Browse entries in the PDBbind-CN Database
HEADER COMPLEX (GTP-BINDING/ATP-BINDING) 18-JUN-96 1GUA TITLE HUMAN RAP1A, RESIDUES 1-167, DOUBLE MUTANT (E30D,K31E) TITLE 2 COMPLEXED WITH GPPNHP AND THE RAS-BINDING-DOMAIN OF HUMAN TITLE 3 C-RAF1, RESIDUES 51-131 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RAP1A; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 1-167; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 OTHER_DETAILS: COMPLEXED TO 5'-GUANOSYL-IMIDO-TRIPHOSPHATE; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: C-RAF1; COMPND 10 CHAIN: B; COMPND 11 FRAGMENT: RESIDUES 51-131; COMPND 12 EC: 2.7.1.-; COMPND 13 ENGINEERED: YES; COMPND 14 OTHER_DETAILS: HUMAN RAP1A AND C-RAF1 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: HUMAN C-RAF1 GENE RESIDUES 51; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: CK600K; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTAC; SOURCE 10 EXPRESSION_SYSTEM_GENE: HUMAN RAP1A GENE; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: HUMAN C-RAF1 GENE RESIDUES 51; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PGEX-RAFRBD; SOURCE 20 EXPRESSION_SYSTEM_GENE: HUMAN C-RAF1 GENE, RESIDUES 51-131; SOURCE 21 OTHER_DETAILS: PURIFIED AS A GST-FUSION PROTEIN WITH SOURCE 22 THROMBIN CLEAVAGE SITE KEYWDS ONCOGENE PROTEIN/KINASE/EFFECTOR PROTEIN GTP-BINDING- KEYWDS 2 PROTEIN, COMPLEX (GTP-BINDING/ATP-BINDING) EXPDTA X-RAY DIFFRACTION AUTHOR N.NASSAR,A.WITTINGHOFER REVDAT 2 24-FEB-09 1GUA 1 VERSN REVDAT 1 11-JAN-97 1GUA 0 JRNL AUTH N.NASSAR,G.HORN,C.HERRMANN,C.BLOCK,R.JANKNECHT, JRNL AUTH 2 A.WITTINGHOFER JRNL TITL RAS/RAP EFFECTOR SPECIFICITY DETERMINED BY CHARGE JRNL TITL 2 REVERSAL. JRNL REF NAT.STRUCT.BIOL. V. 3 723 1996 JRNL REFN ISSN 1072-8368 JRNL PMID 8756332 JRNL DOI 10.1038/NSB0896-723 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.BLOCK,R.JANKNECHT,C.HERRMANN,N.NASSAR, REMARK 1 AUTH 2 A.WITTINGHOFER REMARK 1 TITL QUANTITATIVE STRUCTURE-ACTIVITY ANALYSIS REMARK 1 TITL 2 CORRELATING RAS/RAF INTERACTION IN VITRO TO RAF REMARK 1 TITL 3 ACTIVATION IN VIVO REMARK 1 REF NAT.STRUCT.BIOL. V. 3 244 1996 REMARK 1 REFN ISSN 1072-8368 REMARK 1 REFERENCE 2 REMARK 1 AUTH C.HERRMANN,G.A.MARTIN,A.WITTINGHOFER REMARK 1 TITL QUANTITATIVE ANALYSIS OF THE COMPLEX BETWEEN REMARK 1 TITL 2 P21RAS AND THE RAS-BINDING DOMAIN OF THE HUMAN REMARK 1 TITL 3 RAF-1 PROTEIN KINASE REMARK 1 REF J.BIOL.CHEM. V. 270 2901 1995 REMARK 1 REFN ISSN 0021-9258 REMARK 1 REFERENCE 3 REMARK 1 AUTH N.NASSAR,G.HORN,C.HERRMANN,A.SCHERER,F.MCCORMICK, REMARK 1 AUTH 2 A.WITTINGHOFER REMARK 1 TITL THE 2.2 A CRYSTAL STRUCTURE OF THE RAS-BINDING REMARK 1 TITL 2 DOMAIN OF THE SERINE/THREONINE KINASE C-RAF1 IN REMARK 1 TITL 3 COMPLEX WITH RAP1A AND A GTP ANALOGUE REMARK 1 REF NATURE V. 375 554 1995 REMARK 1 REFN ISSN 0028-0836 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 21693 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 SET) : 0.220 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 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1940 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 34 REMARK 3 SOLVENT ATOMS : 89 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.90 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) : 0.25 REMARK 3 ESD FROM SIGMAA (A) : 0.21 REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.013 REMARK 3 BOND ANGLES (DEGREES) : 1.94 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE ELECTRON DENSITY FOR THE SIDE REMARK 3 CHAINS OF RESIDUES 104 - 107 FROM RBD (CHAIN B) IS WEAK. REMARK 4 REMARK 4 1GUA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. 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) : N REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : SIEMENS HI-STAR REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21975 REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 200 DATA REDUNDANCY : 5.100 REMARK 200 R MERGE (I) : 0.04900 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: X-PLOR 3.1 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 22.25000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.15000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.90000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.15000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.25000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.90000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 PRO B 51 REMARK 465 SER B 52 REMARK 465 LYS B 53 REMARK 465 THR B 54 REMARK 465 SER B 55 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 CYS A 141 CA - CB - SG ANGL. DEV. = 8.4 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 105 47.04 70.90 REMARK 500 LYS A 117 36.09 71.80 REMARK 500 LEU A 120 60.83 -102.02 REMARK 500 HIS B 105 61.19 -102.91 REMARK 500 LYS B 106 81.45 7.75 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 171 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GNP A 170 O3G REMARK 620 2 GNP A 170 O2B 96.6 REMARK 620 3 SER A 17 OG 171.0 90.1 REMARK 620 4 THR A 35 OG1 92.2 171.0 81.4 REMARK 620 5 HOH A 501 O 90.0 90.5 84.0 91.7 REMARK 620 6 HOH A 502 O 96.0 91.4 89.8 85.5 173.5 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 132 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLY B 123 O REMARK 620 2 GLU B 125 OE2 74.0 REMARK 620 3 GLU B 125 OE1 93.6 48.4 REMARK 620 4 HOH B 517 O 92.3 118.9 74.6 REMARK 620 5 HOH B 531 O 84.9 78.4 124.2 161.1 REMARK 620 6 HOH B 574 O 80.5 149.9 151.1 77.3 83.7 REMARK 620 7 ASP B 80 OD1 154.4 130.9 107.9 80.5 93.9 73.9 REMARK 620 8 ASP B 80 OD2 154.2 80.2 69.4 101.1 89.0 123.7 51.0 REMARK 620 N 1 2 3 4 5 6 7 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 171 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 132 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 170 DBREF 1GUA A 1 167 UNP P62834 RAP1A_HUMAN 1 167 DBREF 1GUA B 51 131 UNP P04049 RAF1_HUMAN 51 131 SEQADV 1GUA ASP A 30 UNP P62834 GLU 30 ENGINEERED SEQADV 1GUA GLU A 31 UNP P62834 LYS 31 ENGINEERED SEQRES 1 A 167 MET ARG GLU TYR LYS LEU VAL VAL LEU GLY SER GLY GLY SEQRES 2 A 167 VAL GLY LYS SER ALA LEU THR VAL GLN PHE VAL GLN GLY SEQRES 3 A 167 ILE PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SER SEQRES 4 A 167 TYR ARG LYS GLN VAL GLU VAL ASP CYS GLN GLN CYS MET SEQRES 5 A 167 LEU GLU ILE LEU ASP THR ALA GLY THR GLU GLN PHE THR SEQRES 6 A 167 ALA MET ARG ASP LEU TYR MET LYS ASN GLY GLN GLY PHE SEQRES 7 A 167 ALA LEU VAL TYR SER ILE THR ALA GLN SER THR PHE ASN SEQRES 8 A 167 ASP LEU GLN ASP LEU ARG GLU GLN ILE LEU ARG VAL LYS SEQRES 9 A 167 ASP THR GLU ASP VAL PRO MET ILE LEU VAL GLY ASN LYS SEQRES 10 A 167 CYS ASP LEU GLU ASP GLU ARG VAL VAL GLY LYS GLU GLN SEQRES 11 A 167 GLY GLN ASN LEU ALA ARG GLN TRP CYS ASN CYS ALA PHE SEQRES 12 A 167 LEU GLU SER SER ALA LYS SER LYS ILE ASN VAL ASN GLU SEQRES 13 A 167 ILE PHE TYR ASP LEU VAL ARG GLN ILE ASN ARG SEQRES 1 B 81 PRO SER LYS THR SER ASN THR ILE ARG VAL PHE LEU PRO SEQRES 2 B 81 ASN LYS GLN ARG THR VAL VAL ASN VAL ARG ASN GLY MET SEQRES 3 B 81 SER LEU HIS ASP CYS LEU MET LYS ALA LEU LYS VAL ARG SEQRES 4 B 81 GLY LEU GLN PRO GLU CYS CYS ALA VAL PHE ARG LEU LEU SEQRES 5 B 81 HIS GLU HIS LYS GLY LYS LYS ALA ARG LEU ASP TRP ASN SEQRES 6 B 81 THR ASP ALA ALA SER LEU ILE GLY GLU GLU LEU GLN VAL SEQRES 7 B 81 ASP PHE LEU HET MG A 171 1 HET CA B 132 1 HET GNP A 170 32 HETNAM MG MAGNESIUM ION HETNAM CA CALCIUM ION HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER FORMUL 3 MG MG 2+ FORMUL 4 CA CA 2+ FORMUL 5 GNP C10 H17 N6 O13 P3 FORMUL 6 HOH *89(H2 O) HELIX 1 1 LYS A 16 GLN A 25 1 10 HELIX 2 2 ALA A 66 ASN A 74 5 9 HELIX 3 3 GLN A 87 LYS A 104 1 18 HELIX 4 4 GLU A 121 GLU A 123 5 3 HELIX 5 5 LYS A 128 GLN A 137 1 10 HELIX 6 6 VAL A 154 ILE A 165 1 12 HELIX 7 7 LEU B 78 ARG B 89 1 12 HELIX 8 8 PRO B 93 CYS B 95 5 3 HELIX 9 9 ALA B 118 LEU B 121 5 4 SHEET 1 A11 ALA A 142 GLU A 145 0 SHEET 2 A11 PRO A 110 ASN A 116 1 N LEU A 113 O ALA A 142 SHEET 3 A11 GLY A 77 SER A 83 1 N PHE A 78 O PRO A 110 SHEET 4 A11 GLU A 3 GLY A 10 1 N VAL A 7 O GLY A 77 SHEET 5 A11 GLN A 49 ASP A 57 1 N MET A 52 O TYR A 4 SHEET 6 A11 GLU A 37 VAL A 46 -1 N VAL A 46 O GLN A 49 SHEET 7 A11 GLN B 66 ASN B 71 -1 N VAL B 69 O GLU A 37 SHEET 8 A11 THR B 57 LEU B 62 -1 N LEU B 62 O GLN B 66 SHEET 9 A11 GLU B 125 PHE B 130 1 N LEU B 126 O ARG B 59 SHEET 10 A11 CYS B 96 LEU B 102 -1 N PHE B 99 O GLN B 127 SHEET 11 A11 LYS B 108 LEU B 112 -1 N LEU B 112 O VAL B 98 LINK O3G GNP A 170 MG MG A 171 1555 1555 2.10 LINK O2B GNP A 170 MG MG A 171 1555 1555 2.22 LINK MG MG A 171 OG SER A 17 1555 1555 2.33 LINK MG MG A 171 OG1 THR A 35 1555 1555 2.16 LINK CA CA B 132 O GLY B 123 1555 1555 2.36 LINK MG MG A 171 O HOH A 501 1555 1555 2.21 LINK MG MG A 171 O HOH A 502 1555 1555 2.13 LINK CA CA B 132 OE2 GLU B 125 1555 1555 2.71 LINK CA CA B 132 OE1 GLU B 125 1555 1555 2.55 LINK CA CA B 132 O HOH B 517 1555 1555 2.26 LINK CA CA B 132 O HOH B 531 1555 1555 2.36 LINK CA CA B 132 O HOH B 574 1555 1555 2.32 LINK CA CA B 132 OD1 ASP B 80 1555 4556 2.50 LINK CA CA B 132 OD2 ASP B 80 1555 4556 2.55 SITE 1 AC1 5 SER A 17 THR A 35 GNP A 170 HOH A 501 SITE 2 AC1 5 HOH A 502 SITE 1 AC2 6 ASP B 80 GLY B 123 GLU B 125 HOH B 517 SITE 2 AC2 6 HOH B 531 HOH B 574 SITE 1 AC3 25 GLY A 12 GLY A 13 VAL A 14 GLY A 15 SITE 2 AC3 25 LYS A 16 SER A 17 ALA A 18 PHE A 28 SITE 3 AC3 25 VAL A 