743 CE2 TYR A 100 13.837 25.476 34.400 1.00 29.14 C ATOM 744 CZ TYR A 100 13.623 24.108 34.314 1.00 30.06 C ATOM 745 OH TYR A 100 14.578 23.278 34.836 1.00 31.20 O ATOM 746 N GLU A 101 8.920 28.408 30.881 1.00 41.40 N ATOM 747 CA GLU A 101 7.824 29.391 30.659 1.00 49.38 C ATOM 748 C GLU A 101 6.802 28.872 29.667 1.00 51.36 C ATOM 749 O GLU A 101 5.579 28.936 29.909 1.00 54.46 O ATOM 750 CB GLU A 101 8.389 30.669 30.100 1.00 52.36 C ATOM 751 CG GLU A 101 7.819 32.038 30.318 1.00 57.39 C ATOM 752 CD GLU A 101 8.845 33.148 30.164 1.00 59.97 C ATOM 753 OE1 GLU A 101 9.477 33.363 29.124 1.00 60.08 O ATOM 754 OE2 GLU A 101 8.996 33.792 31.235 1.00 62.54 O ATOM 755 N GLN A 102 7.305 28.242 28.589 1.00 52.91 N ATOM 756 CA GLN A 102 6.392 27.690 27.568 1.00 52.11 C ATOM 757 C GLN A 102 5.840 26.332 27.888 1.00 52.03 C ATOM 758 O GLN A 102 4.678 26.087 27.485 1.00 53.28 O ATOM 759 CB GLN A 102 6.910 27.767 26.159 1.00 52.41 C ATOM 760 CG GLN A 102 7.712 29.027 25.797 1.00 52.47 C ATOM 761 CD GLN A 102 8.517 28.672 24.549 1.00 55.31 C ATOM 762 OE1 GLN A 102 8.319 27.573 24.004 1.00 58.03 O ATOM 763 NE2 GLN A 102 9.371 29.549 24.091 1.00 56.63 N ATOM 764 N PHE A 103 6.552 25.453 28.583 1.00 51.47 N ATOM 765 CA PHE A 103 6.010 24.117 28.907 1.00 47.71 C ATOM 766 C PHE A 103 5.148 23.966 30.107 1.00 48.32 C ATOM 767 O PHE A 103 4.449 22.883 30.267 1.00 50.62 O ATOM 768 CB PHE A 103 7.145 23.091 28.903 1.00 48.28 C ATOM 769 CG PHE A 103 7.616 22.673 27.544 1.00 46.43 C ATOM 770 CD1 PHE A 103 7.100 21.532 26.958 1.00 44.30 C ATOM 771 CD2 PHE A 103 8.563 23.459 26.872 1.00 46.15 C ATOM 772 CE1 PHE A 103 7.571 21.078 25.745 1.00 44.06 C ATOM 773 CE2 PHE A 103 8.992 23.028 25.596 1.00 48.45 C ATOM 774 CZ PHE A 103 8.486 21.844 25.031 1.00 43.14 C ATOM 775 N LEU A 104 5.238 24.878 31.063 1.00 48.18 N ATOM 776 CA LEU A 104 4.417 24.771 32.302 1.00 45.11 C ATOM 777 C LEU A 104 2.999 24.405 31.987 1.00 46.72 C ATOM 778 O LEU A 104 2.436 23.366 32.469 1.00 49.61 O ATOM 779 CB LEU A 104 4.633 26.092 33.016 1.00 46.44 C ATOM 780 CG LEU A 104 3.945 26.370 34.342 1.00 47.04 C ATOM 781 CD1 LEU A 104 4.021 25.194 35.300 1.00 44.94 C ATOM 782 CD2 LEU A 104 4.783 27.538 34.937 1.00 48.39 C ATOM 783 N PRO A 105 2.353 25.232 31.162 1.00 46.06 N ATOM 784 CA PRO A 105 0.938 24.998 30.809 1.00 45.15 C ATOM 785 C PRO A 105 0.678 23.600 30.420 1.00 47.91 C ATOM 786 O PRO A 105 -0.429 23.081 30.813 1.00 52.08 O ATOM 787 CB PRO A 105 0.576 26.099 29.843 1.00 44.28 C ATOM 788 CG PRO A 105 1.593 27.184 30.109 1.00 44.52 C ATOM 789 CD PRO A 105 2.873 26.471 30.542 1.00 43.17 C ATOM 790 N LYS A 106 1.616 22.912 29.762 1.00 48.18 N ATOM 791 CA LYS A 106 1.367 21.521 29.339 1.00 50.61 C ATOM 792 C LYS A 106 1.719 20.464 30.367 1.00 51.66 C ATOM 793 O LYS A 106 1.372 19.244 30.203 1.00 50.11 O ATOM 794 CB LYS A 106 2.091 21.164 28.039 1.00 53.50 C ATOM 795 CG LYS A 106 2.633 22.283 27.164 1.00 53.97 C ATOM 796 N ALA A 107 2.477 20.866 31.381 1.00 51.53 N ATOM 797 CA ALA A 107 2.969 19.966 32.420 1.00 47.95 C ATOM 798 C ALA A 107 1.839 19.474 33.311 1.00 49.63 C ATOM 799 O ALA A 107 0.828 20.139 33.513 1.00 50.75 O ATOM 800 CB ALA A 107 4.033 20.640 33.255 1.00 51.70 C ATOM 801 N GLN A 108 2.082 18.310 33.862 1.00 50.73 N ATOM 802 CA GLN A 108 1.276 17.552 34.768 1.00 52.48 C ATOM 803 C GLN A 108 2.024 17.198 36.060 1.00 52.76 C ATOM 804 O GLN A 108 1.395 16.724 37.045 1.00 54.21 O ATOM 805 CB GLN A 108 0.821 16.228 34.139 1.00 56.53 C ATOM 806 CG GLN A 108 -0.351 16.450 33.163 1.00 60.88 C ATOM 807 CD GLN A 108 -1.063 15.102 33.064 1.00 64.03 C ATOM 808 OE1 GLN A 108 -1.180 14.440 34.097 1.00 64.79 O ATOM 809 NE2 GLN A 108 -1.403 14.743 31.839 1.00 66.96 N ATOM 810 N LYS A 109 3.332 17.406 36.011 1.00 49.65 N ATOM 811 CA LYS A 109 4.115 17.068 37.260 1.00 47.66 C ATOM 812 C LYS A 109 5.343 17.908 37.327 1.00 46.13 C ATOM 813 O LYS A 109 5.823 18.462 36.317 1.00 45.13 O ATOM 814 CB LYS A 109 4.196 15.634 37.456 1.00 45.71 C ATOM 815 CG LYS A 109 5.348 14.889 38.052 1.00 44.05 C ATOM 816 CD LYS A 109 4.938 13.407 38.237 1.00 39.04 C ATOM 817 CE LYS A 109 6.183 12.538 38.414 1.00 43.20 C ATOM 818 NZ LYS A 109 5.771 11.149 38.781 1.00 42.64 N ATOM 819 N LEU A 110 5.684 18.251 38.597 1.00 45.74 N ATOM 820 CA LEU A 110 6.915 19.050 38.821 1.00 43.13 C ATOM 821 C LEU A 110 7.803 18.195 39.737 1.00 39.36 C ATOM 822 O LEU A 110 7.290 17.391 40.499 1.00 39.68 O ATOM 823 CB LEU A 110 6.738 20.445 39.274 1.00 44.58 C ATOM 824 CG LEU A 110 5.649 21.386 38.865 1.00 46.25 C ATOM 825 CD1 LEU A 110 5.575 22.550 39.875 1.00 44.98 C ATOM 826 CD2 LEU A 110 6.008 21.988 37.488 1.00 47.60 C ATOM 827 N TYR A 111 9.075 18.394 39.519 1.00 38.93 N ATOM 828 CA TYR A 111 10.125 17.760 40.370 1.00 34.99 C ATOM 829 C TYR A 111 10.944 18.986 40.790 1.00 36.61 C ATOM 830 O TYR A 111 11.707 19.402 39.896 1.00 35.33 O ATOM 831 CB TYR A 111 11.042 16.837 39.604 1.00 38.44 C ATOM 832 CG TYR A 111 10.410 15.580 39.053 1.00 40.03 C ATOM 833 CD1 TYR A 111 9.611 15.594 37.910 1.00 39.22 C ATOM 834 CD2 TYR A 111 10.635 14.363 39.693 1.00 40.54 C ATOM 835 CE1 TYR A 111 8.995 14.438 37.465 1.00 40.02 C ATOM 836 CE2 TYR A 111 10.126 13.175 39.181 1.00 41.08 C ATOM 837 CZ TYR A 111 9.276 13.229 38.059 1.00 41.46 C ATOM 838 OH TYR A 111 8.737 12.034 37.650 1.00 39.77 O ATOM 839 N LEU A 112 10.695 19.495 42.008 1.00 34.01 N ATOM 840 CA LEU A 112 11.500 20.717 42.378 1.00 29.37 C ATOM 841 C LEU A 112 12.422 20.432 43.568 1.00 28.98 C ATOM 842 O LEU A 112 12.084 19.657 44.450 1.00 28.62 O ATOM 843 CB LEU A 112 10.432 21.761 42.694 1.00 30.64 C ATOM 844 CG LEU A 112 9.355 21.979 41.616 1.00 28.80 C ATOM 845 CD1 LEU A 112 8.017 22.301 42.272 1.00 31.30 C ATOM 846 CD2 LEU A 112 9.754 23.244 40.817 1.00 25.38 C ATOM 847 N THR A 113 13.542 21.083 43.629 1.00 24.22 N ATOM 848 CA THR A 113 14.550 21.294 44.474 1.00 25.52 C ATOM 849 C THR A 113 14.489 22.694 45.136 1.00 30.11 C ATOM 850 O THR A 113 14.703 23.731 44.490 1.00 30.15 O ATOM 851 CB THR A 113 16.019 21.020 43.997 1.00 27.93 C ATOM 852 OG1 THR A 113 15.998 19.650 43.444 1.00 26.05 O ATOM 853 CG2 THR A 113 16.938 20.972 45.269 1.00 27.63 C ATOM 854 N HIS A 114 14.091 22.650 46.442 1.00 29.28 N ATOM 855 CA HIS A 114 14.008 24.063 47.058 1.00 26.33 C ATOM 856 C HIS A 114 15.289 24.263 47.798 1.00 28.78 C ATOM 857 O HIS A 114 15.643 23.507 48.742 1.00 31.18 O ATOM 858 CB HIS A 114 12.736 24.262 47.761 1.00 23.68 C ATOM 859 CG HIS A 114 11.472 23.875 47.086 1.00 20.68 C ATOM 860 ND1 HIS A 114 10.697 24.751 46.356 1.00 16.51 N ATOM 861 CD2 HIS A 114 10.750 22.710 47.211 1.00 18.02 C ATOM 862 CE1 HIS A 114 9.519 24.184 46.119 1.00 14.57 C ATOM 863 NE2 HIS A 114 9.519 22.949 46.611 1.00 18.94 N ATOM 864 N ILE A 115 16.159 25.006 47.127 1.00 33.20 N ATOM 865 CA ILE A 115 17.528 25.230 47.675 1.00 34.49 C ATOM 866 C ILE A 115 17.306 26.294 48.775 1.00 34.43 C ATOM 867 O ILE A 115 16.585 27.297 48.544 1.00 30.90 O ATOM 868 CB ILE A 115 18.454 25.723 46.532 1.00 35.41 C ATOM 869 CG1 ILE A 115 18.754 24.732 45.350 1.00 35.32 C ATOM 870 CG2 ILE A 115 19.868 26.209 47.077 1.00 34.42 C ATOM 871 CD1 ILE A 115 17.999 23.417 45.410 1.00 37.02 C ATOM 872 N ASP A 116 18.036 26.140 49.866 1.00 38.25 N ATOM 873 CA ASP A 116 17.956 27.199 50.943 1.00 39.35 C ATOM 874 C ASP A 116 19.076 28.206 50.718 1.00 39.19 C ATOM 875 O ASP A 116 20.151 28.060 51.334 1.00 40.47 O ATOM 876 CB ASP A 116 18.078 26.523 52.306 1.00 40.83 C ATOM 877 CG ASP A 116 18.115 27.673 53.375 1.00 44.13 C ATOM 878 N ALA A 117 18.898 29.147 49.819 1.00 40.38 N ATOM 879 CA ALA A 117 19.954 30.160 49.580 1.00 41.08 C ATOM 880 C ALA A 117 19.385 31.377 48.867 1.00 44.23 C ATOM 881 O ALA A 117 18.649 31.237 47.875 1.00 47.46 O ATOM 882 CB ALA A 117 21.086 29.573 48.784 1.00 39.62 C ATOM 883 N GLU A 118 19.843 32.527 49.296 1.00 46.31 N ATOM 884 CA GLU A 118 19.470 33.829 48.775 1.00 47.82 C ATOM 885 C GLU A 118 20.594 34.403 47.894 1.00 48.62 C ATOM 886 O GLU A 118 21.384 35.232 48.372 1.00 48.90 O ATOM 887 CB GLU A 118 19.280 34.851 49.870 1.00 50.94 C ATOM 888 CG GLU A 118 17.996 35.168 50.594 1.00 54.88 C ATOM 889 CD GLU A 118 17.858 36.622 50.985 1.00 57.68 C ATOM 890 OE1 GLU A 118 18.615 37.141 51.834 1.00 60.93 O ATOM 891 OE2 GLU A 118 16.978 37.269 50.361 1.00 58.59 O ATOM 892 N VAL A 119 20.608 34.012 46.642 1.00 46.74 N ATOM 893 CA VAL A 119 21.565 34.511 45.645 1.00 43.71 C ATOM 894 C VAL A 119 20.795 35.304 44.593 1.00 41.96 C ATOM 895 O VAL A 119 19.596 34.966 44.386 1.00 47.54 O ATOM 896 CB VAL A 119 22.324 33.306 45.035 1.00 46.17 C ATOM 897 CG1 VAL A 119 22.782 32.304 46.140 1.00 45.01 C ATOM 898 CG2 VAL A 119 21.453 32.615 44.006 1.00 44.67 C ATOM 899 N GLU A 120 21.386 36.278 43.996 1.00 42.94 N ATOM 900 CA GLU A 120 20.763 37.061 42.907 1.00 49.21 C ATOM 901 C GLU A 120 20.984 36.349 41.548 1.00 49.24 C ATOM 902 O GLU A 120 22.017 35.717 41.266 1.00 49.46 O ATOM 903 CB GLU A 120 21.344 38.463 42.745 1.00 49.61 C ATOM 904 CG GLU A 120 21.266 39.043 41.329 1.00 51.30 C ATOM 905 CD GLU A 120 21.965 40.366 41.106 1.00 53.51 C ATOM 906 N GLY A 121 19.945 36.403 40.752 1.00 50.79 N ATOM 907 CA GLY A 121 19.960 35.743 39.430 1.00 50.62 C ATOM 908 C GLY A 121 19.137 36.505 38.426 1.00 51.98 C ATOM 909 O GLY A 121 18.313 37.374 38.772 1.00 51.00 O ATOM 910 N ASP A 122 19.336 36.089 37.159 1.00 52.13 N ATOM 911 CA ASP A 