29 ASP A 30 GLU A 31 PRO A 34 SITE 4 AC3 25 THR A 35 GLN A 50 GLY A 60 ASN A 116 SITE 5 AC3 25 LYS A 117 ASP A 119 SER A 147 ALA A 148 SITE 6 AC3 25 MG A 171 HOH A 501 HOH A 503 HOH A 526 SITE 7 AC3 25 HOH A 537 CRYST1 44.500 71.800 100.300 90.00 90.00 90.00 P 21 21 21 4 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 0.022472 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013928 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009970 0.00000 ATOM 1 N MET A 1 9.848 -2.435 29.104 1.00 36.52 N ATOM 2 CA MET A 1 10.059 -1.653 27.847 1.00 35.42 C ATOM 3 C MET A 1 10.888 -0.430 28.242 1.00 34.33 C ATOM 4 O MET A 1 11.011 -0.124 29.441 1.00 34.73 O ATOM 5 CB MET A 1 8.700 -1.285 27.205 1.00 35.76 C ATOM 6 CG MET A 1 7.772 -0.435 28.061 1.00 36.14 C ATOM 7 SD MET A 1 6.034 -0.917 27.923 1.00 37.16 S ATOM 8 CE MET A 1 5.634 -1.086 29.679 1.00 35.94 C ATOM 9 N ARG A 2 11.543 0.182 27.260 1.00 32.97 N ATOM 10 CA ARG A 2 12.401 1.358 27.468 1.00 31.73 C ATOM 11 C ARG A 2 11.656 2.643 27.846 1.00 29.56 C ATOM 12 O ARG A 2 10.580 2.932 27.323 1.00 28.35 O ATOM 13 CB ARG A 2 13.233 1.594 26.209 1.00 33.44 C ATOM 14 CG ARG A 2 14.345 2.613 26.341 1.00 35.47 C ATOM 15 CD ARG A 2 15.126 2.633 25.043 1.00 38.25 C ATOM 16 NE ARG A 2 16.108 3.708 25.009 1.00 39.68 N ATOM 17 CZ ARG A 2 16.790 4.041 23.928 1.00 40.36 C ATOM 18 NH1 ARG A 2 16.596 3.381 22.783 1.00 41.17 N ATOM 19 NH2 ARG A 2 17.660 5.036 23.987 1.00 41.14 N ATOM 20 N GLU A 3 12.249 3.389 28.768 1.00 27.55 N ATOM 21 CA GLU A 3 11.708 4.637 29.281 1.00 26.41 C ATOM 22 C GLU A 3 12.380 5.853 28.638 1.00 23.05 C ATOM 23 O GLU A 3 13.586 5.860 28.393 1.00 22.28 O ATOM 24 CB GLU A 3 11.948 4.693 30.790 1.00 29.33 C ATOM 25 CG GLU A 3 10.746 4.510 31.672 1.00 34.34 C ATOM 26 CD GLU A 3 10.309 5.815 32.375 1.00 38.09 C ATOM 27 OE1 GLU A 3 11.091 6.411 33.183 1.00 39.21 O ATOM 28 OE2 GLU A 3 9.159 6.253 32.122 1.00 40.20 O ATOM 29 N TYR A 4 11.581 6.865 28.328 1.00 20.40 N ATOM 30 CA TYR A 4 12.083 8.109 27.726 1.00 17.69 C ATOM 31 C TYR A 4 11.620 9.279 28.591 1.00 15.71 C ATOM 32 O TYR A 4 10.431 9.416 28.844 1.00 15.25 O ATOM 33 CB TYR A 4 11.549 8.253 26.302 1.00 16.45 C ATOM 34 CG TYR A 4 12.073 7.210 25.360 1.00 16.63 C ATOM 35 CD1 TYR A 4 13.322 7.349 24.775 1.00 17.84 C ATOM 36 CD2 TYR A 4 11.335 6.079 25.070 1.00 17.10 C ATOM 37 CE1 TYR A 4 13.823 6.393 23.921 1.00 18.77 C ATOM 38 CE2 TYR A 4 11.834 5.108 24.221 1.00 18.94 C ATOM 39 CZ TYR A 4 13.075 5.276 23.651 1.00 18.99 C ATOM 40 OH TYR A 4 13.573 4.328 22.798 1.00 20.16 O ATOM 41 N LYS A 5 12.552 10.078 29.092 1.00 14.57 N ATOM 42 CA LYS A 5 12.182 11.207 29.939 1.00 13.84 C ATOM 43 C LYS A 5 12.170 12.522 29.185 1.00 12.48 C ATOM 44 O LYS A 5 13.209 13.044 28.831 1.00 12.24 O ATOM 45 CB LYS A 5 13.108 11.304 31.151 1.00 15.03 C ATOM 46 CG LYS A 5 13.154 10.039 31.993 1.00 18.04 C ATOM 47 CD LYS A 5 13.727 10.310 33.355 1.00 22.94 C ATOM 48 CE LYS A 5 12.832 11.285 34.111 1.00 25.49 C ATOM 49 NZ LYS A 5 13.331 11.617 35.471 1.00 28.26 N ATOM 50 N LEU A 6 10.986 13.066 28.958 1.00 11.69 N ATOM 51 CA LEU A 6 10.868 14.312 28.212 1.00 11.05 C ATOM 52 C LEU A 6 10.386 15.451 29.090 1.00 9.89 C ATOM 53 O LEU A 6 9.610 15.256 30.014 1.00 10.18 O ATOM 54 CB LEU A 6 9.913 14.128 27.011 1.00 10.97 C ATOM 55 CG LEU A 6 10.042 12.842 26.171 1.00 9.03 C ATOM 56 CD1 LEU A 6 8.913 12.736 25.196 1.00 9.16 C ATOM 57 CD2 LEU A 6 11.352 12.790 25.475 1.00 7.97 C ATOM 58 N VAL A 7 10.842 16.647 28.790 1.00 10.09 N ATOM 59 CA VAL A 7 10.443 17.819 29.549 1.00 9.99 C ATOM 60 C VAL A 7 9.858 18.830 28.583 1.00 9.15 C ATOM 61 O VAL A 7 10.429 19.077 27.540 1.00 9.26 O ATOM 62 CB VAL A 7 11.648 18.471 30.265 1.00 10.17 C ATOM 63 CG1 VAL A 7 11.179 19.580 31.206 1.00 9.16 C ATOM 64 CG2 VAL A 7 12.472 17.426 31.014 1.00 10.95 C ATOM 65 N VAL A 8 8.684 19.358 28.900 1.00 9.28 N ATOM 66 CA VAL A 8 8.042 20.390 28.080 1.00 9.65 C ATOM 67 C VAL A 8 8.274 21.740 28.767 1.00 10.05 C ATOM 68 O VAL A 8 7.825 21.967 29.893 1.00 9.43 O ATOM 69 CB VAL A 8 6.540 20.163 27.933 1.00 9.95 C ATOM 70 CG1 VAL A 8 5.942 21.220 27.014 1.00 8.75 C ATOM 71 CG2 VAL A 8 6.268 18.766 27.376 1.00 9.20 C ATOM 72 N LEU A 9 8.990 22.620 28.086 1.00 10.61 N ATOM 73 CA LEU A 9 9.322 23.942 28.600 1.00 10.34 C ATOM 74 C LEU A 9 8.692 25.050 27.784 1.00 11.02 C ATOM 75 O LEU A 9 8.332 24.850 26.621 1.00 10.09 O ATOM 76 CB LEU A 9 10.831 24.129 28.571 1.00 9.91 C ATOM 77 CG LEU A 9 11.637 23.192 29.439 1.00 10.66 C ATOM 78 CD1 LEU A 9 13.019 23.036 28.902 1.00 11.08 C ATOM 79 CD2 LEU A 9 11.655 23.754 30.832 1.00 12.43 C ATOM 80 N GLY A 10 8.600 26.234 28.397 1.00 11.90 N ATOM 81 CA GLY A 10 8.044 27.392 27.725 1.00 11.22 C ATOM 82 C GLY A 10 7.376 28.345 28.680 1.00 11.24 C ATOM 83 O GLY A 10 7.125 27.988 29.818 1.00 10.93 O ATOM 84 N SER A 11 7.084 29.553 28.219 1.00 11.25 N ATOM 85 CA SER A 11 6.435 30.571 29.045 1.00 10.65 C ATOM 86 C SER A 11 4.973 30.242 29.276 1.00 9.88 C ATOM 87 O SER A 11 4.436 29.343 28.657 1.00 8.12 O ATOM 88 CB SER A 11 6.567 31.947 28.392 1.00 11.44 C ATOM 89 OG SER A 11 7.931 32.334 28.335 1.00 13.20 O ATOM 90 N GLY A 12 4.321 31.023 30.130 1.00 9.96 N ATOM 91 CA GLY A 12 2.936 30.774 30.465 1.00 9.41 C ATOM 92 C GLY A 12 1.912 31.012 29.385 1.00 10.23 C ATOM 93 O GLY A 12 2.040 31.950 28.607 1.00 11.51 O ATOM 94 N GLY A 13 0.919 30.123 29.334 1.00 9.06 N ATOM 95 CA GLY A 13 -0.189 30.209 28.407 1.00 8.88 C ATOM 96 C GLY A 13 0.069 29.816 26.967 1.00 9.71 C ATOM 97 O GLY A 13 -0.795 30.019 26.108 1.00 10.16 O ATOM 98 N VAL A 14 1.243 29.272 26.683 1.00 10.51 N ATOM 99 CA VAL A 14 1.579 28.897 25.322 1.00 9.66 C ATOM 100 C VAL A 14 0.930 27.590 24.867 1.00 10.67 C ATOM 101 O VAL A 14 0.895 27.310 23.675 1.00 10.42 O ATOM 102 CB VAL A 14 3.132 28.818 25.101 1.00 9.65 C ATOM 103 CG1 VAL A 14 3.776 30.162 25.398 1.00 7.47 C ATOM 104 CG2 VAL A 14 3.769 27.694 25.922 1.00 7.20 C ATOM 105 N GLY A 15 0.431 26.799 25.813 1.00 9.85 N ATOM 106 CA GLY A 15 -0.192 25.535 25.481 1.00 9.06 C ATOM 107 C GLY A 15 0.579 24.282 25.877 1.00 10.24 C ATOM 108 O GLY A 15 0.256 23.200 25.404 1.00 10.61 O ATOM 109 N LYS A 16 1.585 24.386 26.731 1.00 9.51 N ATOM 110 CA LYS A 16 2.339 23.202 27.157 1.00 9.70 C ATOM 111 C LYS A 16 1.419 22.078 27.664 1.00 9.92 C ATOM 112 O LYS A 16 1.562 20.925 27.256 1.00 9.19 O ATOM 113 CB LYS A 16 3.345 23.553 28.260 1.00 10.22 C ATOM 114 CG LYS A 16 4.505 24.442 27.824 1.00 10.08 C ATOM 115 CD LYS A 16 5.493 24.739 28.958 1.00 8.65 C ATOM 116 CE LYS A 16 4.864 25.527 30.058 1.00 8.91 C ATOM 117 NZ LYS A 16 4.098 26.680 29.571 1.00 10.18 N ATOM 118 N SER A 17 0.497 22.417 28.564 1.00 9.61 N ATOM 119 CA SER A 17 -0.431 21.441 29.115 1.00 9.79 C ATOM 120 C SER A 17 -1.446 20.958 28.097 1.00 10.40 C ATOM 121 O SER A 17 -1.816 19.781 28.092 1.00 9.31 O ATOM 122 CB SER A 17 -1.155 22.000 30.329 1.00 9.96 C ATOM 123 OG SER A 17 -0.247 22.260 31.364 1.00 9.72 O ATOM 124 N ALA A 18 -1.940 21.872 27.279 1.00 9.85 N ATOM 125 CA ALA A 18 -2.899 21.505 26.256 1.00 10.43 C ATOM 126 C ALA A 18 -2.321 20.498 25.262 1.00 9.95 C ATOM 127 O ALA A 18 -3.041 19.634 24.772 1.00 11.46 O ATOM 128 CB ALA A 18 -3.388 22.722 25.526 1.00 10.81 C ATOM 129 N LEU A 19 -1.048 20.642 24.922 1.00 8.96 N ATOM 130 CA LEU A 19 -0.397 19.729 24.004 1.00 9.53 C ATOM 131 C LEU A 19 -0.221 18.379 24.688 1.00 10.47 C ATOM 132 O LEU A 19 -0.551 17.339 24.118 1.00 10.36 O ATOM 133 CB LEU A 19 0.958 20.283 23.588 1.00 9.46 C ATOM 134 CG LEU A 19 0.946 21.408 22.552 1.00 10.33 C ATOM 135 CD1 LEU A 19 2.331 22.025 22.428 1.00 10.23 C ATOM 136 CD2 LEU A 19 0.461 20.879 21.215 1.00 9.77 C ATOM 137 N THR A 20 0.244 18.415 25.934 1.00 10.51 N ATOM 138 CA THR A 20 0.466 17.220 26.727 1.00 10.13 C ATOM 139 C THR A 20 -0.783 16.401 26.962 1.00 9.66 C ATOM 140 O THR A 20 -0.776 15.211 26.674 1.00 9.53 O ATOM 141 CB THR A 20 1.137 17.544 28.062 1.00 9.89 C ATOM 142 OG1 THR A 20 2.349 18.263 27.811 1.00 10.92 O ATOM 143 CG2 THR A 20 1.479 16.273 28.805 1.00 9.77 C ATOM 144 N VAL A 21 -1.858 17.002 27.462 1.00 9.40 N ATOM 145 CA VAL A 21 -3.048 16.202 27.685 1.00 10.53 C ATOM 146 C VAL A 21 -3.768 15.795 26.398 1.00 11.44 C ATOM 147 O VAL A 21 -4.472 14.795 26.370 1.00 11.52 O ATOM 148 CB VAL A 21 -4.006 16.733 28.824 1.00 11.26 C ATOM 149 CG1 VAL A 21 -3.316 17.698 29.717 1.00 9.97 C ATOM 150 CG2 VAL A 21 -5.309 17.206 28.311 1.00 12.30 C ATOM 151 N GLN A 22 -3.583 16.552 25.324 1.00 11.22 N ATOM 152 CA GLN A 22 -4.171 16.167 24.051 1.00 11.47 C ATOM 153 C GLN A 22 -3.414 14.896 23.631 1.00 11.40 C ATOM 154 O GLN A 22 -4.027 13.918 23.218 1.00 12.20 O ATOM 155 CB GLN A 22 -3.996 17.277 23.013 1.00 13.19 C ATOM 156 CG GLN A 22 -4.539 16.965 21.623 1.00 15.21 C ATOM 157 CD GLN A 22 -6.034 16.854 21.599 1.00 17.63 C ATOM 158 OE1 GLN A 22 -6.571 15.768 21.527 1.00 18.57 O ATOM 159 NE2 GLN A 22 -6.718 17.978 21.628 1.00 18.74 N ATOM 160 N PHE A 23 -2.096 14.877 23.830 1.00 11.12 N ATOM 161 CA PHE A 23 -1.270 13.719 23.484 1.00 12.00 C ATOM 162 C PHE A 23 -1.562 12.461 24.298 1.00 13.24 C ATOM 163 O PHE A 23 -1.690 11.360 23.736 1.00 12.82 O ATOM 164 CB PHE A 23 0.225 14.053 23.571 1.00 11.83 C ATOM 165 CG PHE A 23 1.132 12.853 23.372 1.00 14.19 C ATOM 166 CD1 PHE A 23 1.269 12.263 22.118 1.00 15.13 C ATOM 167 CD2 PHE A 23 1.848 12.309 24.440 1.00 14.48 C ATOM 168 CE1 PHE A 23 2.092 11.160 