122 18.671 36.752 36.024 1.00 48.17 C ATOM 912 C ASP A 122 17.597 35.930 35.408 1.00 49.46 C ATOM 913 O ASP A 122 16.841 36.497 34.551 1.00 51.95 O ATOM 914 CB ASP A 122 19.737 37.241 35.042 1.00 50.01 C ATOM 915 CG ASP A 122 20.532 36.035 34.500 1.00 51.09 C ATOM 916 OD1 ASP A 122 21.617 36.223 33.973 1.00 47.93 O ATOM 917 OD2 ASP A 122 19.952 34.909 34.630 1.00 51.03 O ATOM 918 N THR A 123 17.472 34.664 35.788 1.00 47.63 N ATOM 919 CA THR A 123 16.411 33.798 35.230 1.00 42.39 C ATOM 920 C THR A 123 15.659 33.219 36.436 1.00 39.64 C ATOM 921 O THR A 123 16.351 32.730 37.306 1.00 42.17 O ATOM 922 CB THR A 123 16.920 32.616 34.315 1.00 43.29 C ATOM 923 OG1 THR A 123 18.163 33.009 33.692 1.00 44.86 O ATOM 924 CG2 THR A 123 15.829 32.118 33.325 1.00 41.97 C ATOM 925 N HIS A 124 14.365 33.262 36.409 1.00 38.28 N ATOM 926 CA HIS A 124 13.434 32.876 37.418 1.00 37.86 C ATOM 927 C HIS A 124 12.496 31.837 36.916 1.00 39.46 C ATOM 928 O HIS A 124 12.408 31.710 35.687 1.00 47.30 O ATOM 929 CB HIS A 124 12.655 34.105 38.028 1.00 37.70 C ATOM 930 CG HIS A 124 13.703 35.103 38.475 1.00 38.58 C ATOM 931 ND1 HIS A 124 14.006 35.381 39.751 1.00 42.67 N ATOM 932 CD2 HIS A 124 14.605 35.766 37.754 1.00 41.49 C ATOM 933 CE1 HIS A 124 15.012 36.222 39.837 1.00 42.41 C ATOM 934 NE2 HIS A 124 15.418 36.494 38.630 1.00 42.69 N ATOM 935 N PHE A 125 11.904 31.035 37.733 1.00 37.28 N ATOM 936 CA PHE A 125 11.024 29.934 37.305 1.00 37.51 C ATOM 937 C PHE A 125 9.602 30.452 37.093 1.00 42.09 C ATOM 938 O PHE A 125 9.090 31.388 37.759 1.00 44.62 O ATOM 939 CB PHE A 125 11.136 28.847 38.365 1.00 30.08 C ATOM 940 CG PHE A 125 10.458 27.579 38.048 1.00 27.32 C ATOM 941 CD1 PHE A 125 11.051 26.694 37.116 1.00 27.61 C ATOM 942 CD2 PHE A 125 9.191 27.335 38.519 1.00 27.96 C ATOM 943 CE1 PHE A 125 10.406 25.531 36.782 1.00 31.38 C ATOM 944 CE2 PHE A 125 8.478 26.187 38.172 1.00 28.88 C ATOM 945 CZ PHE A 125 9.111 25.271 37.313 1.00 32.62 C ATOM 946 N PRO A 126 8.984 29.923 36.065 1.00 44.05 N ATOM 947 CA PRO A 126 7.591 30.342 35.724 1.00 48.18 C ATOM 948 C PRO A 126 6.812 30.413 37.055 1.00 50.21 C ATOM 949 O PRO A 126 6.997 29.558 37.934 1.00 50.36 O ATOM 950 CB PRO A 126 7.076 29.193 34.874 1.00 46.28 C ATOM 951 CG PRO A 126 8.110 28.083 34.981 1.00 44.19 C ATOM 952 CD PRO A 126 9.433 28.886 35.136 1.00 43.40 C ATOM 953 N ASP A 127 5.876 31.354 37.109 1.00 54.02 N ATOM 954 CA ASP A 127 5.017 31.486 38.260 1.00 56.22 C ATOM 955 C ASP A 127 3.976 30.404 38.351 1.00 56.30 C ATOM 956 O ASP A 127 2.809 30.772 38.084 1.00 61.24 O ATOM 957 CB ASP A 127 4.337 32.879 38.401 1.00 59.24 C ATOM 958 CG ASP A 127 4.016 33.009 39.922 1.00 62.15 C ATOM 959 OD1 ASP A 127 3.132 32.276 40.377 1.00 62.54 O ATOM 960 OD2 ASP A 127 4.755 33.782 40.573 1.00 62.41 O ATOM 961 N TYR A 128 4.293 29.202 38.778 1.00 56.56 N ATOM 962 CA TYR A 128 3.147 28.215 38.945 1.00 54.89 C ATOM 963 C TYR A 128 2.143 28.877 39.899 1.00 57.35 C ATOM 964 O TYR A 128 2.366 29.964 40.467 1.00 55.88 O ATOM 965 CB TYR A 128 3.564 26.855 39.351 1.00 50.69 C ATOM 966 CG TYR A 128 4.418 26.597 40.551 1.00 50.40 C ATOM 967 CD1 TYR A 128 5.732 27.048 40.608 1.00 51.26 C ATOM 968 CD2 TYR A 128 3.974 25.827 41.636 1.00 50.68 C ATOM 969 CE1 TYR A 128 6.556 26.816 41.690 1.00 51.25 C ATOM 970 CE2 TYR A 128 4.795 25.569 42.734 1.00 50.23 C ATOM 971 CZ TYR A 128 6.070 26.052 42.767 1.00 51.45 C ATOM 972 OH TYR A 128 6.911 25.825 43.855 1.00 50.60 O ATOM 973 N GLU A 129 1.026 28.172 40.071 1.00 60.14 N ATOM 974 CA GLU A 129 -0.080 28.695 40.933 1.00 58.67 C ATOM 975 C GLU A 129 -0.583 27.580 41.833 1.00 58.28 C ATOM 976 O GLU A 129 -1.292 26.666 41.374 1.00 60.47 O ATOM 977 N PRO A 130 -0.190 27.657 43.081 1.00 58.19 N ATOM 978 CA PRO A 130 -0.449 26.761 44.170 1.00 57.33 C ATOM 979 C PRO A 130 -1.698 25.938 44.127 1.00 58.80 C ATOM 980 O PRO A 130 -1.661 24.699 44.334 1.00 61.24 O ATOM 981 CB PRO A 130 -0.480 27.688 45.406 1.00 57.16 C ATOM 982 CG PRO A 130 -0.068 29.053 44.899 1.00 57.73 C ATOM 983 CD PRO A 130 0.681 28.779 43.608 1.00 58.33 C ATOM 984 N ASP A 131 -2.828 26.609 43.968 1.00 58.86 N ATOM 985 CA ASP A 131 -4.120 25.908 43.965 1.00 60.15 C ATOM 986 C ASP A 131 -4.186 24.866 42.868 1.00 60.31 C ATOM 987 O ASP A 131 -5.047 23.952 42.935 1.00 62.88 O ATOM 988 N ASP A 132 -3.351 24.975 41.863 1.00 60.62 N ATOM 989 CA ASP A 132 -3.430 24.029 40.713 1.00 61.60 C ATOM 990 C ASP A 132 -2.750 22.705 40.963 1.00 59.18 C ATOM 991 O ASP A 132 -3.186 21.650 40.460 1.00 60.13 O ATOM 992 CB ASP A 132 -3.016 24.753 39.435 1.00 62.90 C ATOM 993 CG ASP A 132 -4.011 25.825 39.026 1.00 65.13 C ATOM 994 OD1 ASP A 132 -5.207 25.769 39.392 1.00 66.10 O ATOM 995 OD2 ASP A 132 -3.549 26.772 38.344 1.00 66.60 O ATOM 996 N TRP A 133 -1.738 22.738 41.791 1.00 56.60 N ATOM 997 CA TRP A 133 -0.857 21.633 42.135 1.00 52.81 C ATOM 998 C TRP A 133 -1.024 21.044 43.538 1.00 51.69 C ATOM 999 O TRP A 133 -1.323 21.735 44.493 1.00 46.77 O ATOM 1000 CB TRP A 133 0.578 22.248 42.016 1.00 48.27 C ATOM 1001 CG TRP A 133 0.925 22.595 40.595 1.00 44.32 C ATOM 1002 CD1 TRP A 133 0.993 23.849 40.041 1.00 43.47 C ATOM 1003 CD2 TRP A 133 1.294 21.678 39.572 1.00 41.10 C ATOM 1004 NE1 TRP A 133 1.378 23.772 38.737 1.00 44.43 N ATOM 1005 CE2 TRP A 133 1.525 22.422 38.413 1.00 44.02 C ATOM 1006 CE3 TRP A 133 1.365 20.283 39.524 1.00 43.30 C ATOM 1007 CZ2 TRP A 133 1.924 21.851 37.212 1.00 42.21 C ATOM 1008 CZ3 TRP A 133 1.740 19.672 38.341 1.00 42.87 C ATOM 1009 CH2 TRP A 133 2.035 20.467 37.230 1.00 45.20 C ATOM 1010 N GLU A 134 -0.691 19.762 43.605 1.00 52.06 N ATOM 1011 CA GLU A 134 -0.722 18.937 44.775 1.00 51.84 C ATOM 1012 C GLU A 134 0.676 18.350 45.047 1.00 48.73 C ATOM 1013 O GLU A 134 1.131 17.455 44.364 1.00 48.14 O ATOM 1014 CB GLU A 134 -1.653 17.701 44.742 1.00 53.80 C ATOM 1015 CG GLU A 134 -1.777 17.009 46.098 1.00 60.52 C ATOM 1016 CD GLU A 134 -2.574 15.796 46.306 1.00 64.73 C ATOM 1017 OE1 GLU A 134 -3.357 15.238 45.479 1.00 69.45 O ATOM 1018 OE2 GLU A 134 -2.393 15.257 47.435 1.00 66.23 O ATOM 1019 N SER A 135 1.276 18.903 46.079 1.00 47.36 N ATOM 1020 CA SER A 135 2.615 18.471 46.557 1.00 43.50 C ATOM 1021 C SER A 135 2.406 17.024 47.029 1.00 42.97 C ATOM 1022 O SER A 135 1.532 16.898 47.930 1.00 46.07 O ATOM 1023 CB SER A 135 3.017 19.318 47.759 1.00 39.67 C ATOM 1024 OG SER A 135 4.186 18.826 48.357 1.00 42.47 O ATOM 1025 N VAL A 136 3.027 16.068 46.407 1.00 37.83 N ATOM 1026 CA VAL A 136 2.799 14.671 46.804 1.00 36.04 C ATOM 1027 C VAL A 136 4.109 14.041 47.236 1.00 36.40 C ATOM 1028 O VAL A 136 4.181 12.808 47.137 1.00 40.25 O ATOM 1029 CB VAL A 136 2.173 13.845 45.661 1.00 39.31 C ATOM 1030 CG1 VAL A 136 1.134 14.604 44.828 1.00 40.78 C ATOM 1031 CG2 VAL A 136 3.250 13.292 44.713 1.00 39.14 C ATOM 1032 N PHE A 137 5.103 14.818 47.625 1.00 35.96 N ATOM 1033 CA PHE A 137 6.377 14.229 48.059 1.00 32.74 C ATOM 1034 C PHE A 137 7.330 15.349 48.399 1.00 35.16 C ATOM 1035 O PHE A 137 7.447 16.341 47.684 1.00 36.85 O ATOM 1036 CB PHE A 137 6.949 13.235 47.079 1.00 34.86 C ATOM 1037 CG PHE A 137 8.418 12.925 47.236 1.00 33.02 C ATOM 1038 CD1 PHE A 137 8.797 11.755 47.903 1.00 36.29 C ATOM 1039 CD2 PHE A 137 9.384 13.777 46.750 1.00 29.68 C ATOM 1040 CE1 PHE A 137 10.167 11.442 48.072 1.00 31.59 C ATOM 1041 CE2 PHE A 137 10.739 13.502 46.892 1.00 28.78 C ATOM 1042 CZ PHE A 137 11.101 12.305 47.554 1.00 29.00 C ATOM 1043 N SER A 138 8.092 15.061 49.439 1.00 36.76 N ATOM 1044 CA SER A 138 9.032 16.002 50.072 1.00 34.87 C ATOM 1045 C SER A 138 10.084 15.176 50.790 1.00 36.19 C ATOM 1046 O SER A 138 9.792 14.057 51.267 1.00 38.44 O ATOM 1047 CB SER A 138 8.127 16.797 51.038 1.00 36.95 C ATOM 1048 OG SER A 138 7.872 18.109 50.606 1.00 37.94 O ATOM 1049 N GLU A 139 11.303 15.624 50.799 1.00 37.40 N ATOM 1050 CA GLU A 139 12.490 15.039 51.392 1.00 35.93 C ATOM 1051 C GLU A 139 13.507 16.178 51.650 1.00 34.76 C ATOM 1052 O GLU A 139 13.856 16.880 50.674 1.00 33.02 O ATOM 1053 CB GLU A 139 13.208 14.084 50.434 1.00 39.54 C ATOM 1054 CG GLU A 139 13.845 12.818 51.025 1.00 37.65 C ATOM 1055 CD GLU A 139 14.779 12.086 50.106 1.00 38.24 C ATOM 1056 OE1 GLU A 139 15.975 12.431 49.901 1.00 36.44 O ATOM 1057 OE2 GLU A 139 14.279 11.022 49.668 1.00 37.57 O ATOM 1058 N PHE A 140 13.952 16.278 52.878 1.00 30.06 N ATOM 1059 CA PHE A 140 14.861 17.344 53.335 1.00 28.28 C ATOM 1060 C PHE A 140 16.260 16.855 53.513 1.00 27.83 C ATOM 1061 O PHE A 140 16.592 15.706 53.817 1.00 27.56 O ATOM 1062 CB PHE A 140 14.313 18.011 54.647 1.00 31.56 C ATOM 1063 CG PHE A 140 15.306 18.956 55.274 1.00 30.47 C ATOM 1064 CD1 PHE A 140 15.304 20.294 54.912 1.00 29.39 C ATOM 1065 CD2 PHE A 140 16.276 18.498 56.178 1.00 29.60 C ATOM 1066 CE1 PHE A 140 16.248 21.160 55.378 1.00 27.49 C ATOM 1067 CE2 PHE A 140 17.235 19.389 56.680 1.00 28.38 C ATOM 1068 CZ PHE A 140 17.188 20.737 56.322 1.00 26.20 C ATOM 1069 N HIS A 141 17.202 17.812 53.331 1.00 30.59 N ATOM 1070 CA HIS A 141 18.626 17.508 53.385 1.00 27.99 C ATOM 1071 C HIS A 141 19.378 18.801 53.652 1.00 31.98 C ATOM 1072 O HIS A 141 19.252 19.826 52.977 1.00 33.27 O ATOM 1073 CB HIS A 141 19.194 16.894 52.100 1.00 30.13 C ATOM 1074 CG HIS A 141 18.582 15.604 51.648 1.00 27.35 C ATOM 1075 ND1 HIS A 141 19.044 14.395 52.039 1.00 29.88 N ATOM 1076 CD2 HIS A 141 17.582 15.334 50.820 1.00 26.85 C ATOM 1077 CE1 HIS A 141 18.308 13.407 