21.925 1.00 14.75 C ATOM 169 CE2 PHE A 23 2.670 11.202 24.244 1.00 14.76 C ATOM 170 CZ PHE A 23 2.787 10.631 22.986 1.00 15.24 C ATOM 171 N VAL A 24 -1.657 12.605 25.617 1.00 12.44 N ATOM 172 CA VAL A 24 -1.916 11.452 26.460 1.00 12.97 C ATOM 173 C VAL A 24 -3.369 11.051 26.624 1.00 13.79 C ATOM 174 O VAL A 24 -3.666 9.878 26.744 1.00 15.19 O ATOM 175 CB VAL A 24 -1.305 11.612 27.881 1.00 13.39 C ATOM 176 CG1 VAL A 24 0.192 11.823 27.804 1.00 12.85 C ATOM 177 CG2 VAL A 24 -1.958 12.734 28.616 1.00 14.11 C ATOM 178 N GLN A 25 -4.295 11.987 26.573 1.00 13.57 N ATOM 179 CA GLN A 25 -5.663 11.613 26.832 1.00 14.43 C ATOM 180 C GLN A 25 -6.645 11.918 25.752 1.00 15.11 C ATOM 181 O GLN A 25 -7.796 11.512 25.836 1.00 15.40 O ATOM 182 CB GLN A 25 -6.091 12.261 28.138 1.00 16.66 C ATOM 183 CG GLN A 25 -7.146 11.518 28.930 1.00 18.74 C ATOM 184 CD GLN A 25 -6.815 10.060 29.176 1.00 20.55 C ATOM 185 OE1 GLN A 25 -7.699 9.221 29.116 1.00 23.51 O ATOM 186 NE2 GLN A 25 -5.562 9.753 29.475 1.00 21.07 N ATOM 187 N GLY A 26 -6.214 12.655 24.738 1.00 16.14 N ATOM 188 CA GLY A 26 -7.111 12.996 23.647 1.00 17.01 C ATOM 189 C GLY A 26 -8.190 13.961 24.060 1.00 18.54 C ATOM 190 O GLY A 26 -9.243 14.011 23.435 1.00 19.91 O ATOM 191 N ILE A 27 -7.915 14.746 25.096 1.00 18.67 N ATOM 192 CA ILE A 27 -8.849 15.728 25.640 1.00 19.06 C ATOM 193 C ILE A 27 -8.285 17.110 25.308 1.00 18.24 C ATOM 194 O ILE A 27 -7.068 17.282 25.363 1.00 18.00 O ATOM 195 CB ILE A 27 -8.889 15.591 27.208 1.00 21.08 C ATOM 196 CG1 ILE A 27 -9.708 14.383 27.627 1.00 22.99 C ATOM 197 CG2 ILE A 27 -9.439 16.838 27.886 1.00 22.46 C ATOM 198 CD1 ILE A 27 -10.872 14.110 26.725 1.00 24.63 C ATOM 199 N PHE A 28 -9.128 18.072 24.914 1.00 17.11 N ATOM 200 CA PHE A 28 -8.628 19.436 24.670 1.00 16.06 C ATOM 201 C PHE A 28 -8.984 20.295 25.872 1.00 15.15 C ATOM 202 O PHE A 28 -10.153 20.459 26.195 1.00 15.06 O ATOM 203 CB PHE A 28 -9.197 20.098 23.398 1.00 16.23 C ATOM 204 CG PHE A 28 -8.808 21.575 23.250 1.00 14.60 C ATOM 205 CD1 PHE A 28 -7.484 21.945 23.106 1.00 13.38 C ATOM 206 CD2 PHE A 28 -9.759 22.575 23.323 1.00 14.14 C ATOM 207 CE1 PHE A 28 -7.119 23.257 23.046 1.00 13.86 C ATOM 208 CE2 PHE A 28 -9.389 23.912 23.262 1.00 14.82 C ATOM 209 CZ PHE A 28 -8.072 24.253 23.126 1.00 13.52 C ATOM 210 N VAL A 29 -7.975 20.842 26.531 1.00 14.18 N ATOM 211 CA VAL A 29 -8.197 21.673 27.687 1.00 15.17 C ATOM 212 C VAL A 29 -8.410 23.095 27.210 1.00 14.96 C ATOM 213 O VAL A 29 -7.489 23.756 26.749 1.00 14.65 O ATOM 214 CB VAL A 29 -7.009 21.580 28.660 1.00 16.06 C ATOM 215 CG1 VAL A 29 -7.264 22.385 29.917 1.00 15.35 C ATOM 216 CG2 VAL A 29 -6.809 20.132 29.059 1.00 16.44 C ATOM 217 N ASP A 30 -9.656 23.531 27.277 1.00 15.08 N ATOM 218 CA ASP A 30 -10.032 24.865 26.861 1.00 17.19 C ATOM 219 C ASP A 30 -9.730 25.959 27.886 1.00 16.67 C ATOM 220 O ASP A 30 -9.453 27.097 27.514 1.00 16.89 O ATOM 221 CB ASP A 30 -11.521 24.896 26.486 1.00 20.36 C ATOM 222 CG ASP A 30 -12.430 24.416 27.619 1.00 23.89 C ATOM 223 OD1 ASP A 30 -12.111 23.409 28.269 1.00 25.66 O ATOM 224 OD2 ASP A 30 -13.487 25.047 27.875 1.00 28.46 O ATOM 225 N GLU A 31 -9.785 25.622 29.167 1.00 15.74 N ATOM 226 CA GLU A 31 -9.536 26.587 30.219 1.00 15.60 C ATOM 227 C GLU A 31 -8.053 26.833 30.417 1.00 14.29 C ATOM 228 O GLU A 31 -7.218 26.008 30.059 1.00 13.77 O ATOM 229 CB GLU A 31 -10.168 26.125 31.541 1.00 17.38 C ATOM 230 CG GLU A 31 -9.477 24.931 32.231 1.00 21.46 C ATOM 231 CD GLU A 31 -10.069 23.596 31.870 1.00 23.85 C ATOM 232 OE1 GLU A 31 -10.762 23.496 30.851 1.00 24.88 O ATOM 233 OE2 GLU A 31 -9.854 22.624 32.611 1.00 26.61 O ATOM 234 N TYR A 32 -7.744 27.979 31.000 1.00 13.70 N ATOM 235 CA TYR A 32 -6.383 28.366 31.281 1.00 13.70 C ATOM 236 C TYR A 32 -6.190 28.162 32.773 1.00 14.37 C ATOM 237 O TYR A 32 -6.550 29.006 33.593 1.00 14.09 O ATOM 238 CB TYR A 32 -6.199 29.833 30.912 1.00 15.41 C ATOM 239 CG TYR A 32 -4.787 30.370 30.981 1.00 16.67 C ATOM 240 CD1 TYR A 32 -3.751 29.635 31.543 1.00 17.03 C ATOM 241 CD2 TYR A 32 -4.512 31.662 30.536 1.00 19.00 C ATOM 242 CE1 TYR A 32 -2.479 30.176 31.673 1.00 18.56 C ATOM 243 CE2 TYR A 32 -3.256 32.207 30.659 1.00 19.49 C ATOM 244 CZ TYR A 32 -2.254 31.479 31.226 1.00 19.38 C ATOM 245 OH TYR A 32 -1.037 32.088 31.373 1.00 20.32 O ATOM 246 N ASP A 33 -5.600 27.032 33.120 1.00 13.48 N ATOM 247 CA ASP A 33 -5.374 26.687 34.505 1.00 13.77 C ATOM 248 C ASP A 33 -3.869 26.539 34.675 1.00 12.50 C ATOM 249 O ASP A 33 -3.310 25.475 34.391 1.00 11.92 O ATOM 250 CB ASP A 33 -6.098 25.372 34.768 1.00 18.02 C ATOM 251 CG ASP A 33 -6.137 25.001 36.215 1.00 21.79 C ATOM 252 OD1 ASP A 33 -5.880 25.854 37.090 1.00 24.59 O ATOM 253 OD2 ASP A 33 -6.458 23.834 36.485 1.00 24.42 O ATOM 254 N PRO A 34 -3.190 27.605 35.141 1.00 11.68 N ATOM 255 CA PRO A 34 -1.741 27.549 35.319 1.00 11.55 C ATOM 256 C PRO A 34 -1.214 26.337 36.085 1.00 11.40 C ATOM 257 O PRO A 34 -1.720 25.975 37.146 1.00 11.99 O ATOM 258 CB PRO A 34 -1.431 28.868 36.008 1.00 10.35 C ATOM 259 CG PRO A 34 -2.445 29.768 35.431 1.00 12.24 C ATOM 260 CD PRO A 34 -3.693 28.933 35.514 1.00 11.14 C ATOM 261 N THR A 35 -0.195 25.708 35.514 1.00 10.49 N ATOM 262 CA THR A 35 0.429 24.539 36.089 1.00 9.71 C ATOM 263 C THR A 35 1.306 24.920 37.254 1.00 9.39 C ATOM 264 O THR A 35 1.918 25.975 37.270 1.00 8.77 O ATOM 265 CB THR A 35 1.319 23.841 35.040 1.00 9.58 C ATOM 266 OG1 THR A 35 0.514 23.399 33.951 1.00 9.88 O ATOM 267 CG2 THR A 35 2.046 22.649 35.613 1.00 9.00 C ATOM 268 N ILE A 36 1.362 24.024 38.225 1.00 9.45 N ATOM 269 CA ILE A 36 2.211 24.178 39.372 1.00 10.25 C ATOM 270 C ILE A 36 3.258 23.087 39.228 1.00 11.30 C ATOM 271 O ILE A 36 4.441 23.375 39.166 1.00 12.48 O ATOM 272 CB ILE A 36 1.445 23.980 40.678 1.00 11.71 C ATOM 273 CG1 ILE A 36 0.333 25.014 40.773 1.00 12.88 C ATOM 274 CG2 ILE A 36 2.396 24.076 41.864 1.00 10.95 C ATOM 275 CD1 ILE A 36 -0.518 24.863 41.980 1.00 16.33 C ATOM 276 N GLU A 37 2.819 21.841 39.084 1.00 11.38 N ATOM 277 CA GLU A 37 3.733 20.714 38.962 1.00 11.83 C ATOM 278 C GLU A 37 2.901 19.532 38.470 1.00 9.82 C ATOM 279 O GLU A 37 1.910 19.192 39.072 1.00 8.90 O ATOM 280 CB GLU A 37 4.391 20.428 40.339 1.00 13.66 C ATOM 281 CG GLU A 37 5.298 19.169 40.448 1.00 17.12 C ATOM 282 CD GLU A 37 5.906 18.982 41.847 1.00 18.63 C ATOM 283 OE1 GLU A 37 6.385 19.979 42.422 1.00 19.78 O ATOM 284 OE2 GLU A 37 5.903 17.843 42.380 1.00 18.87 O ATOM 285 N ASP A 38 3.286 18.942 37.347 1.00 9.62 N ATOM 286 CA ASP A 38 2.550 17.823 36.768 1.00 10.16 C ATOM 287 C ASP A 38 3.430 16.891 35.948 1.00 10.49 C ATOM 288 O ASP A 38 4.254 17.342 35.172 1.00 12.74 O ATOM 289 CB ASP A 38 1.445 18.344 35.847 1.00 9.03 C ATOM 290 CG ASP A 38 0.153 18.628 36.572 1.00 10.51 C ATOM 291 OD1 ASP A 38 -0.446 17.684 37.097 1.00 10.78 O ATOM 292 OD2 ASP A 38 -0.305 19.786 36.597 1.00 10.27 O ATOM 293 N SER A 39 3.309 15.592 36.152 1.00 10.69 N ATOM 294 CA SER A 39 4.067 14.673 35.331 1.00 10.45 C ATOM 295 C SER A 39 3.113 13.587 34.858 1.00 10.62 C ATOM 296 O SER A 39 2.158 13.231 35.547 1.00 10.40 O ATOM 297 CB SER A 39 5.308 14.134 36.035 1.00 11.20 C ATOM 298 OG SER A 39 4.989 13.101 36.932 1.00 14.10 O ATOM 299 N TYR A 40 3.292 13.185 33.603 1.00 10.89 N ATOM 300 CA TYR A 40 2.450 12.191 32.971 1.00 10.10 C ATOM 301 C TYR A 40 3.328 11.069 32.470 1.00 11.16 C ATOM 302 O TYR A 40 4.519 11.260 32.231 1.00 11.09 O ATOM 303 CB TYR A 40 1.732 12.815 31.772 1.00 9.99 C ATOM 304 CG TYR A 40 0.857 13.986 32.093 1.00 9.65 C ATOM 305 CD1 TYR A 40 1.393 15.258 32.262 1.00 9.89 C ATOM 306 CD2 TYR A 40 -0.505 13.818 32.257 1.00 10.11 C ATOM 307 CE1 TYR A 40 0.591 16.336 32.601 1.00 9.65 C ATOM 308 CE2 TYR A 40 -1.315 14.872 32.585 1.00 11.50 C ATOM 309 CZ TYR A 40 -0.761 16.138 32.764 1.00 10.88 C ATOM 310 OH TYR A 40 -1.573 17.170 33.138 1.00 10.17 O ATOM 311 N ARG A 41 2.756 9.883 32.370 1.00 12.26 N ATOM 312 CA ARG A 41 3.472 8.716 31.857 1.00 13.98 C ATOM 313 C ARG A 41 2.478 7.949 31.029 1.00 14.89 C ATOM 314 O ARG A 41 1.331 7.802 31.432 1.00 16.44 O ATOM 315 CB ARG A 41 4.005 7.808 32.962 1.00 14.12 C ATOM 316 CG ARG A 41 5.181 8.342 33.702 1.00 15.60 C ATOM 317 CD ARG A 41 6.238 7.281 33.874 1.00 18.02 C ATOM 318 NE ARG A 41 5.717 6.028 34.419 1.00 18.62 N ATOM 319 CZ ARG A 41 6.403 4.890 34.444 1.00 18.57 C ATOM 320 NH1 ARG A 41 7.631 4.846 33.954 1.00 18.92 N ATOM 321 NH2 ARG A 41 5.880 3.802 34.988 1.00 18.26 N ATOM 322 N LYS A 42 2.901 7.478 29.865 1.00 15.37 N ATOM 323 CA LYS A 42 2.011 6.723 29.007 1.00 16.60 C ATOM 324 C LYS A 42 2.810 5.745 28.157 1.00 17.56 C ATOM 325 O LYS A 42 3.881 6.087 27.648 1.00 16.36 O ATOM 326 CB LYS A 42 1.218 7.645 28.091 1.00 17.20 C ATOM 327 CG LYS A 42 0.112 6.916 27.401 1.00 18.72 C ATOM 328 CD LYS A 42 -0.563 7.735 26.367 1.00 21.40 C ATOM 329 CE LYS A 42 -1.870 7.085 25.961 1.00 22.89 C ATOM 330 NZ LYS A 42 -2.802 6.965 27.142 1.00 26.61 N ATOM 331 N GLN A 43 2.293 4.519 28.054 1.00 18.70 N ATOM 332 CA GLN A 43 2.900 3.442 27.266 1.00 19.68 C ATOM 333 C GLN A 43 2.414 3.718 25.863 1.00 20.35 C ATOM 334 O GLN A 43 1.211 3.812 25.641 1.00 20.56 O ATOM 335 CB GLN A 43 2.356 2.079 27.742 1.00 20.38 C ATOM 336 CG GLN A 43 3.076 0.840 27.194 1.00 21.11 C ATOM 337 CD GLN A 43 2.211 -0.011 26.285 1.00 21.19 C ATOM 338 OE1 GLN A 43 1.418 -0.812 26.750 1.00 19.61 O ATOM 339 NE2 GLN A 43 2.364 0.159 24.981 1.00 22.34 N ATOM 