51.486 1.00 24.97 C ATOM 1078 NE2 HIS A 141 17.432 13.950 50.767 1.00 24.22 N ATOM 1079 N ASP A 142 20.287 18.639 54.581 1.00 36.52 N ATOM 1080 CA ASP A 142 21.168 19.602 55.179 1.00 36.05 C ATOM 1081 C ASP A 142 22.432 19.695 54.356 1.00 33.52 C ATOM 1082 O ASP A 142 22.810 18.694 53.723 1.00 30.36 O ATOM 1083 CB ASP A 142 21.520 19.137 56.652 1.00 43.79 C ATOM 1084 CG ASP A 142 21.391 20.344 57.581 1.00 50.05 C ATOM 1085 OD1 ASP A 142 20.268 20.862 57.767 1.00 54.54 O ATOM 1086 OD2 ASP A 142 22.406 20.876 58.074 1.00 51.62 O ATOM 1087 N ALA A 143 22.996 20.898 54.433 1.00 29.75 N ATOM 1088 CA ALA A 143 24.245 21.180 53.775 1.00 29.60 C ATOM 1089 C ALA A 143 25.237 20.113 54.137 1.00 30.34 C ATOM 1090 O ALA A 143 24.874 19.331 55.020 1.00 37.96 O ATOM 1091 CB ALA A 143 24.672 22.581 54.118 1.00 29.94 C ATOM 1092 N ASP A 144 26.397 20.009 53.522 1.00 32.68 N ATOM 1093 CA ASP A 144 27.351 18.925 53.978 1.00 30.25 C ATOM 1094 C ASP A 144 28.675 19.254 53.339 1.00 30.80 C ATOM 1095 O ASP A 144 28.799 20.434 52.948 1.00 26.77 O ATOM 1096 CB ASP A 144 26.823 17.575 53.965 1.00 29.53 C ATOM 1097 CG ASP A 144 26.668 17.016 52.578 1.00 36.97 C ATOM 1098 OD1 ASP A 144 27.335 17.625 51.671 1.00 40.39 O ATOM 1099 OD2 ASP A 144 26.047 15.955 52.496 1.00 38.09 O ATOM 1100 N ALA A 145 29.581 18.330 53.401 1.00 33.50 N ATOM 1101 CA ALA A 145 30.966 18.641 52.847 1.00 36.08 C ATOM 1102 C ALA A 145 30.809 19.126 51.437 1.00 38.61 C ATOM 1103 O ALA A 145 31.246 20.200 51.028 1.00 43.10 O ATOM 1104 CB ALA A 145 31.740 17.306 53.019 1.00 33.47 C ATOM 1105 N GLN A 146 30.062 18.383 50.641 1.00 44.08 N ATOM 1106 CA GLN A 146 29.704 18.497 49.255 1.00 45.77 C ATOM 1107 C GLN A 146 28.705 19.577 48.853 1.00 46.20 C ATOM 1108 O GLN A 146 28.806 20.126 47.735 1.00 49.81 O ATOM 1109 CB GLN A 146 28.941 17.165 48.854 1.00 48.23 C ATOM 1110 CG GLN A 146 29.359 16.035 49.825 1.00 50.89 C ATOM 1111 CD GLN A 146 30.755 15.642 49.309 1.00 52.21 C ATOM 1112 OE1 GLN A 146 31.658 16.447 49.429 1.00 52.79 O ATOM 1113 NE2 GLN A 146 30.766 14.504 48.626 1.00 54.63 N ATOM 1114 N ASN A 147 27.636 19.694 49.616 1.00 42.51 N ATOM 1115 CA ASN A 147 26.503 20.554 49.384 1.00 38.07 C ATOM 1116 C ASN A 147 26.348 21.685 50.356 1.00 37.01 C ATOM 1117 O ASN A 147 25.627 21.553 51.334 1.00 37.48 O ATOM 1118 CB ASN A 147 25.245 19.657 49.398 1.00 40.13 C ATOM 1119 CG ASN A 147 25.494 18.521 48.412 1.00 41.23 C ATOM 1120 OD1 ASN A 147 24.890 18.598 47.346 1.00 43.96 O ATOM 1121 ND2 ASN A 147 26.351 17.582 48.791 1.00 40.35 N ATOM 1122 N SER A 148 26.967 22.783 50.052 1.00 36.12 N ATOM 1123 CA SER A 148 27.052 24.000 50.791 1.00 34.09 C ATOM 1124 C SER A 148 25.761 24.522 51.375 1.00 38.58 C ATOM 1125 O SER A 148 25.849 25.407 52.312 1.00 35.22 O ATOM 1126 CB SER A 148 27.896 24.978 50.067 1.00 35.30 C ATOM 1127 OG SER A 148 27.437 26.206 49.710 1.00 34.13 O ATOM 1128 N HIS A 149 24.623 23.988 50.912 1.00 36.31 N ATOM 1129 CA HIS A 149 23.299 24.390 51.329 1.00 29.98 C ATOM 1130 C HIS A 149 22.376 23.174 51.434 1.00 30.92 C ATOM 1131 O HIS A 149 22.641 22.109 50.825 1.00 29.66 O ATOM 1132 CB HIS A 149 22.516 25.364 50.464 1.00 32.20 C ATOM 1133 CG HIS A 149 23.246 26.535 49.909 1.00 34.13 C ATOM 1134 ND1 HIS A 149 23.744 26.619 48.653 1.00 31.80 N ATOM 1135 CD2 HIS A 149 23.464 27.773 50.487 1.00 35.02 C ATOM 1136 CE1 HIS A 149 24.349 27.792 48.508 1.00 33.54 C ATOM 1137 NE2 HIS A 149 24.178 28.523 49.557 1.00 32.44 N ATOM 1138 N SER A 150 21.352 23.410 52.285 1.00 26.95 N ATOM 1139 CA SER A 150 20.300 22.381 52.445 1.00 27.79 C ATOM 1140 C SER A 150 19.291 22.730 51.276 1.00 29.41 C ATOM 1141 O SER A 150 19.260 23.856 50.776 1.00 28.00 O ATOM 1142 CB SER A 150 19.519 22.533 53.749 1.00 27.20 C ATOM 1143 OG SER A 150 19.332 23.941 53.992 1.00 31.47 O ATOM 1144 N TYR A 151 18.383 21.819 51.120 1.00 27.98 N ATOM 1145 CA TYR A 151 17.437 21.824 50.040 1.00 30.36 C ATOM 1146 C TYR A 151 16.425 20.718 50.403 1.00 31.65 C ATOM 1147 O TYR A 151 16.802 19.872 51.152 1.00 30.96 O ATOM 1148 CB TYR A 151 18.148 21.305 48.732 1.00 29.25 C ATOM 1149 CG TYR A 151 18.992 20.057 48.935 1.00 24.37 C ATOM 1150 CD1 TYR A 151 20.342 20.184 49.307 1.00 26.79 C ATOM 1151 CD2 TYR A 151 18.535 18.813 48.663 1.00 25.03 C ATOM 1152 CE1 TYR A 151 21.184 19.082 49.437 1.00 27.43 C ATOM 1153 CE2 TYR A 151 19.354 17.652 48.782 1.00 27.72 C ATOM 1154 CZ TYR A 151 20.663 17.823 49.207 1.00 31.06 C ATOM 1155 OH TYR A 151 21.433 16.678 49.392 1.00 34.27 O ATOM 1156 N CYS A 152 15.285 20.928 49.800 1.00 33.94 N ATOM 1157 CA CYS A 152 14.154 20.037 49.897 1.00 32.79 C ATOM 1158 C CYS A 152 13.673 19.683 48.468 1.00 30.90 C ATOM 1159 O CYS A 152 13.345 20.580 47.652 1.00 30.83 O ATOM 1160 CB CYS A 152 13.047 20.704 50.672 1.00 34.66 C ATOM 1161 SG CYS A 152 12.065 19.577 51.666 1.00 43.57 S ATOM 1162 N PHE A 153 13.709 18.414 48.232 1.00 28.79 N ATOM 1163 CA PHE A 153 13.139 17.857 46.979 1.00 32.52 C ATOM 1164 C PHE A 153 11.609 17.864 47.228 1.00 34.26 C ATOM 1165 O PHE A 153 11.205 17.550 48.369 1.00 35.12 O ATOM 1166 CB PHE A 153 13.587 16.419 46.752 1.00 29.95 C ATOM 1167 CG PHE A 153 15.036 16.209 46.613 1.00 28.77 C ATOM 1168 CD1 PHE A 153 15.781 17.086 45.798 1.00 28.28 C ATOM 1169 CD2 PHE A 153 15.655 15.116 47.186 1.00 31.64 C ATOM 1170 CE1 PHE A 153 17.149 16.886 45.629 1.00 26.13 C ATOM 1171 CE2 PHE A 153 17.042 14.890 47.029 1.00 32.91 C ATOM 1172 CZ PHE A 153 17.761 15.817 46.198 1.00 31.59 C ATOM 1173 N GLU A 154 10.864 18.114 46.164 1.00 34.12 N ATOM 1174 CA GLU A 154 9.391 18.025 46.306 1.00 34.04 C ATOM 1175 C GLU A 154 8.849 17.523 44.975 1.00 35.14 C ATOM 1176 O GLU A 154 9.563 17.657 43.972 1.00 37.98 O ATOM 1177 CB GLU A 154 8.762 19.416 46.511 1.00 31.40 C ATOM 1178 CG GLU A 154 7.232 19.345 46.692 1.00 27.27 C ATOM 1179 CD GLU A 154 6.572 20.643 46.974 1.00 26.48 C ATOM 1180 OE1 GLU A 154 5.389 20.617 47.445 1.00 28.27 O ATOM 1181 OE2 GLU A 154 7.242 21.658 46.658 1.00 19.51 O ATOM 1182 N ILE A 155 7.657 17.008 44.983 1.00 36.74 N ATOM 1183 CA ILE A 155 6.958 16.544 43.801 1.00 38.52 C ATOM 1184 C ILE A 155 5.483 16.922 43.942 1.00 39.03 C ATOM 1185 O ILE A 155 4.844 16.580 44.926 1.00 39.67 O ATOM 1186 CB ILE A 155 7.146 15.030 43.512 1.00 39.53 C ATOM 1187 CG1 ILE A 155 8.634 14.722 43.194 1.00 36.43 C ATOM 1188 CG2 ILE A 155 6.224 14.517 42.322 1.00 40.49 C ATOM 1189 CD1 ILE A 155 8.899 13.201 43.552 1.00 39.86 C ATOM 1190 N LEU A 156 5.041 17.596 42.912 1.00 41.89 N ATOM 1191 CA LEU A 156 3.698 18.135 42.741 1.00 46.28 C ATOM 1192 C LEU A 156 2.995 17.607 41.487 1.00 48.68 C ATOM 1193 O LEU A 156 3.568 17.573 40.373 1.00 49.34 O ATOM 1194 CB LEU A 156 3.875 19.675 42.743 1.00 45.51 C ATOM 1195 CG LEU A 156 4.790 20.223 43.830 1.00 44.48 C ATOM 1196 CD1 LEU A 156 6.140 19.526 43.835 1.00 46.82 C ATOM 1197 CD2 LEU A 156 5.104 21.681 43.494 1.00 46.64 C ATOM 1198 N GLU A 157 1.707 17.329 41.678 1.00 50.31 N ATOM 1199 CA GLU A 157 0.800 16.850 40.634 1.00 51.56 C ATOM 1200 C GLU A 157 -0.310 17.819 40.341 1.00 55.43 C ATOM 1201 O GLU A 157 -1.023 18.251 41.284 1.00 58.93 O ATOM 1202 CB GLU A 157 0.288 15.463 40.949 1.00 50.37 C ATOM 1203 CG GLU A 157 1.429 14.392 40.905 1.00 53.13 C ATOM 1204 CD GLU A 157 0.893 13.003 40.966 1.00 57.41 C ATOM 1205 OE1 GLU A 157 -0.334 12.787 40.825 1.00 60.55 O ATOM 1206 OE2 GLU A 157 1.730 12.113 41.214 1.00 60.06 O ATOM 1207 N ARG A 158 -0.393 18.232 39.071 1.00 55.97 N ATOM 1208 CA ARG A 158 -1.385 19.223 38.585 1.00 55.15 C ATOM 1209 C ARG A 158 -2.727 18.664 39.062 1.00 59.78 C ATOM 1210 O ARG A 158 -3.047 17.544 38.617 1.00 60.61 O ATOM 1211 CB ARG A 158 -1.346 19.389 37.102 1.00 52.96 C ATOM 1212 CG ARG A 158 -2.425 20.135 36.359 1.00 47.56 C ATOM 1213 CD ARG A 158 -2.071 21.533 36.045 1.00 49.48 C ATOM 1214 NE ARG A 158 -1.063 21.658 34.955 1.00 46.30 N ATOM 1215 CZ ARG A 158 -0.639 22.860 34.595 1.00 47.14 C ATOM 1216 NH1 ARG A 158 -1.050 24.007 35.096 1.00 45.21 N ATOM 1217 NH2 ARG A 158 0.345 22.912 33.654 1.00 52.77 N ATOM 1218 N ARG A 159 -3.344 19.398 39.967 1.00 62.71 N ATOM 1219 CA ARG A 159 -4.555 18.954 40.645 1.00 66.67 C ATOM 1220 C ARG A 159 -5.799 18.933 39.771 1.00 69.50 C ATOM 1221 O ARG A 159 -6.266 20.061 39.482 1.00 70.64 O ATOM 1222 CB ARG A 159 -4.831 19.764 41.921 1.00 67.04 C ATOM 1223 CG ARG A 159 -5.621 18.924 42.937 1.00 69.19 C ATOM 1224 CD ARG A 159 -6.157 19.735 44.062 1.00 68.15 C ATOM 1225 NE ARG A 159 -5.172 20.649 44.611 1.00 66.87 N ATOM 1226 CZ ARG A 159 -4.598 20.458 45.805 1.00 67.99 C ATOM 1227 NH1 ARG A 159 -4.606 19.277 46.411 1.00 68.04 N ATOM 1228 NH2 ARG A 159 -4.087 21.531 46.431 1.00 68.01 N ATOM 1229 OXT ARG A 159 -6.268 17.814 39.440 1.00 69.97 O TER 1230 ARG A 159 HETATM 1231 N1 FOL A 161 17.000 19.895 37.748 1.00 27.05 N HETATM 1232 C2 FOL A 161 17.454 19.764 38.995 1.00 30.68 C HETATM 1233 NA2 FOL A 161 16.717 19.252 39.996 1.00 25.62 N HETATM 1234 N3 FOL A 161 18.722 20.301 39.310 1.00 30.43 N HETATM 1235 C4 FOL A 161 19.555 20.882 38.410 1.00 33.39 C HETATM 1236 O4 FOL A 161 20.739 21.290 38.700 1.00 34.29 O HETATM 1237 C4A FOL A 161 19.063 20.925 37.005 1.00 33.22 C HETATM 1238 N5 FOL A 161 19.915 21.390 36.030 1.00 33.98 N HETATM 1239 C6 FOL A 161 19.386 21.451 34.797 1.00 35.01 C HETATM 1240 C7 FOL A 161 18.089 20.962 34.642 1.00 34.68 C HETATM 1241 N8 FOL A 161 17.292 20.477 35.519 1.00 35.35 N