340 N VAL A 44 3.343 3.898 24.929 1.00 21.25 N ATOM 341 CA VAL A 44 2.997 4.179 23.551 1.00 21.96 C ATOM 342 C VAL A 44 3.742 3.222 22.639 1.00 22.49 C ATOM 343 O VAL A 44 4.488 2.346 23.093 1.00 21.70 O ATOM 344 CB VAL A 44 3.368 5.648 23.115 1.00 22.00 C ATOM 345 CG1 VAL A 44 2.486 6.645 23.817 1.00 22.74 C ATOM 346 CG2 VAL A 44 4.838 5.952 23.407 1.00 21.55 C ATOM 347 N GLU A 45 3.492 3.381 21.348 1.00 23.43 N ATOM 348 CA GLU A 45 4.128 2.580 20.334 1.00 24.97 C ATOM 349 C GLU A 45 4.763 3.571 19.380 1.00 24.68 C ATOM 350 O GLU A 45 4.074 4.405 18.802 1.00 24.64 O ATOM 351 CB GLU A 45 3.074 1.755 19.593 1.00 27.07 C ATOM 352 CG GLU A 45 3.467 0.306 19.358 1.00 31.81 C ATOM 353 CD GLU A 45 2.695 -0.316 18.215 1.00 33.94 C ATOM 354 OE1 GLU A 45 1.520 -0.725 18.435 1.00 34.79 O ATOM 355 OE2 GLU A 45 3.261 -0.368 17.086 1.00 35.82 O ATOM 356 N VAL A 46 6.082 3.557 19.284 1.00 24.92 N ATOM 357 CA VAL A 46 6.764 4.459 18.372 1.00 25.47 C ATOM 358 C VAL A 46 7.595 3.583 17.458 1.00 25.92 C ATOM 359 O VAL A 46 8.449 2.835 17.938 1.00 25.65 O ATOM 360 CB VAL A 46 7.709 5.462 19.106 1.00 25.32 C ATOM 361 CG1 VAL A 46 8.463 6.289 18.092 1.00 25.78 C ATOM 362 CG2 VAL A 46 6.910 6.408 19.978 1.00 25.35 C ATOM 363 N ASP A 47 7.278 3.612 16.158 1.00 27.59 N ATOM 364 CA ASP A 47 7.997 2.834 15.136 1.00 27.68 C ATOM 365 C ASP A 47 8.019 1.353 15.428 1.00 28.21 C ATOM 366 O ASP A 47 9.101 0.743 15.468 1.00 27.64 O ATOM 367 CB ASP A 47 9.439 3.318 15.020 1.00 28.26 C ATOM 368 CG ASP A 47 9.534 4.730 14.525 1.00 28.96 C ATOM 369 OD1 ASP A 47 8.493 5.343 14.211 1.00 28.45 O ATOM 370 OD2 ASP A 47 10.671 5.232 14.455 1.00 30.22 O ATOM 371 N CYS A 48 6.832 0.797 15.686 1.00 30.04 N ATOM 372 CA CYS A 48 6.650 -0.635 15.975 1.00 32.02 C ATOM 373 C CYS A 48 7.222 -1.066 17.327 1.00 31.71 C ATOM 374 O CYS A 48 7.406 -2.258 17.590 1.00 32.21 O ATOM 375 CB CYS A 48 7.288 -1.493 14.863 1.00 33.77 C ATOM 376 SG CYS A 48 6.884 -0.942 13.164 1.00 38.41 S ATOM 377 N GLN A 49 7.463 -0.116 18.218 1.00 31.07 N ATOM 378 CA GLN A 49 8.028 -0.480 19.501 1.00 29.71 C ATOM 379 C GLN A 49 7.217 0.128 20.614 1.00 27.15 C ATOM 380 O GLN A 49 6.778 1.277 20.512 1.00 25.59 O ATOM 381 CB GLN A 49 9.470 -0.004 19.566 1.00 33.20 C ATOM 382 CG GLN A 49 10.327 -0.833 20.477 1.00 38.52 C ATOM 383 CD GLN A 49 11.724 -1.020 19.931 1.00 41.97 C ATOM 384 OE1 GLN A 49 11.923 -1.730 18.923 1.00 43.53 O ATOM 385 NE2 GLN A 49 12.718 -0.404 20.598 1.00 44.01 N ATOM 386 N GLN A 50 6.922 -0.698 21.619 1.00 24.32 N ATOM 387 CA GLN A 50 6.165 -0.279 22.788 1.00 22.23 C ATOM 388 C GLN A 50 7.154 0.332 23.746 1.00 21.95 C ATOM 389 O GLN A 50 8.177 -0.293 24.061 1.00 21.54 O ATOM 390 CB GLN A 50 5.508 -1.479 23.462 1.00 20.71 C ATOM 391 CG GLN A 50 4.490 -2.166 22.585 1.00 19.32 C ATOM 392 CD GLN A 50 3.719 -3.215 23.329 1.00 17.15 C ATOM 393 OE1 GLN A 50 4.301 -4.033 24.028 1.00 16.65 O ATOM 394 NE2 GLN A 50 2.404 -3.190 23.201 1.00 14.99 N ATOM 395 N CYS A 51 6.909 1.573 24.158 1.00 20.80 N ATOM 396 CA CYS A 51 7.808 2.205 25.105 1.00 20.75 C ATOM 397 C CYS A 51 7.110 3.071 26.119 1.00 18.51 C ATOM 398 O CYS A 51 5.949 3.420 25.961 1.00 17.55 O ATOM 399 CB CYS A 51 8.926 2.958 24.409 1.00 22.51 C ATOM 400 SG CYS A 51 8.390 3.916 23.038 1.00 28.68 S ATOM 401 N MET A 52 7.811 3.347 27.202 1.00 17.17 N ATOM 402 CA MET A 52 7.264 4.145 28.271 1.00 17.34 C ATOM 403 C MET A 52 7.715 5.600 28.181 1.00 16.47 C ATOM 404 O MET A 52 8.910 5.884 28.158 1.00 15.58 O ATOM 405 CB MET A 52 7.701 3.558 29.597 1.00 17.93 C ATOM 406 CG MET A 52 6.751 3.845 30.706 1.00 21.63 C ATOM 407 SD MET A 52 5.164 3.057 30.453 1.00 27.18 S ATOM 408 CE MET A 52 4.270 4.440 30.761 1.00 20.65 C ATOM 409 N LEU A 53 6.767 6.520 28.095 1.00 15.28 N ATOM 410 CA LEU A 53 7.139 7.918 28.038 1.00 15.78 C ATOM 411 C LEU A 53 6.813 8.666 29.321 1.00 15.22 C ATOM 412 O LEU A 53 5.694 8.590 29.826 1.00 14.57 O ATOM 413 CB LEU A 53 6.456 8.619 26.862 1.00 17.03 C ATOM 414 CG LEU A 53 7.273 8.890 25.599 1.00 18.86 C ATOM 415 CD1 LEU A 53 7.939 7.633 25.087 1.00 19.44 C ATOM 416 CD2 LEU A 53 6.356 9.478 24.560 1.00 19.77 C ATOM 417 N GLU A 54 7.805 9.344 29.874 1.00 14.41 N ATOM 418 CA GLU A 54 7.572 10.162 31.035 1.00 15.30 C ATOM 419 C GLU A 54 7.609 11.607 30.536 1.00 13.85 C ATOM 420 O GLU A 54 8.580 12.020 29.922 1.00 14.41 O ATOM 421 CB GLU A 54 8.665 9.961 32.059 1.00 17.82 C ATOM 422 CG GLU A 54 8.426 10.766 33.310 1.00 23.45 C ATOM 423 CD GLU A 54 9.263 10.297 34.465 1.00 26.01 C ATOM 424 OE1 GLU A 54 9.785 9.163 34.428 1.00 28.34 O ATOM 425 OE2 GLU A 54 9.394 11.056 35.430 1.00 28.45 O ATOM 426 N ILE A 55 6.553 12.365 30.791 1.00 12.99 N ATOM 427 CA ILE A 55 6.490 13.751 30.353 1.00 12.01 C ATOM 428 C ILE A 55 6.307 14.720 31.521 1.00 11.35 C ATOM 429 O ILE A 55 5.264 14.727 32.165 1.00 10.87 O ATOM 430 CB ILE A 55 5.344 13.971 29.349 1.00 12.18 C ATOM 431 CG1 ILE A 55 5.447 12.975 28.193 1.00 12.30 C ATOM 432 CG2 ILE A 55 5.392 15.389 28.824 1.00 11.50 C ATOM 433 CD1 ILE A 55 4.270 12.990 27.254 1.00 13.63 C ATOM 434 N LEU A 56 7.347 15.488 31.818 1.00 10.38 N ATOM 435 CA LEU A 56 7.289 16.486 32.875 1.00 10.43 C ATOM 436 C LEU A 56 6.789 17.779 32.238 1.00 10.64 C ATOM 437 O LEU A 56 7.402 18.289 31.311 1.00 10.39 O ATOM 438 CB LEU A 56 8.668 16.701 33.508 1.00 9.81 C ATOM 439 CG LEU A 56 8.830 17.713 34.654 1.00 12.95 C ATOM 440 CD1 LEU A 56 7.997 17.380 35.884 1.00 13.59 C ATOM 441 CD2 LEU A 56 10.275 17.753 35.036 1.00 12.80 C ATOM 442 N ASP A 57 5.648 18.263 32.715 1.00 10.69 N ATOM 443 CA ASP A 57 5.000 19.474 32.235 1.00 11.28 C ATOM 444 C ASP A 57 5.372 20.546 33.252 1.00 11.58 C ATOM 445 O ASP A 57 5.039 20.440 34.426 1.00 14.71 O ATOM 446 CB ASP A 57 3.486 19.217 32.213 1.00 10.09 C ATOM 447 CG ASP A 57 2.677 20.376 31.669 1.00 10.42 C ATOM 448 OD1 ASP A 57 3.251 21.302 31.062 1.00 9.67 O ATOM 449 OD2 ASP A 57 1.440 20.341 31.863 1.00 9.76 O ATOM 450 N THR A 58 6.089 21.565 32.822 1.00 11.75 N ATOM 451 CA THR A 58 6.536 22.599 33.735 1.00 11.07 C ATOM 452 C THR A 58 5.649 23.826 33.860 1.00 11.06 C ATOM 453 O THR A 58 4.771 24.055 33.049 1.00 10.68 O ATOM 454 CB THR A 58 7.928 23.025 33.377 1.00 10.34 C ATOM 455 OG1 THR A 58 7.923 23.545 32.044 1.00 11.93 O ATOM 456 CG2 THR A 58 8.872 21.849 33.447 1.00 10.87 C ATOM 457 N ALA A 59 5.833 24.568 34.943 1.00 11.57 N ATOM 458 CA ALA A 59 5.080 25.783 35.216 1.00 12.19 C ATOM 459 C ALA A 59 5.705 26.946 34.452 1.00 13.82 C ATOM 460 O ALA A 59 6.861 27.277 34.671 1.00 15.54 O ATOM 461 CB ALA A 59 5.108 26.077 36.698 1.00 11.27 C ATOM 462 N GLY A 60 4.948 27.564 33.558 1.00 14.22 N ATOM 463 CA GLY A 60 5.490 28.665 32.797 1.00 15.53 C ATOM 464 C GLY A 60 5.552 29.909 33.640 1.00 17.29 C ATOM 465 O GLY A 60 6.307 30.831 33.355 1.00 17.44 O ATOM 466 N THR A 61 4.790 29.914 34.715 1.00 18.39 N ATOM 467 CA THR A 61 4.740 31.066 35.591 1.00 21.37 C ATOM 468 C THR A 61 5.007 30.675 37.024 1.00 22.13 C ATOM 469 O THR A 61 4.073 30.380 37.755 1.00 24.31 O ATOM 470 CB THR A 61 3.346 31.688 35.534 1.00 21.71 C ATOM 471 OG1 THR A 61 2.994 31.961 34.165 1.00 22.94 O ATOM 472 CG2 THR A 61 3.317 32.958 36.305 1.00 23.56 C ATOM 473 N GLU A 62 6.256 30.668 37.445 1.00 23.82 N ATOM 474 CA GLU A 62 6.555 30.311 38.830 1.00 25.92 C ATOM 475 C GLU A 62 7.550 31.265 39.465 1.00 25.90 C ATOM 476 O GLU A 62 8.348 31.883 38.788 1.00 25.38 O ATOM 477 CB GLU A 62 7.042 28.870 38.955 1.00 26.23 C ATOM 478 CG GLU A 62 8.290 28.556 38.170 1.00 29.51 C ATOM 479 CD GLU A 62 8.706 27.103 38.302 1.00 30.89 C ATOM 480 OE1 GLU A 62 8.306 26.431 39.281 1.00 32.54 O ATOM 481 OE2 GLU A 62 9.435 26.618 37.426 1.00 33.25 O ATOM 482 N GLN A 63 7.506 31.357 40.784 1.00 26.96 N ATOM 483 CA GLN A 63 8.376 32.277 41.494 1.00 27.48 C ATOM 484 C GLN A 63 9.768 31.768 41.746 1.00 26.12 C ATOM 485 O GLN A 63 10.722 32.547 41.786 1.00 25.33 O ATOM 486 CB GLN A 63 7.752 32.674 42.830 1.00 30.34 C ATOM 487 CG GLN A 63 8.402 33.932 43.408 1.00 34.69 C ATOM 488 CD GLN A 63 8.172 34.101 44.882 1.00 36.54 C ATOM 489 OE1 GLN A 63 8.955 34.801 45.564 1.00 38.09 O ATOM 490 NE2 GLN A 63 7.102 33.481 45.406 1.00 36.86 N ATOM 491 N PHE A 64 9.881 30.467 41.989 1.00 24.08 N ATOM 492 CA PHE A 64 11.172 29.870 42.269 1.00 22.38 C ATOM 493 C PHE A 64 11.499 28.937 41.113 1.00 21.73 C ATOM 494 O PHE A 64 10.749 28.032 40.807 1.00 21.93 O ATOM 495 CB PHE A 64 11.108 29.148 43.615 1.00 21.87 C ATOM 496 CG PHE A 64 10.726 30.054 44.768 1.00 21.36 C ATOM 497 CD1 PHE A 64 11.412 31.244 44.995 1.00 21.15 C ATOM 498 CD2 PHE A 64 9.661 29.741 45.594 1.00 21.72 C ATOM 499 CE1 PHE A 64 11.045 32.102 46.024 1.00 20.62 C ATOM 500 CE2 PHE A 64 9.277 30.593 46.638 1.00 20.47 C ATOM 501 CZ PHE A 64 9.969 31.770 46.849 1.00 20.94 C ATOM 502 N THR A 65 12.613 29.197 40.451 1.00 20.79 N ATOM 503 CA THR A 65 13.040 28.438 39.298 1.00 20.63 C ATOM 504 C THR A 65 14.280 27.600 39.540 1.00 19.87 C ATOM 505 O THR A 65 14.866 27.092 38.590 1.00 19.69 O ATOM 506 CB THR A 65 13.368 29.400 38.152 1.00 22.18 C ATOM 507 OG1 THR A 65 14.138 30.493 38.680 1.00 23.05 O ATOM 508 CG2 THR A 65 12.102 29.926 37.491 1.00 21.45 C ATOM 509 N ALA A 66 14.687 27.465 40.793 1.00 18.50 N ATOM 510 CA ALA A 66 15.856 26.676 41.147 1.00 18.02 C ATOM 511 C ALA A 66 15.796 25.208 40.659 1.00 17.72 C ATOM 512 O ALA A 66 16.822 24.619 40.332 1.00 17.74 O ATOM 513 CB ALA A 66 16.033 