HETATM 1242 C8A FOL A 161 17.831 20.488 36.774 1.00 32.88 C HETATM 1243 C9 FOL A 161 20.178 21.993 33.660 1.00 34.44 C HETATM 1244 N10 FOL A 161 21.659 21.820 33.875 1.00 33.84 N HETATM 1245 C11 FOL A 161 23.788 18.293 34.458 1.00 26.72 C HETATM 1246 C12 FOL A 161 24.403 19.521 34.446 1.00 23.79 C HETATM 1247 C13 FOL A 161 23.715 20.706 34.203 1.00 24.58 C HETATM 1248 C14 FOL A 161 22.379 20.625 34.033 1.00 26.26 C HETATM 1249 C15 FOL A 161 21.728 19.417 33.972 1.00 24.53 C HETATM 1250 C16 FOL A 161 22.408 18.211 34.251 1.00 25.03 C HETATM 1251 C FOL A 161 24.669 17.129 34.647 1.00 30.23 C HETATM 1252 O FOL A 161 25.886 17.163 34.733 1.00 27.01 O HETATM 1253 N FOL A 161 24.026 15.989 34.692 1.00 35.23 N HETATM 1254 CA FOL A 161 24.806 14.717 34.977 1.00 40.15 C HETATM 1255 CB FOL A 161 25.113 14.743 36.489 1.00 48.03 C HETATM 1256 CG FOL A 161 26.518 14.948 37.113 1.00 55.04 C HETATM 1257 CD FOL A 161 27.663 15.645 36.409 1.00 59.41 C HETATM 1258 OE1 FOL A 161 28.711 14.883 36.400 1.00 63.11 O HETATM 1259 OE2 FOL A 161 27.720 16.797 35.912 1.00 59.80 O HETATM 1260 CT FOL A 161 23.903 13.579 34.593 1.00 40.87 C HETATM 1261 O1 FOL A 161 22.631 13.688 34.723 1.00 42.93 O HETATM 1262 O2 FOL A 161 24.491 12.601 34.166 1.00 43.04 O HETATM 1263 PA NAP A 164 17.044 28.534 27.601 1.00 46.16 P HETATM 1264 O1A NAP A 164 15.617 28.131 27.582 1.00 49.13 O HETATM 1265 O2A NAP A 164 17.847 27.487 28.290 1.00 50.15 O HETATM 1266 O5B NAP A 164 17.681 28.911 26.091 1.00 53.00 O HETATM 1267 C5B NAP A 164 16.679 29.590 25.244 1.00 49.98 C HETATM 1268 C4B NAP A 164 16.930 29.415 23.756 1.00 53.16 C HETATM 1269 O4B NAP A 164 16.219 28.523 23.438 1.00 55.21 O HETATM 1270 C3B NAP A 164 16.535 30.611 22.838 1.00 52.57 C HETATM 1271 O3B NAP A 164 17.683 31.501 22.697 1.00 51.80 O HETATM 1272 C2B NAP A 164 16.195 29.863 21.575 1.00 55.32 C HETATM 1273 O2B NAP A 164 17.059 29.755 20.557 1.00 58.01 O HETATM 1274 C1B NAP A 164 15.743 28.568 22.087 1.00 55.00 C HETATM 1275 N9A NAP A 164 14.285 28.410 22.125 1.00 55.22 N HETATM 1276 C8A NAP A 164 13.533 28.454 23.226 1.00 54.94 C HETATM 1277 N7A NAP A 164 12.257 28.258 22.913 1.00 55.47 N HETATM 1278 C5A NAP A 164 12.343 28.052 21.479 1.00 54.07 C HETATM 1279 C6A NAP A 164 11.315 27.825 20.330 1.00 53.18 C HETATM 1280 N6A NAP A 164 9.975 27.683 20.560 1.00 54.01 N HETATM 1281 N1A NAP A 164 11.785 27.636 19.099 1.00 51.99 N HETATM 1282 C2A NAP A 164 13.101 27.872 18.956 1.00 52.21 C HETATM 1283 N3A NAP A 164 14.080 28.148 19.802 1.00 53.45 N HETATM 1284 C4A NAP A 164 13.597 28.183 21.077 1.00 54.97 C HETATM 1285 O3 NAP A 164 17.353 29.899 28.211 1.00 47.36 O HETATM 1286 PN NAP A 164 17.159 30.812 29.496 1.00 41.08 P HETATM 1287 O1N NAP A 164 15.729 30.905 29.744 1.00 42.05 O HETATM 1288 O2N NAP A 164 18.070 31.827 29.609 1.00 37.42 O HETATM 1289 O5D NAP A 164 17.736 29.661 30.648 1.00 43.45 O HETATM 1290 C5D NAP A 164 19.209 29.505 30.855 1.00 36.71 C HETATM 1291 C4D NAP A 164 19.513 29.802 32.381 1.00 36.15 C HETATM 1292 O4D NAP A 164 18.659 28.877 33.141 1.00 38.21 O HETATM 1293 C3D NAP A 164 20.948 29.371 32.852 1.00 36.57 C HETATM 1294 O3D NAP A 164 21.542 30.081 33.856 1.00 40.12 O HETATM 1295 C2D NAP A 164 20.733 27.873 33.213 1.00 36.22 C HETATM 1296 O2D NAP A 164 21.820 27.314 33.828 1.00 40.83 O HETATM 1297 C1D NAP A 164 19.481 27.934 33.912 1.00 35.10 C HETATM 1298 N1N NAP A 164 18.838 26.565 34.200 1.00 34.36 N HETATM 1299 C2N NAP A 164 18.441 26.179 35.484 1.00 32.02 C HETATM 1300 C3N NAP A 164 17.857 25.019 35.733 1.00 32.17 C HETATM 1301 C7N NAP A 164 17.638 24.675 37.132 1.00 28.88 C HETATM 1302 O7N NAP A 164 16.916 23.707 37.484 1.00 28.74 O HETATM 1303 N7N NAP A 164 18.009 25.511 38.092 1.00 27.60 N HETATM 1304 C4N NAP A 164 17.379 24.062 34.591 1.00 34.06 C HETATM 1305 C5N NAP A 164 17.823 24.664 33.253 1.00 28.82 C HETATM 1306 C6N NAP A 164 18.415 25.796 33.150 1.00 29.50 C HETATM 1307 P2B NAP A 164 18.231 30.366 19.833 1.00 57.99 P HETATM 1308 O1X NAP A 164 18.741 29.292 18.811 1.00 62.16 O HETATM 1309 O2X NAP A 164 17.659 31.541 19.082 1.00 62.59 O HETATM 1310 O3X NAP A 164 19.461 30.826 20.586 1.00 59.70 O HETATM 1311 O HOH A 201 12.505 12.961 54.947 1.00 51.99 O HETATM 1312 O HOH A 202 24.597 9.714 17.173 1.00 43.61 O HETATM 1313 O HOH A 203 28.276 13.586 12.108 1.00 43.74 O HETATM 1314 O HOH A 204 28.865 16.674 11.175 1.00 50.31 O HETATM 1315 O HOH A 205 32.529 17.122 20.798 1.00 51.31 O HETATM 1316 O HOH A 206 21.732 21.707 41.337 1.00 35.89 O HETATM 1317 O HOH A 207 22.622 17.863 14.319 1.00 51.89 O HETATM 1318 O HOH A 208 3.605 19.785 51.254 1.00 55.03 O HETATM 1319 O HOH A 209 6.033 12.453 22.307 1.00 46.65 O HETATM 1320 