26.708 42.649 1.00 17.00 C ATOM 514 N MET A 67 14.598 24.635 40.620 1.00 17.92 N ATOM 515 CA MET A 67 14.400 23.251 40.192 1.00 18.55 C ATOM 516 C MET A 67 14.541 23.002 38.700 1.00 19.45 C ATOM 517 O MET A 67 14.776 21.871 38.302 1.00 18.90 O ATOM 518 CB MET A 67 13.040 22.710 40.656 1.00 18.06 C ATOM 519 CG MET A 67 12.938 22.380 42.142 1.00 18.37 C ATOM 520 SD MET A 67 14.276 21.370 42.797 1.00 21.73 S ATOM 521 CE MET A 67 13.781 19.805 42.241 1.00 15.81 C ATOM 522 N ARG A 68 14.432 24.048 37.879 1.00 20.19 N ATOM 523 CA ARG A 68 14.541 23.921 36.427 1.00 21.34 C ATOM 524 C ARG A 68 15.850 23.295 36.012 1.00 20.45 C ATOM 525 O ARG A 68 15.909 22.477 35.083 1.00 19.55 O ATOM 526 CB ARG A 68 14.397 25.286 35.764 1.00 24.22 C ATOM 527 CG ARG A 68 13.669 25.213 34.444 1.00 28.61 C ATOM 528 CD ARG A 68 13.036 26.558 34.154 1.00 32.08 C ATOM 529 NE ARG A 68 14.077 27.581 34.054 1.00 35.04 N ATOM 530 CZ ARG A 68 13.880 28.809 33.593 1.00 36.77 C ATOM 531 NH1 ARG A 68 12.665 29.195 33.194 1.00 37.49 N ATOM 532 NH2 ARG A 68 14.922 29.614 33.434 1.00 37.57 N ATOM 533 N ASP A 69 16.910 23.688 36.695 1.00 19.94 N ATOM 534 CA ASP A 69 18.223 23.134 36.432 1.00 20.55 C ATOM 535 C ASP A 69 18.224 21.616 36.634 1.00 19.68 C ATOM 536 O ASP A 69 18.927 20.901 35.919 1.00 18.98 O ATOM 537 CB ASP A 69 19.246 23.752 37.391 1.00 23.60 C ATOM 538 CG ASP A 69 20.142 24.751 36.734 1.00 25.51 C ATOM 539 OD1 ASP A 69 19.699 25.446 35.810 1.00 28.56 O ATOM 540 OD2 ASP A 69 21.307 24.844 37.149 1.00 29.42 O ATOM 541 N LEU A 70 17.480 21.139 37.637 1.00 18.49 N ATOM 542 CA LEU A 70 17.411 19.706 37.966 1.00 17.90 C ATOM 543 C LEU A 70 16.533 18.940 36.993 1.00 17.41 C ATOM 544 O LEU A 70 16.808 17.781 36.676 1.00 17.74 O ATOM 545 CB LEU A 70 16.932 19.489 39.411 1.00 18.34 C ATOM 546 CG LEU A 70 17.957 19.475 40.550 1.00 18.82 C ATOM 547 CD1 LEU A 70 19.371 19.478 40.021 1.00 20.10 C ATOM 548 CD2 LEU A 70 17.745 20.622 41.455 1.00 19.39 C ATOM 549 N TYR A 71 15.469 19.584 36.532 1.00 17.30 N ATOM 550 CA TYR A 71 14.596 18.986 35.544 1.00 17.62 C ATOM 551 C TYR A 71 15.378 18.803 34.242 1.00 17.59 C ATOM 552 O TYR A 71 15.214 17.809 33.534 1.00 17.30 O ATOM 553 CB TYR A 71 13.392 19.890 35.320 1.00 19.61 C ATOM 554 CG TYR A 71 12.509 19.946 36.525 1.00 22.40 C ATOM 555 CD1 TYR A 71 12.590 18.949 37.481 1.00 23.87 C ATOM 556 CD2 TYR A 71 11.600 20.981 36.722 1.00 23.75 C ATOM 557 CE1 TYR A 71 11.797 18.962 38.621 1.00 26.24 C ATOM 558 CE2 TYR A 71 10.775 21.004 37.874 1.00 25.50 C ATOM 559 CZ TYR A 71 10.899 19.978 38.814 1.00 27.02 C ATOM 560 OH TYR A 71 10.152 19.924 39.973 1.00 28.38 O ATOM 561 N MET A 72 16.251 19.751 33.936 1.00 17.25 N ATOM 562 CA MET A 72 17.047 19.663 32.726 1.00 18.03 C ATOM 563 C MET A 72 18.136 18.628 32.849 1.00 19.56 C ATOM 564 O MET A 72 18.518 18.013 31.875 1.00 20.12 O ATOM 565 CB MET A 72 17.655 21.010 32.409 1.00 16.83 C ATOM 566 CG MET A 72 16.629 22.035 32.024 1.00 15.52 C ATOM 567 SD MET A 72 17.318 23.671 31.952 1.00 16.96 S ATOM 568 CE MET A 72 15.883 24.557 31.574 1.00 13.84 C ATOM 569 N LYS A 73 18.673 18.465 34.050 1.00 21.07 N ATOM 570 CA LYS A 73 19.726 17.492 34.300 1.00 22.47 C ATOM 571 C LYS A 73 19.203 16.086 34.051 1.00 22.15 C ATOM 572 O LYS A 73 19.868 15.284 33.391 1.00 22.95 O ATOM 573 CB LYS A 73 20.234 17.666 35.743 1.00 24.15 C ATOM 574 CG LYS A 73 21.147 16.577 36.312 1.00 28.22 C ATOM 575 CD LYS A 73 21.153 16.699 37.858 1.00 31.52 C ATOM 576 CE LYS A 73 21.980 15.630 38.566 1.00 33.48 C ATOM 577 NZ LYS A 73 21.967 15.828 40.082 1.00 35.12 N ATOM 578 N ASN A 74 17.997 15.783 34.529 1.00 22.08 N ATOM 579 CA ASN A 74 17.433 14.434 34.347 1.00 22.14 C ATOM 580 C ASN A 74 16.641 14.124 33.093 1.00 20.17 C ATOM 581 O ASN A 74 16.318 12.971 32.874 1.00 20.25 O ATOM 582 CB ASN A 74 16.563 14.050 35.541 1.00 24.78 C ATOM 583 CG ASN A 74 17.344 13.979 36.826 1.00 26.63 C ATOM 584 OD1 ASN A 74 16.906 14.485 37.845 1.00 28.41 O ATOM 585 ND2 ASN A 74 18.519 13.365 36.785 1.00 29.36 N ATOM 586 N GLY A 75 16.275 15.139 32.314 1.00 18.20 N ATOM 587 CA GLY A 75 15.500 14.911 31.114 1.00 15.92 C ATOM 588 C GLY A 75 16.355 14.484 29.946 1.00 15.40 C ATOM 589 O GLY A 75 17.507 14.895 29.836 1.00 14.10 O ATOM 590 N GLN A 76 15.797 13.663 29.065 1.00 14.51 N ATOM 591 CA GLN A 76 16.543 13.186 27.912 1.00 14.28 C ATOM 592 C GLN A 76 16.248 13.991 26.651 1.00 13.94 C ATOM 593 O GLN A 76 17.123 14.163 25.829 1.00 14.38 O ATOM 594 CB GLN A 76 16.242 11.720 27.648 1.00 14.21 C ATOM 595 CG GLN A 76 16.681 10.782 28.729 1.00 15.74 C ATOM 596 CD GLN A 76 16.128 9.402 28.501 1.00 17.53 C ATOM 597 OE1 GLN A 76 15.022 9.109 28.903 1.00 18.62 O ATOM 598 NE2 GLN A 76 16.876 8.562 27.799 1.00 19.87 N ATOM 599 N GLY A 77 15.018 14.476 26.520 1.00 12.76 N ATOM 600 CA GLY A 77 14.610 15.248 25.362 1.00 12.26 C ATOM 601 C GLY A 77 13.766 16.432 25.795 1.00 11.91 C ATOM 602 O GLY A 77 12.983 16.320 26.740 1.00 11.24 O ATOM 603 N PHE A 78 13.888 17.552 25.090 1.00 11.73 N ATOM 604 CA PHE A 78 13.172 18.766 25.448 1.00 11.17 C ATOM 605 C PHE A 78 12.326 19.369 24.361 1.00 10.99 C ATOM 606 O PHE A 78 12.760 19.458 23.228 1.00 11.09 O ATOM 607 CB PHE A 78 14.175 19.827 25.899 1.00 9.90 C ATOM 608 CG PHE A 78 15.097 19.349 26.962 1.00 10.80 C ATOM 609 CD1 PHE A 78 16.262 18.669 26.628 1.00 10.30 C ATOM 610 CD2 PHE A 78 14.747 19.466 28.299 1.00 11.05 C ATOM 611 CE1 PHE A 78 17.050 18.105 27.598 1.00 10.77 C ATOM 612 CE2 PHE A 78 15.538 18.902 29.278 1.00 11.49 C ATOM 613 CZ PHE A 78 16.692 18.217 28.923 1.00 10.14 C ATOM 614 N ALA A 79 11.104 19.742 24.707 1.00 10.74 N ATOM 615 CA ALA A 79 10.196 20.412 23.789 1.00 11.34 C ATOM 616 C ALA A 79 10.084 21.876 24.273 1.00 11.57 C ATOM 617 O ALA A 79 9.621 22.117 25.381 1.00 11.26 O ATOM 618 CB ALA A 79 8.828 19.743 23.821 1.00 11.84 C ATOM 619 N LEU A 80 10.587 22.827 23.487 1.00 11.50 N ATOM 620 CA LEU A 80 10.531 24.254 23.823 1.00 11.51 C ATOM 621 C LEU A 80 9.368 24.824 23.056 1.00 10.16 C ATOM 622 O LEU A 80 9.408 24.919 21.842 1.00 9.72 O ATOM 623 CB LEU A 80 11.818 24.958 23.419 1.00 13.35 C ATOM 624 CG LEU A 80 13.026 24.812 24.347 1.00 15.30 C ATOM 625 CD1 LEU A 80 13.311 23.360 24.637 1.00 16.66 C ATOM 626 CD2 LEU A 80 14.230 25.451 23.678 1.00 17.11 C ATOM 627 N VAL A 81 8.319 25.185 23.768 1.00 9.65 N ATOM 628 CA VAL A 81 7.109 25.677 23.145 1.00 9.15 C ATOM 629 C VAL A 81 6.831 27.174 23.299 1.00 9.81 C ATOM 630 O VAL A 81 7.023 27.737 24.367 1.00 10.14 O ATOM 631 CB VAL A 81 5.905 24.915 23.722 1.00 9.37 C ATOM 632 CG1 VAL A 81 4.623 25.262 22.971 1.00 8.34 C ATOM 633 CG2 VAL A 81 6.187 23.408 23.688 1.00 9.77 C ATOM 634 N TYR A 82 6.416 27.811 22.206 1.00 10.23 N ATOM 635 CA TYR A 82 6.016 29.215 22.217 1.00 9.50 C ATOM 636 C TYR A 82 4.673 29.261 21.506 1.00 9.68 C ATOM 637 O TYR A 82 4.229 28.269 20.941 1.00 9.69 O ATOM 638 CB TYR A 82 7.029 30.141 21.534 1.00 8.69 C ATOM 639 CG TYR A 82 7.204 29.967 20.050 1.00 9.21 C ATOM 640 CD1 TYR A 82 8.110 29.046 19.563 1.00 8.74 C ATOM 641 CD2 TYR A 82 6.472 30.729 19.132 1.00 9.62 C ATOM 642 CE1 TYR A 82 8.293 28.874 18.209 1.00 9.92 C ATOM 643 CE2 TYR A 82 6.651 30.558 17.765 1.00 9.20 C ATOM 644 CZ TYR A 82 7.568 29.616 17.325 1.00 10.19 C ATOM 645 OH TYR A 82 7.760 29.356 16.000 1.00 11.86 O ATOM 646 N SER A 83 4.003 30.392 21.584 1.00 9.01 N ATOM 647 CA SER A 83 2.724 30.555 20.953 1.00 9.05 C ATOM 648 C SER A 83 2.928 31.515 19.794 1.00 10.68 C ATOM 649 O SER A 83 3.621 32.516 19.947 1.00 11.33 O ATOM 650 CB SER A 83 1.773 31.162 21.960 1.00 8.59 C ATOM 651 OG SER A 83 0.576 31.569 21.348 1.00 10.11 O ATOM 652 N ILE A 84 2.354 31.229 18.631 1.00 11.03 N ATOM 653 CA ILE A 84 2.510 32.142 17.490 1.00 11.04 C ATOM 654 C ILE A 84 1.713 33.451 17.639 1.00 10.94 C ATOM 655 O ILE A 84 1.817 34.348 16.803 1.00 10.87 O ATOM 656 CB ILE A 84 2.125 31.492 16.157 1.00 9.86 C ATOM 657 CG1 ILE A 84 0.636 31.166 16.142 1.00 9.38 C ATOM 658 CG2 ILE A 84 3.016 30.302 15.880 1.00 10.64 C ATOM 659 CD1 ILE A 84 0.078 30.933 14.772 1.00 8.67 C ATOM 660 N THR A 85 0.924 33.559 18.700 1.00 11.01 N ATOM 661 CA THR A 85 0.131 34.750 18.936 1.00 10.41 C ATOM 662 C THR A 85 0.750 35.676 19.979 1.00 10.49 C ATOM 663 O THR A 85 0.209 36.726 20.267 1.00 11.24 O ATOM 664 CB THR A 85 -1.296 34.396 19.376 1.00 10.38 C ATOM 665 OG1 THR A 85 -1.266 33.882 20.707 1.00 12.02 O ATOM 666 CG2 THR A 85 -1.918 33.385 18.460 1.00 8.51 C ATOM 667 N ALA A 86 1.914 35.329 20.497 1.00 10.79 N ATOM 668 CA ALA A 86 2.556 36.162 21.494 1.00 12.52 C ATOM 669 C ALA A 86 4.053 36.171 21.289 1.00 13.63 C ATOM 670 O ALA A 86 4.725 35.212 21.643 1.00 13.89 O ATOM 671 CB ALA A 86 2.224 35.662 22.877 1.00 12.93 C ATOM 672 N GLN A 87 4.569 37.287 20.774 1.00 14.21 N ATOM 673 CA GLN A 87 5.992 37.468 20.481 1.00 15.09 C ATOM 674 C GLN A 87 6.910 37.206 21.656 1.00 13.81 C ATOM 675 O GLN A 87 7.928 36.570 21.492 1.00 14.41 O ATOM 676 CB GLN A 87 6.267 38.890 19.958 1.00 17.92 C ATOM 677 CG GLN A 87 5.672 39.189 18.584 1.00 21.73 C ATOM 678 CD GLN A 87 5.380 40.673 18.338 1.00 23.27 C ATOM 679 OE1 GLN A 87 5.370 41.506 19.262 1.00 25.77 O ATOM 680 NE2 GLN A 87 5.107 41.000 17.089 1.00 24.59 N ATOM 681 N SER A 88 6.559 37.695 22.837 1.00 13.51 N ATOM 682 CA SER A 88 7.408 37.509 24.001 1.00 13.80 C ATOM 683 C SER A 88 7.687 36.062 24.346 1.00 12.73 C ATOM 684 O SER A 88 8.773 35.753 24.795 1.00 13.64 O ATOM 685 CB SER A 88 6.862 38.251 25.226 1.00 13.76 C ATOM 686 OG SER A 88 5.660 37.683 25.690 1.00 14.55 O ATOM 687 N THR A 89 6.747 35.165 24.079 1.00 11.68 N ATOM 688 CA THR A 89 6.963 33.756 24.403 1.00 10.89 C ATOM 689 C THR A 89 8.040 33.131 23.533 1.00 11.01 C ATOM 690 O THR A 89 8.785 32.274 23.979 1.00 10.78 O ATOM 691 CB THR A 89 5.666 32.960 24.331 1.00 9.59 C ATOM 692 OG1 THR A 89 5.217 32.874 22.980 1.00 9.19 O ATOM 693 CG2 THR A 89 4.614 33.645 25.155 1.00 9.42 C ATOM 694 N PHE A 90 8.151 33.615 22.302 1.00 12.03 N ATOM 695 CA PHE A 90 9.153 33.159 21.331 1.00 12.55 C ATOM 696 C PHE A 90 10.525 33.717 21.730 1.00 13.89 C ATOM 697 O PHE A 90 11.526 33.008 21.703 1.00 13.27 O ATOM 698 CB PHE A 90 8.730 33.644 19.928 1.00 13.21 C ATOM 699 CG PHE A 90 9.706 33.326 18.841 1.00 13.38 C ATOM 700 CD1 PHE A 90 9.752 32.067 18.278 1.00 14.37 C ATOM 701 CD2 PHE A 90 10.577 34.293 18.372 1.00 14.73 C ATOM 702 CE1 PHE A 90 10.644 31.768 17.270 1.00 13.54 C ATOM 703 CE2 PHE A 90 11.477 33.998 17.360 1.00 13.28 C ATOM 704 CZ PHE A 90 11.505 32.737 16.816 1.00 14.08 C ATOM 705 N ASN A 91 10.547 34.977 22.164 1.00 15.49 N ATOM 706 CA ASN A 91 11.772 35.649 22.587 1.00 17.13 C ATOM 707 C ASN A 91 12.375 35.032 23.835 1.00 17.79 C ATOM 708 O ASN A 91 13.593 35.018 24.006 1.00 18.16 O ATOM 709 CB ASN A 91 11.503 37.127 22.866 1.00 18.57 C ATOM 710 CG ASN A 91 11.251 37.916 21.617 1.00 20.49 C ATOM 711 OD1 ASN A 91 11.562 37.473 20.505 1.00 21.23 O ATOM 712 ND2 ASN A 91 10.667 39.094 21.781 1.00 20.28 N ATOM 713 N ASP A 92 11.511 34.555 24.719 1.00 17.88 N ATOM 714 CA ASP A 92 11.914 33.930 25.969 1.00 17.85 C ATOM 715 C ASP A 92 12.636 32.591 25.807 1.00 18.40 C ATOM 716 O ASP A 92 13.265 32.120 26.748 1.00 17.96 O ATOM 717 CB ASP A 92 10.675 33.645 26.823 1.00 19.42 C ATOM 718 CG ASP A 92 10.067 34.883 27.465 1.00 20.88 C ATOM 719 OD1 ASP A 92 10.735 35.927 27.550 1.00 22.53 O ATOM 720 OD2 ASP A 92 8.904 34.800 27.918 1.00 20.63 O ATOM 721 N LEU A 93 12.553 31.960 24.642 1.00 18.42 N ATOM 722 CA LEU A 93 13.161 30.644 24.477 1.00 19.75 C ATOM 723 C LEU A 93 14.661 30.530 24.369 1.00 21.38 C ATOM 724 O LEU A 93 15.233 29.546 24.820 1.00 21.08 O ATOM 725 CB LEU A 93 12.482 29.876 23.345 1.00 19.07 C ATOM 726 CG LEU A 93 11.014 29.534 23.634 1.00 19.23 C ATOM 727 CD1 LEU A 93 10.427 28.775 22.466 1.00 18.70 C ATOM 728 CD2 LEU A 93 10.909 28.708 24.912 1.00 18.12 C ATOM 729 N GLN A 94 15.323 31.553 23.846 1.00 23.15 N ATOM 730 CA GLN A 94 16.776 31.512 23.709 1.00 24.85 C ATOM 731 C GLN A 94 17.462 31.218 25.047 1.00 24.39 C ATOM 732 O GLN A 94 18.400 30.421 25.125 1.00 23.00 O ATOM 733 CB GLN A 94 17.264 32.823 23.071 1.00 27.24 C ATOM 734 CG GLN A 94 18.780 32.963 22.867 1.00 32.00 C ATOM 735 CD GLN A 94 19.412 31.890 21.992 1.00 33.90 C ATOM 736 OE1 GLN A 94 18.902 31.550 20.928 1.00 36.67 O ATOM 737 NE2 GLN A 94 20.552 31.379 22.417 1.00 35.23 N ATOM 738 N ASP A 95 16.955 31.825 26.111 1.00 25.42 N ATOM 739 CA ASP A 95 17.500 31.618 27.450 1.00 26.60 C ATOM 740 C ASP A 95 17.336 30.187 27.924 1.00 24.89 C ATOM 741 O ASP A 95 18.195 29.668 28.633 1.00 25.24 O ATOM 742 CB ASP A 95 16.821 32.543 28.458 1.00 29.54 C ATOM 743 CG ASP A 95 17.574 33.832 28.665 1.00 33.18 C ATOM 744 OD1 ASP A 95 18.563 34.120 27.929 1.00 36.09 O ATOM 745 OD2 ASP A 95 17.165 34.584 29.572 1.00 36.18 O ATOM 746 N LEU A 96 16.203 29.578 27.591 1.00 23.52 N ATOM 747 CA LEU A 96 15.930 28.205 27.973 1.00 22.66 C ATOM 748 C LEU A 96 16.890 27.297 27.231 1.00 22.64 C ATOM 749 O LEU A 96 17.489 26.424 27.843 1.00 22.68 O ATOM 750 CB LEU A 96 14.480 27.828 27.670 1.00 21.93 C ATOM 751 CG LEU A 96 13.435 27.848 28.784 1.00 22.84 C ATOM 752 CD1 LEU A 96 13.514 29.098 29.591 1.00 24.77 C ATOM 753 CD2 LEU A 96 12.066 27.727 28.206 1.00 22.64 C ATOM 754 N ARG A 97 17.101 27.515 25.934 1.00 22.12 N ATOM 755 CA ARG A 97 18.024 26.650 25.209 1.00 22.39 C ATOM 756 C ARG A 97 19.447 26.783 25.697 1.00 21.87 C ATOM 757 O ARG A 97 20.180 25.805 25.704 1.00 21.29 O ATOM 758 CB ARG A 97 17.954 26.859 23.698 1.00 23.61 C ATOM 759 CG ARG A 97 19.293 26.665 22.975 1.00 25.98 C ATOM 760 CD ARG A 97 19.371 25.443 22.044 1.00 28.35 C ATOM 761 NE ARG A 97 20.656 25.432 21.336 1.00 29.37 N ATOM 762 CZ ARG A 97 21.121 24.439 20.583 1.00 30.09 C ATOM 763 NH1 ARG A 97 20.415 23.329 20.392 1.00 30.58 N ATOM 764 NH2 ARG A 97 22.335 24.540 20.059 1.00 30.55 N ATOM 765 N GLU A 98 19.845 27.981 26.095 1.00 22.13 N ATOM 766 CA GLU A 98 21.206 28.187 26.590 1.00 23.51 C ATOM 767 C GLU A 98 21.389 27.492 27.944 1.00 22.15 C ATOM 768 O GLU A 98 22.436 26.915 28.226 1.00 22.03 O ATOM 769 CB GLU A 98 21.511 29.684 26.738 1.00 25.49 C ATOM 770 CG GLU A 98 21.545 30.499 25.414 1.00 30.27 C ATOM 771 CD GLU A 98 21.757 32.020 25.625 1.00 33.12 C ATOM 772 OE1 GLU A 98 22.114 32.443 26.742 1.00 35.44 O ATOM 773 OE2 GLU A 98 21.583 32.821 24.670 1.00 35.39 O ATOM 774 N GLN A 99 20.352 27.550 28.774 1.00 22.01 N ATOM 775 CA GLN A 99 20.364 26.951 30.099 1.00 21.13 C ATOM 776 C GLN A 99 20.479 25.437 30.028 1.00 20.20 C ATOM 777 O GLN A 99 21.211 24.843 30.814 1.00 20.27 O ATOM 778 CB GLN A 99 19.108 27.371 30.841 1.00 22.87 C ATOM 779 CG GLN A 99 19.216 27.288 32.350 1.00 26.54 C ATOM 780 CD GLN A 99 17.954 27.749 33.072 1.00 27.55 C ATOM 781 OE1 GLN A 99 17.253 28.674 32.626 1.00 29.44 O ATOM 782 NE2 GLN A 99 17.664 27.113 34.208 1.00 27.68 N ATOM 783 N ILE A 100 19.790 24.821 29.066 1.00 18.81 N ATOM 784 CA ILE A 100 19.838 23.368 28.850 1.00 18.74 C ATOM 785 C ILE A 100 21.248 22.926 28.435 1.00 20.05 C ATOM 786 O ILE A 100 21.781 21.960 28.976 1.00 19.24 O ATOM 787 CB ILE A 100 18.864 22.921 27.711 1.00 17.22 C ATOM 788 CG1 ILE A 100 17.409 23.043 28.158 1.00 15.53 C ATOM 789 CG2 ILE A 100 19.189 21.504 27.248 1.00 16.58 C ATOM 790 CD1 ILE A 100 16.439 22.796 27.065 1.00 14.85 C ATOM 791 N LEU A 101 21.847 23.619 27.462 1.00 21.04 N ATOM 792 CA LEU A 101 23.185 23.259 26.992 1.00 23.17 C ATOM 793 C LEU A 101 24.165 23.333 28.127 1.00 23.78 C ATOM 794 O LEU A 101 25.096 22.536 28.200 1.00 24.25 O ATOM 795 CB LEU A 101 23.678 24.201 25.887 1.00 23.75 C ATOM 796 CG LEU A 101 22.990 24.193 24.516 1.00 26.10 C ATOM 797 CD1 LEU A 101 24.004 24.612 23.438 1.00 27.16 C ATOM 798 CD2 LEU A 101 22.455 22.813 24.192 1.00 25.88 C ATOM 799 N ARG A 102 23.993 24.358 28.949 1.00 24.90 N ATOM 800 CA ARG A 102 24.822 24.601 30.112 1.00 27.02 C ATOM 801 C ARG A 102 24.722 23.457 31.118 1.00 27.09 C ATOM 802 O ARG A 102 25.735 22.993 31.633 1.00 26.77 O ATOM 803 CB ARG A 102 24.371 25.906 30.770 1.00 29.76 C ATOM 804 CG ARG A 102 25.081 26.256 32.079 1.00 34.91 C ATOM 805 CD ARG A 102 24.511 27.504 32.756 1.00 38.30 C ATOM 806 NE ARG A 102 23.244 27.270 33.466 1.00 42.56 N ATOM 807 CZ ARG A 102 23.109 26.570 34.602 1.00 44.67 C ATOM 808 NH1 ARG A 102 24.154 25.979 35.194 1.00 44.84 N ATOM 809 NH2 ARG A 102 21.939 26.585 35.243 1.00 45.62 N ATOM 810 N VAL A 103 23.505 22.986 31.382 1.00 27.23 N ATOM 811 CA VAL A 103 23.280 21.898 32.334 1.00 27.45 C ATOM 812 C VAL A 103 23.739 20.542 31.814 1.00 27.78 C ATOM 813 O VAL A 103 24.333 19.780 32.551 1.00 27.70 O ATOM 814 CB VAL A 103 21.803 21.856 32.754 1.00 27.01 C ATOM 815 CG1 VAL A 103 21.451 20.536 33.385 1.00 27.53 C ATOM 816 CG2 VAL A 103 21.528 22.981 33.729 1.00 26.17 C ATOM 817 N LYS A 104 23.473 20.244 30.549 1.00 28.82 N ATOM 818 CA LYS A 104 23.893 18.975 29.956 1.00 30.46 C ATOM 819 C LYS A 104 25.373 19.034 29.573 1.00 32.34 C ATOM 820 O LYS A 104 26.060 17.999 29.525 1.00 32.37 O ATOM 821 CB LYS A 104 23.080 18.654 28.697 1.00 29.24 C ATOM 822 CG LYS A 104 21.588 18.923 28.810 1.00 28.15 C ATOM 823 CD LYS A 104 20.916 17.977 29.733 1.00 27.32 C ATOM 824 CE LYS A 104 20.813 16.611 29.100 1.00 26.12 C ATOM 825 NZ LYS A 104 20.165 15.689 30.064 1.00 23.91 N ATOM 826 N ASP A 105 25.825 20.227 29.192 1.00 34.66 N ATOM 827 CA ASP A 105 27.207 20.437 28.810 1.00 37.01 C ATOM 828 C ASP A 105 27.502 19.771 27.466 1.00 37.91 C ATOM 829 O ASP A 105 28.506 19.058 27.327 1.00 38.70 O ATOM 830 CB ASP A 105 28.108 19.884 29.916 1.00 38.62 C ATOM 831 CG ASP A 105 29.540 20.381 29.836 1.00 41.35 C ATOM 832 OD1 ASP A 105 29.854 21.270 28.998 1.00 43.36 O ATOM 833 OD2 ASP A 105 30.359 19.876 30.649 1.00 42.51 O ATOM 834 N THR A 106 26.619 19.987 26.484 1.00 38.08 N ATOM 835 CA THR A 106 26.779 19.448 25.128 1.00 38.11 C ATOM 836 C THR A 106 25.851 20.247 24.253 1.00 38.28 C ATOM 837 O THR A 106 24.819 20.685 24.737 1.00 38.71 O ATOM 838 CB THR A 106 26.291 18.022 25.009 1.00 38.59 C ATOM 839 OG1 THR A 106 26.601 17.301 26.205 1.00 40.72 O ATOM 840 CG2 THR A 106 26.958 17.352 23.832 1.00 38.41 C ATOM 841 N GLU A 107 26.189 20.433 22.978 1.00 38.64 N ATOM 842 CA GLU A 107 25.318 21.188 22.065 1.00 38.98 C ATOM 843 C GLU A 107 24.374 20.224 21.405 1.00 37.87 C ATOM 844 O GLU A 107 23.421 20.617 20.740 1.00 37.92 O ATOM 845 CB GLU A 107 26.119 21.931 20.979 1.00 41.59 C ATOM 846 CG GLU A 107 26.834 21.039 19.927 1.00 45.45 C ATOM 847 CD GLU A 107 27.488 21.842 18.763 1.00 47.67 C ATOM 848 OE1 GLU A 107 28.320 22.748 19.036 1.00 48.29 O ATOM 849 OE2 GLU A 107 27.172 21.559 17.573 1.00 48.12 O ATOM 850 N ASP A 108 24.650 18.942 21.588 1.00 36.79 N ATOM 851 CA ASP A 108 23.819 17.916 20.987 1.00 36.00 C ATOM 852 C ASP A 108 22.950 17.221 22.003 1.00 33.38 C ATOM 853 O ASP A 108 