O HOH A 210 21.160 3.946 28.972 1.00 38.48 O HETATM 1321 O HOH A 211 9.171 7.774 30.383 1.00 53.20 O HETATM 1322 O HOH A 212 -3.646 15.994 40.030 1.00 61.34 O HETATM 1323 O HOH A 213 35.245 16.300 51.887 1.00 47.24 O HETATM 1324 O HOH A 214 28.751 20.133 21.335 1.00 54.01 O HETATM 1325 O HOH A 215 -6.357 20.456 48.803 1.00 55.65 O HETATM 1326 O HOH A 216 15.286 36.676 32.671 1.00 45.58 O HETATM 1327 O HOH A 217 11.262 7.383 36.432 1.00 61.52 O HETATM 1328 O HOH A 218 1.412 28.154 33.612 1.00 49.91 O HETATM 1329 O HOH A 219 25.431 29.866 20.475 1.00 52.34 O HETATM 1330 O HOH A 220 17.149 24.019 59.044 1.00 38.56 O HETATM 1331 O HOH A 221 9.163 35.717 44.842 1.00 38.29 O HETATM 1332 O HOH A 222 21.280 8.223 24.432 1.00 53.14 O HETATM 1333 O HOH A 223 33.430 12.873 21.996 1.00 49.23 O HETATM 1334 O HOH A 224 21.818 27.068 17.430 1.00 73.27 O HETATM 1335 O HOH A 225 20.005 33.116 21.752 1.00 62.39 O HETATM 1336 O HOH A 226 21.620 26.733 53.378 1.00 47.02 O HETATM 1337 O HOH A 227 9.632 5.902 37.764 1.00 57.93 O HETATM 1338 O HOH A 228 12.839 33.859 30.427 1.00 58.59 O HETATM 1339 O HOH A 229 8.385 28.394 17.768 1.00 63.46 O HETATM 1340 O HOH A 230 9.774 37.277 47.997 1.00 44.66 O HETATM 1341 O HOH A 231 24.193 20.488 60.206 1.00 58.20 O HETATM 1342 O HOH A 232 22.631 11.517 16.971 1.00 44.76 O HETATM 1343 O HOH A 233 20.655 12.303 45.899 1.00 50.76 O HETATM 1344 O HOH A 234 -1.569 32.471 46.567 1.00 63.59 O HETATM 1345 O HOH A 235 21.783 19.393 12.862 1.00 61.49 O HETATM 1346 O HOH A 236 23.953 22.332 41.234 1.00 49.75 O HETATM 1347 O HOH A 237 22.638 25.148 33.996 1.00 59.90 O HETATM 1348 O HOH A 238 25.333 27.015 18.483 1.00 62.18 O HETATM 1349 O HOH A 239 28.074 28.136 49.683 1.00 38.66 O HETATM 1350 O HOH A 240 20.440 40.384 44.011 1.00 56.07 O HETATM 1351 O HOH A 241 21.489 13.365 49.722 1.00 65.58 O HETATM 1352 O HOH A 301 14.205 18.976 41.138 1.00 46.70 O HETATM 1353 O HOH A 304 18.230 10.848 49.503 1.00 56.27 O HETATM 1354 O HOH A 305 18.069 30.050 52.392 1.00 66.77 O HETATM 1355 O HOH A 310 17.803 23.948 15.471 1.00 52.90 O HETATM 1356 O HOH A 311 15.938 25.827 53.086 1.00 64.41 O HETATM 1357 O HOH A 313 24.868 24.450 33.926 1.00 52.32 O HETATM 1358 O HOH A 314 10.575 31.486 22.285 1.00 62.18 O HETATM 1359 O HOH A 315 -3.585 15.604 43.078 1.00 50.06 O HETATM 1360 O HOH A 317 23.207 16.880 51.064 1.00 52.52 O HETATM 1361 O HOH A 318 -1.222 16.912 49.825 1.00 52.83 O HETATM 1362 O HOH A 323 26.493 29.202 17.029 1.00 56.26 O HETATM 1363 O HOH A 401 21.501 37.242 52.762 0.50 49.74 O HETATM 1364 O HOH A 402 13.909 24.091 52.762 0.50 45.72 O HETATM 1365 O HOH A 403 7.310 12.660 52.762 0.50 66.47 O CONECT 1231 1232 1242 CONECT 1232 1231 1233 1234 CONECT 1233 1232 CONECT 1234 1232 1235 CONECT 1235 1234 1236 1237 CONECT 1236 1235 CONECT 1237 1235 1238 1242 CONECT 1238 1237 1239 CONECT 1239 1238 1240 1243 CONECT 1240 1239 1241 CONECT 1241 1240 1242 CONECT 1242 1231 1237 1241 CONECT 1243 1239 1244 CONECT 1244 1243 1248 CONECT 1245 1246 1250 1251 CONECT 1246 1245 1247 CONECT 1247 1246 1248 CONECT 1248 1244 1247 1249 CONECT 1249 1248 1250 CONECT 1250 1245 1249 CONECT 1251 1245 1252 1253 CONECT 1252 1251 CONECT 1253 1251 1254 CONECT 1254 1253 1255 1260 CONECT 1255 1254 1256 CONECT 1256 1255 1257 CONECT 1257 1256 1258 1259 CONECT 1258 1257 CONECT 1259 1257 CONECT 1260 1254 1261 1262 CONECT 1261 1260 CONECT 1262 1260 CONECT 1263 1264 1265 1266 1285 CONECT 1264 1263 CONECT 1265 1263 CONECT 1266 1263 1267 CONECT 1267 1266 1268 CONECT 1268 1267 1269 1270 CONECT 1269 1268 1274 CONECT 1270 1268 1271 1272 CONECT 1271 1270 CONECT 1272 1270 1273 1274 CONECT 1273 1272 1307 CONECT 1274 1269 1272 1275 CONECT 1275 1274 1276 1284 CONECT 1276 1275 1277 CONECT 1277 1276 1278 CONECT 1278 1277 1279 1284 CONECT 1279 1278 1280 1281 CONECT 1280 1279 CONECT 1281 1279 1282 CONECT 1282 1281 1283 CONECT 1283 1282 1284 CONECT 1284 1275 1278 1283 CONECT 1285 1263 1286 CONECT 1286 1285 1287 1288 1289 CONECT 1287 1286 CONECT 1288 1286 CONECT 1289 1286 1290 CONECT 1290 1289 1291 CONECT 1291 1290 1292 1293 CONECT 1292 1291 1297 CONECT 1293 1291 1294 1295 CONECT 1294 1293 CONECT 1295 1293 1296 1297 CONECT 1296 1295 CONECT 1297 1292 1295 1298 CONECT 1298 1297 1299 1306 CONECT 1299 1298 1300 CONECT 1300 1299 1301 1304 CONECT 1301 1300 1302 1303 CONECT 1302 1301 CONECT 1303 1301 CONECT 1304 1300 1305 CONECT 1305 1304 1306 CONECT 1306 1298 1305 CONECT 1307 1273 1308 1309 1310 CONECT 1308 1307 CONECT 1309 1307 CONECT 1310 1307 MASTER 471 0 2 4 8 0 11 6 1364 1 80 13 END If you find results from this site helpful for your research, please cite one of our papers:
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