23.333 16.213 22.619 1.00 33.72 O ATOM 854 CB ASP A 108 24.682 16.951 20.170 1.00 39.07 C ATOM 855 CG ASP A 108 25.144 17.586 18.864 1.00 41.73 C ATOM 856 OD1 ASP A 108 24.440 18.522 18.417 1.00 42.72 O ATOM 857 OD2 ASP A 108 26.204 17.187 18.292 1.00 43.80 O ATOM 858 N VAL A 109 21.765 17.792 22.168 1.00 29.11 N ATOM 859 CA VAL A 109 20.768 17.329 23.120 1.00 25.37 C ATOM 860 C VAL A 109 19.489 17.255 22.314 1.00 22.39 C ATOM 861 O VAL A 109 19.247 18.152 21.518 1.00 23.31 O ATOM 862 CB VAL A 109 20.565 18.414 24.221 1.00 24.73 C ATOM 863 CG1 VAL A 109 19.485 17.984 25.210 1.00 24.96 C ATOM 864 CG2 VAL A 109 21.873 18.676 24.951 1.00 23.91 C ATOM 865 N PRO A 110 18.713 16.153 22.425 1.00 18.67 N ATOM 866 CA PRO A 110 17.449 15.994 21.701 1.00 16.36 C ATOM 867 C PRO A 110 16.529 17.175 22.019 1.00 15.95 C ATOM 868 O PRO A 110 16.229 17.446 23.181 1.00 15.38 O ATOM 869 CB PRO A 110 16.930 14.681 22.256 1.00 16.72 C ATOM 870 CG PRO A 110 18.193 13.916 22.443 1.00 16.50 C ATOM 871 CD PRO A 110 19.055 14.917 23.142 1.00 17.05 C ATOM 872 N MET A 111 16.049 17.857 20.985 1.00 14.98 N ATOM 873 CA MET A 111 15.247 19.055 21.179 1.00 14.99 C ATOM 874 C MET A 111 14.369 19.365 19.980 1.00 13.70 C ATOM 875 O MET A 111 14.702 19.047 18.863 1.00 13.60 O ATOM 876 CB MET A 111 16.212 20.216 21.389 1.00 16.10 C ATOM 877 CG MET A 111 15.674 21.412 22.074 1.00 19.46 C ATOM 878 SD MET A 111 16.971 22.616 22.106 1.00 21.97 S ATOM 879 CE MET A 111 17.857 22.218 23.521 1.00 20.44 C ATOM 880 N ILE A 112 13.223 19.973 20.234 1.00 12.43 N ATOM 881 CA ILE A 112 12.313 20.365 19.187 1.00 11.87 C ATOM 882 C ILE A 112 11.687 21.713 19.575 1.00 11.94 C ATOM 883 O ILE A 112 11.296 21.911 20.729 1.00 10.96 O ATOM 884 CB ILE A 112 11.250 19.286 18.930 1.00 11.68 C ATOM 885 CG1 ILE A 112 10.457 19.612 17.676 1.00 11.91 C ATOM 886 CG2 ILE A 112 10.316 19.135 20.113 1.00 11.58 C ATOM 887 CD1 ILE A 112 9.457 18.553 17.296 1.00 12.94 C ATOM 888 N LEU A 113 11.736 22.669 18.644 1.00 11.74 N ATOM 889 CA LEU A 113 11.157 24.000 18.805 1.00 10.75 C ATOM 890 C LEU A 113 9.741 23.872 18.288 1.00 10.21 C ATOM 891 O LEU A 113 9.526 23.408 17.168 1.00 11.24 O ATOM 892 CB LEU A 113 11.918 25.026 17.959 1.00 11.36 C ATOM 893 CG LEU A 113 11.413 26.464 18.110 1.00 11.44 C ATOM 894 CD1 LEU A 113 11.552 26.882 19.541 1.00 11.21 C ATOM 895 CD2 LEU A 113 12.203 27.374 17.245 1.00 11.90 C ATOM 896 N VAL A 114 8.772 24.251 19.102 1.00 9.60 N ATOM 897 CA VAL A 114 7.383 24.126 18.728 1.00 8.81 C ATOM 898 C VAL A 114 6.612 25.435 18.772 1.00 9.76 C ATOM 899 O VAL A 114 6.551 26.087 19.808 1.00 9.69 O ATOM 900 CB VAL A 114 6.657 23.137 19.659 1.00 8.34 C ATOM 901 CG1 VAL A 114 5.216 23.030 19.278 1.00 7.05 C ATOM 902 CG2 VAL A 114 7.321 21.792 19.649 1.00 7.19 C ATOM 903 N GLY A 115 6.011 25.793 17.643 1.00 10.05 N ATOM 904 CA GLY A 115 5.198 26.991 17.567 1.00 8.87 C ATOM 905 C GLY A 115 3.763 26.540 17.662 1.00 10.26 C ATOM 906 O GLY A 115 3.195 26.056 16.678 1.00 10.59 O ATOM 907 N ASN A 116 3.165 26.703 18.838 1.00 9.56 N ATOM 908 CA ASN A 116 1.800 26.285 19.091 1.00 8.62 C ATOM 909 C ASN A 116 0.743 27.340 18.762 1.00 9.91 C ATOM 910 O ASN A 116 1.043 28.518 18.615 1.00 10.05 O ATOM 911 CB ASN A 116 1.666 25.833 20.549 1.00 7.37 C ATOM 912 CG ASN A 116 0.475 24.946 20.766 1.00 7.34 C ATOM 913 OD1 ASN A 116 0.175 24.114 19.944 1.00 9.53 O ATOM 914 ND2 ASN A 116 -0.211 25.126 21.860 1.00 7.59 N ATOM 915 N LYS A 117 -0.505 26.893 18.687 1.00 10.54 N ATOM 916 CA LYS A 117 -1.663 27.723 18.376 1.00 11.12 C ATOM 917 C LYS A 117 -1.650 28.123 16.921 1.00 12.05 C ATOM 918 O LYS A 117 -2.148 29.184 16.573 1.00 11.73 O ATOM 919 CB LYS A 117 -1.760 28.968 19.270 1.00 10.94 C ATOM 920 CG LYS A 117 -1.709 28.671 20.771 1.00 10.95 C ATOM 921 CD LYS A 117 -2.210 29.801 21.660 1.00 9.09 C ATOM 922 CE LYS A 117 -1.978 29.455 23.126 1.00 9.34 C ATOM 923 NZ LYS A 117 -2.644 30.394 24.053 1.00 7.95 N ATOM 924 N CYS A 118 -1.191 27.206 16.063 1.00 12.78 N ATOM 925 CA CYS A 118 -1.104 27.439 14.612 1.00 13.19 C ATOM 926 C CYS A 118 -2.476 27.549 13.953 1.00 13.19 C ATOM 927 O CYS A 118 -2.597 27.978 12.794 1.00 14.07 O ATOM 928 CB CYS A 118 -0.215 26.383 13.932 1.00 13.77 C ATOM 929 SG CYS A 118 -0.948 24.757 13.625 1.00 14.63 S ATOM 930 N ASP A 119 -3.509 27.215 14.719 1.00 12.68 N ATOM 931 CA ASP A 119 -4.882 27.318 14.275 1.00 13.38 C ATOM 932 C ASP A 119 -5.377 28.771 14.355 1.00 14.02 C ATOM 933 O ASP A 119 -6.443 29.094 13.840 1.00 14.96 O ATOM 934 CB ASP A 119 -5.807 26.392 15.085 1.00 13.07 C ATOM 935 CG ASP A 119 -5.832 26.710 16.574 1.00 12.73 C ATOM 936 OD1 ASP A 119 -4.816 26.507 17.239 1.00 12.44 O ATOM 937 OD2 ASP A 119 -6.887 27.130 17.094 1.00 12.92 O ATOM 938 N LEU A 120 -4.626 29.634 15.034 1.00 14.09 N ATOM 939 CA LEU A 120 -4.988 31.043 15.173 1.00 14.73 C ATOM 940 C LEU A 120 -4.134 31.839 14.201 1.00 15.79 C ATOM 941 O LEU A 120 -3.414 32.762 14.578 1.00 15.18 O ATOM 942 CB LEU A 120 -4.745 31.521 16.602 1.00 13.73 C ATOM 943 CG LEU A 120 -5.560 30.769 17.653 1.00 12.82 C ATOM 944 CD1 LEU A 120 -5.235 31.316 19.024 1.00 12.75 C ATOM 945 CD2 LEU A 120 -7.044 30.859 17.367 1.00 12.54 C ATOM 946 N GLU A 121 -4.296 31.522 12.923 1.00 16.78 N ATOM 947 CA GLU A 121 -3.533 32.138 11.875 1.00 18.78 C ATOM 948 C GLU A 121 -3.724 33.642 11.761 1.00 18.43 C ATOM 949 O GLU A 121 -2.752 34.367 11.555 1.00 17.83 O ATOM 950 CB GLU A 121 -3.844 31.446 10.558 1.00 21.12 C ATOM 951 CG GLU A 121 -3.142 32.046 9.351 1.00 25.13 C ATOM 952 CD GLU A 121 -1.629 32.006 9.457 1.00 26.73 C ATOM 953 OE1 GLU A 121 -1.091 30.915 9.745 1.00 29.65 O ATOM 954 OE2 GLU A 121 -0.982 33.058 9.241 1.00 28.15 O ATOM 955 N ASP A 122 -4.949 34.115 11.949 1.00 18.85 N ATOM 956 CA ASP A 122 -5.230 35.548 11.854 1.00 20.76 C ATOM 957 C ASP A 122 -4.603 36.355 12.963 1.00 19.82 C ATOM 958 O ASP A 122 -4.460 37.569 12.828 1.00 20.87 O ATOM 959 CB ASP A 122 -6.728 35.813 11.863 1.00 24.07 C ATOM 960 CG ASP A 122 -7.387 35.422 10.580 1.00 28.25 C ATOM 961 OD1 ASP A 122 -6.773 35.642 9.504 1.00 31.94 O ATOM 962 OD2 ASP A 122 -8.522 34.892 10.634 1.00 31.05 O ATOM 963 N GLU A 123 -4.270 35.694 14.069 1.00 17.77 N ATOM 964 CA GLU A 123 -3.647 36.340 15.203 1.00 15.49 C ATOM 965 C GLU A 123 -2.128 36.136 15.239 1.00 14.16 C ATOM 966 O GLU A 123 -1.456 36.575 16.161 1.00 13.85 O ATOM 967 CB GLU A 123 -4.281 35.838 16.497 1.00 16.70 C ATOM 968 CG GLU A 123 -5.709 36.289 16.714 1.00 19.93 C ATOM 969 CD GLU A 123 -6.723 35.470 15.948 1.00 22.62 C ATOM 970 OE1 GLU A 123 -6.572 34.234 15.851 1.00 23.69 O ATOM 971 OE2 GLU A 123 -7.696 36.061 15.426 1.00 26.64 O ATOM 972 N ARG A 124 -1.571 35.512 14.216 1.00 13.18 N ATOM 973 CA ARG A 124 -0.135 35.269 14.152 1.00 11.98 C ATOM 974 C ARG A 124 0.734 36.538 14.260 1.00 12.79 C ATOM 975 O ARG A 124 0.500 37.521 13.531 1.00 13.39 O ATOM 976 CB ARG A 124 0.185 34.534 12.842 1.00 10.82 C ATOM 977 CG ARG A 124 1.665 34.379 12.594 1.00 9.65 C ATOM 978 CD ARG A 124 2.006 33.770 11.263 1.00 10.75 C ATOM 979 NE ARG A 124 1.529 32.399 11.089 1.00 10.77 N ATOM 980 CZ ARG A 124 2.208 31.324 11.439 1.00 8.47 C ATOM 981 NH1 ARG A 124 3.392 31.427 11.999 1.00 9.90 N ATOM 982 NH2 ARG A 124 1.735 30.145 11.146 1.00 9.66 N ATOM 983 N VAL A 125 1.719 36.523 15.163 1.00 11.11 N ATOM 984 CA VAL A 125 2.663 37.634 15.329 1.00 11.55 C ATOM 985 C VAL A 125 4.110 37.138 15.256 1.00 11.31 C ATOM 986 O VAL A 125 5.069 37.908 15.422 1.00 11.82 O ATOM 987 CB VAL A 125 2.442 38.496 16.607 1.00 11.10 C ATOM 988 CG1 VAL A 125 1.147 39.252 16.538 1.00 10.58 C ATOM 989 CG2 VAL A 125 2.497 37.663 17.836 1.00 10.67 C ATOM 990 N VAL A 126 4.265 35.844 15.007 1.00 11.63 N ATOM 991 CA VAL A 126 5.577 35.237 14.833 1.00 12.93 C ATOM 992 C VAL A 126 5.455 34.449 13.531 1.00 13.57 C ATOM 993 O VAL A 126 4.604 33.572 13.405 1.00 13.91 O ATOM 994 CB VAL A 126 5.974 34.254 15.966 1.00 13.25 C ATOM 995 CG1 VAL A 126 7.410 33.791 15.748 1.00 11.93 C ATOM 996 CG2 VAL A 126 5.837 34.896 17.348 1.00 13.25 C ATOM 997 N GLY A 127 6.265 34.794 12.543 1.00 14.52 N ATOM 998 CA GLY A 127 6.193 34.103 11.272 1.00 13.84 C ATOM 999 C GLY A 127 6.768 32.706 11.314 1.00 14.80 C ATOM 1000 O GLY A 127 7.591 32.368 12.166 1.00 14.02 O ATOM 1001 N LYS A 128 6.359 31.884 10.368 1.00 15.80 N ATOM 1002 CA LYS A 128 6.877 30.534 10.319 1.00 17.28 C ATOM 1003 C LYS A 128 8.372 30.503 9.959 1.00 16.96 C ATOM 1004 O LYS A 128 9.134 29.783 10.589 1.00 15.49 O ATOM 1005 CB LYS A 128 6.039 29.684 9.373 1.00 19.83 C ATOM 1006 CG LYS A 128 6.419 28.224 9.387 1.00 24.25 C ATOM 1007 CD LYS A 128 5.214 27.342 9.107 1.00 27.96 C ATOM 1008 CE LYS A 128 4.447 27.807 7.855 1.00 30.49 C ATOM 1009 NZ LYS A 128 3.308 28.763 8.158 1.00 32.99 N ATOM 1010 N GLU A 129 8.818 31.296 8.985 1.00 17.33 N ATOM 1011 CA GLU A 129 10.248 31.284 8.657 1.00 18.36 C ATOM 1012 C GLU A 129 11.054 31.851 9.818 1.00 17.30 C ATOM 1013 O GLU A 129 12.196 31.472 10.043 1.00 17.79 O ATOM 1014 CB GLU A 129 10.558 32.067 7.381 1.00 21.22 C ATOM 1015 CG GLU A 129 12.033 32.019 7.006 1.00 25.49 C ATOM 1016 CD GLU A 129 12.369 32.864 5.791 1.00 28.98 C ATOM 1017 OE1 GLU A 129 11.676 32.723 4.750 1.00 29.86 O ATOM 1018 OE2 GLU A 129 13.338 33.671 5.872 1.00 32.06 O ATOM 1019 N GLN A 130 10.442 32.749 10.572 1.00 16.81 N ATOM 1020 CA GLN A 130 11.071 33.346 11.732 1.00 15.85 C ATOM 1021 C GLN A 130 11.329 32.212 12.716 1.00 15.75 C ATOM 1022 O GLN A 130 12.366 32.169 13.359 1.00 15.61 O ATOM 1023 CB GLN A 130 10.117 34.377 12.336 1.00 15.90 C ATOM 1024 CG GLN A 130 10.678 35.172 13.462 1.00 15.49 C ATOM 1025 CD GLN A 130 9.745 36.254 13.953 1.00 15.21 C ATOM 1026 OE1 GLN A 130 8.584 36.353 13.563 1.00 15.33 O ATOM 1027 NE2 GLN A 130 10.258 37.077 14.823 1.00 17.48 N ATOM 1028 N GLY A 131 10.366 31.303 12.832 1.00 16.31 N ATOM 1029 CA GLY A 131 10.505 30.165 13.724 1.00 15.99 C ATOM 1030 C GLY A 131 11.515 29.211 13.138 1.00 17.09 C ATOM 1031 O GLY A 131 12.442 28.804 13.804 1.00 17.51 O ATOM 1032 N GLN A 132 11.390 28.884 11.867 1.00 18.25 N ATOM 1033 CA GLN A 132 12.362 27.991 11.246 1.00 21.02 C ATOM 1034 C GLN A 132 13.771 28.532 11.291 1.00 21.45 C ATOM 1035 O GLN A 132 14.728 27.765 11.405 1.00 21.40 O ATOM 1036 CB GLN A 132 12.008 27.719 9.796 1.00 23.06 C ATOM 1037 CG GLN A 132 13.023 26.821 9.104 1.00 27.45 C ATOM 1038 CD GLN A 132 12.880 25.373 9.513 1.00 28.82 C ATOM 1039 OE1 GLN A 132 11.906 24.726 9.137 1.00 31.43 O ATOM 1040 NE2 GLN A 132 13.839 24.856 10.278 1.00 28.26 N ATOM 1041 N ASN A 133 13.926 29.845 11.164 1.00 22.27 N ATOM 1042 CA ASN A 133 15.268 30.419 11.199 1.00 23.09 C ATOM 1043 C ASN A 133 15.928 30.381 12.559 1.00 22.64 C ATOM 1044 O ASN A 133 17.154 30.426 12.647 1.00 21.88 O ATOM 1045 CB ASN A 133 15.292 31.835 10.610 1.00 26.25 C ATOM 1046 CG ASN A 133 15.261 31.831 9.061 1.00 29.50 C ATOM 1047 OD1 ASN A 133 15.621 30.834 8.404 1.00 30.33 O ATOM 1048 ND2 ASN A 133 14.839 32.952 8.475 1.00 31.41 N ATOM 1049 N LEU A 134 15.130 30.284 13.623 1.00 21.55 N ATOM 1050 CA LEU A 134 15.673 30.209 14.980 1.00 21.11 C ATOM 1051 C LEU A 134 16.189 28.778 15.168 1.00 20.88 C ATOM 1052 O LEU A 134 17.286 28.559 15.667 1.00 20.12 O ATOM 1053 CB LEU A 134 14.576 30.493 16.024 1.00 19.36 C ATOM 1054 CG LEU A 134 14.929 31.216 17.313 1.00 19.31 C ATOM 1055 CD1 LEU A 134 14.040 30.745 18.428 1.00 16.70 C ATOM 1056 CD2 LEU A 134 16.354 31.011 17.660 1.00 17.98 C ATOM 1057 N ALA A 135 15.416 27.805 14.713 1.00 21.44 N ATOM 1058 CA ALA A 135 15.809 26.407 14.836 1.00 22.88 C ATOM 1059 C ALA A 135 17.093 26.080 14.057 1.00 24.59 C ATOM 1060 O ALA A 135 17.910 25.267 14.488 1.00 24.15 O ATOM 1061 CB ALA A 135 14.678 25.510 14.391 1.00 21.39 C ATOM 1062 N ARG A 136 17.277 26.697 12.905 1.00 26.47 N ATOM 1063 CA ARG A 136 18.467 26.429 12.129 1.00 29.05 C ATOM 1064 C ARG A 136 19.714 26.903 12.872 1.00 30.13 C ATOM 1065 O ARG A 136 20.782 26.278 12.802 1.00 30.04 O ATOM 1066 CB ARG A 136 18.364 27.081 10.763 1.00 30.88 C ATOM 1067 CG ARG A 136 17.702 26.184 9.755 1.00 34.77 C ATOM 1068 CD ARG A 136 18.163 26.531 8.332 1.00 39.11 C ATOM 1069 NE ARG A 136 17.480 27.724 7.817 1.00 42.04 N ATOM 1070 CZ ARG A 136 16.265 27.687 7.280 1.00 44.11 C ATOM 1071 NH1 ARG A 136 15.626 26.518 7.173 1.00 45.30 N ATOM 1072 NH2 ARG A 136 15.642 28.820 6.941 1.00 45.30 N ATOM 1073 N GLN A 137 19.568 27.998 13.605 1.00 31.06 N ATOM 1074 CA GLN A 137 20.654 28.550 14.382 1.00 31.38 C ATOM 1075 C GLN A 137 20.951 27.651 15.556 1.00 30.66 C ATOM 1076 O GLN A 137 22.085 27.544 16.005 1.00 30.92 O ATOM 1077 CB GLN A 137 20.285 29.920 14.892 1.00 32.81 C ATOM 1078 CG GLN A 137 21.038 30.966 14.190 1.00 36.88 C ATOM 1079 CD GLN A 137 20.183 32.145 13.910 1.00 39.82 C ATOM 1080 OE1 GLN A 137 19.913 32.463 12.741 1.00 42.00 O ATOM 1081 NE2 GLN A 137 19.720 32.815 14.975 1.00 40.31 N ATOM 1082 N TRP A 138 19.932 27.000 16.075 1.00 29.62 N ATOM 1083 CA TRP A 138 20.160 26.104 17.187 1.00 28.94 C ATOM 1084 C TRP A 138 20.638 24.779 16.636 1.00 29.98 C ATOM 1085 O TRP A 138 20.079 23.731 16.930 1.00 30.45 O ATOM 1086 CB TRP A 138 18.867 25.908 17.963 1.00 26.29 C ATOM 1087 CG TRP A 138 18.488 27.080 18.744 1.00 23.12 C ATOM 1088 CD1 TRP A 138 19.209 28.221 18.911 1.00 21.68 C ATOM 1089 CD2 TRP A 138 17.302 27.225 19.528 1.00 22.06 C ATOM 1090 NE1 TRP A 138 18.548 29.069 19.759 1.00 21.52 N ATOM 1091 CE2 TRP A 138 17.370 28.483 20.151 1.00 22.03 C ATOM 1092 CE3 TRP A 138 16.197 26.405 19.775 1.00 20.94 C ATOM 1093 CZ2 TRP A 138 16.368 28.951 21.004 1.00 20.70 C ATOM 1094 CZ3 TRP A 138 15.207 26.866 20.624 1.00 20.21 C ATOM 1095 CH2 TRP A 138 15.300 28.125 21.228 1.00 20.02 C ATOM 1096 N CYS A 139 21.667 24.832 15.801 1.00 31.95 N ATOM 1097 CA CYS A 139 22.241 23.639 15.189 1.00 33.19 C ATOM 1098 C CYS A 139 21.277 22.794 14.389 1.00 32.32 C ATOM 1099 O CYS A 139 21.341 21.553 14.389 1.00 31.69 O ATOM 1100 CB CYS A 139 22.962 22.820 16.239 1.00 35.17 C ATOM 1101 SG CYS A 139 24.416 23.705 16.694 1.00 40.56 S ATOM 1102 N ASN A 140 20.414 23.492 13.661 1.00 31.70 N ATOM 1103 CA ASN A 140 19.426 22.859 12.803 1.00 31.18 C ATOM 1104 C ASN A 140 18.484 21.924 13.565 1.00 29.02 C ATOM 1105 O ASN A 140 18.110 20.852 13.049 1.00 28.57 O ATOM 1106 CB ASN A 140 20.124 22.102 11.644 1.00 33.66 C ATOM 1107 CG ASN A 140 20.930 23.023 10.726 1.00 36.47 C ATOM 1108 OD1 ASN A 140 20.384 23.648 9.813 1.00 38.76 O ATOM 1109 ND2 ASN A 140 22.249 23.069 10.931 1.00 37.77 N ATOM 1110 N CYS A 141 18.040 22.336 14.754 1.00 26.64 N ATOM 1111 CA CYS A 141 17.159 21.465 15.522 1.00 23.59 C ATOM 1112 C CYS A 141 15.775 21.359 14.921 1.00 21.93 C ATOM 1113 O CYS A 141 15.400 22.162 14.062 1.00 20.29 O ATOM 1114 CB CYS A 141 17.151 21.836 17.020 1.00 24.97 C ATOM 1115 SG CYS A 141 15.924 22.959 17.741 1.00 25.29 S ATOM 1116 N ALA A 142 15.071 20.282 15.260 1.00 19.53 N ATOM 1117 CA ALA A 142 13.724 20.060 14.760 1.00 18.23 C ATOM 1118 C ALA A 142 12.821 21.256 15.053 1.00 17.11 C ATOM 1119 O ALA A 142 12.940 21.901 16.088 1.00 16.40 O ATOM 1120 CB ALA A 142 13.146 18.822 15.382 1.00 18.01 C ATOM 1121 N PHE A 143 11.878 21.508 14.160 1.00 15.95 N ATOM 1122 CA PHE A 143 10.967 22.615 14.306 1.00 14.25 C ATOM 1123 C PHE A 143 9.643 22.224 13.717 1.00 14.19 C ATOM 1124 O PHE A 143 9.584 21.496 12.722 1.00 14.66 O ATOM 1125 CB PHE A 143 11.497 23.846 13.549 1.00 14.72 C ATOM 1126 CG PHE A 143 10.472 24.926 13.363 1.00 14.75 C ATOM 1127 CD1 PHE A 143 10.143 25.768 14.400 1.00 15.29 C ATOM 1128 CD2 PHE A 143 9.768 25.036 12.179 1.00 14.24 C ATOM 1129 CE1 PHE A 143 9.118 26.694 14.261 1.00 15.30 C ATOM 1130 CE2 PHE A 143 8.749 25.949 12.032 1.00 14.14 C ATOM 1131 CZ PHE A 143 8.420 26.781 13.078 1.00 14.97 C ATOM 1132 N LEU A 144 8.570 22.637 14.369 1.00 13.68 N ATOM 1133 CA LEU A 144 7.259 22.386 13.826 1.00 14.07 C ATOM 1134 C LEU A 144 6.259 23.324 14.433 1.00 13.51 C ATOM 1135 O LEU A 144 6.544 23.958 15.433 1.00 13.62 O ATOM 1136 CB LEU A 144 6.857 20.905 13.949 1.00 16.18 C ATOM 1137 CG LEU A 144 6.542 20.148 15.222 1.00 16.37 C ATOM 1138 CD1 LEU A 144 5.150 20.526 15.691 1.00 18.09 C ATOM 1139 CD2 LEU A 144 6.587 18.665 14.912 1.00 16.02 C ATOM 1140 N GLU A 145 5.145 23.513 13.748 1.00 12.61 N ATOM 1141 CA GLU A 145 4.080 24.357 14.240 1.00 12.25 C ATOM 1142 C GLU A 145 2.920 23.458 14.592 1.00 12.82 C ATOM 1143 O GLU A 145 2.502 22.633 13.796 1.00 13.42 O ATOM 1144 CB GLU A 145 3.681 25.388 13.196 1.00 12.81 C ATOM 1145 CG GLU A 145 4.650 26.554 13.133 1.00 13.08 C ATOM 1146 CD GLU A 145 4.058 27.808 12.487 1.00 13.73 C ATOM 1147 OE1 GLU A 145 2.958 27.764 11.907 1.00 13.79 O ATOM 1148 OE2 GLU A 145 4.710 28.854 12.592 1.00 15.12 O ATOM 1149 N SER A 146 2.367 23.629 15.774 1.00 12.20 N ATOM 1150 CA SER A 146 1.304 22.747 16.188 1.00 12.30 C ATOM 1151 C SER A 146 0.036 23.431 16.630 1.00 11.84 C ATOM 1152 O SER A 146 -0.055 24.661 16.654 1.00 11.56 O ATOM 1153 CB SER A 146 1.814 21.875 17.339 1.00 12.51 C ATOM 1154 OG SER A 146 2.065 22.677 18.484 1.00 13.47 O ATOM 1155 N SER A 147 -0.929 22.600 16.999 1.00 11.05 N ATOM 1156 CA SER A 147 -2.202 23.038 17.509 1.00 10.75 C ATOM 1157 C SER A 147 -2.780 21.935 18.359 1.00 12.29 C ATOM 1158 O SER A 147 -3.099 20.873 17.849 1.00 12.42 O ATOM 1159 CB SER A 147 -3.186 23.336 16.393 1.00 8.55 C ATOM 1160 OG SER A 147 -4.416 23.787 16.939 1.00 8.40 O ATOM 1161 N ALA A 148 -2.947 22.206 19.651 1.00 14.07 N ATOM 1162 CA ALA A 148 -3.543 21.258 20.597 1.00 13.99 C ATOM 1163 C ALA A 148 -5.033 21.200 20.317 1.00 14.24 C ATOM 1164 O ALA A 148 -5.682 20.172 20.520 1.00 13.64 O ATOM 1165 CB ALA A 148 -3.324 21.724 22.008 1.00 12.78 C ATOM 1166 N LYS A 149 -5.577 22.318 19.846 1.00 14.81 N ATOM 1167 CA LYS A 149 -6.999 22.395 19.538 1.00 16.47 C ATOM 1168 C LYS A 149 -7.454 21.613 18.300 1.00 17.46 C ATOM 1169 O LYS A 149 -8.487 20.942 18.340 1.00 18.07 O ATOM 1170 CB LYS A 149 -7.441 23.839 19.410 1.00 15.70 C ATOM 1171 CG LYS A 149 -8.930 23.958 19.316 1.00 17.37 C ATOM 1172 CD LYS A 149 -9.358 25.373 19.348 1.00 18.09 C ATOM 1173 CE LYS A 149 -10.843 25.419 19.489 1.00 21.68 C ATOM 1174 NZ LYS A 149 -11.341 26.737 19.015 1.00 25.75 N ATOM 1175 N SER A 150 -6.729 21.773 17.193 1.00 17.61 N ATOM 1176 CA SER A 150 -7.036 21.098 15.935 1.00 18.94 C ATOM 1177 C SER A 150 -6.306 19.775 15.771 1.00 18.62 C ATOM 1178 O SER A 150 -6.469 19.113 14.753 1.00 18.65 O ATOM 1179 CB SER A 150 -6.647 21.983 14.755 1.00 17.97 C ATOM 1180 OG SER A 150 -7.358 23.195 14.800 1.00 22.14 O ATOM 1181 N LYS A 151 -5.441 19.444 16.720 1.00 18.24 N ATOM 1182 CA LYS A 151 -4.671 18.217 16.687 1.00 19.12 C ATOM 1183 C LYS A 151 -3.729 18.167 15.512 1.00 18.79 C ATOM 1184 O LYS A 151 -3.687 17.187 14.769 1.00 19.88 O ATOM 1185 CB LYS A 151 -5.574 16.995 16.657 1.00 20.86 C ATOM 1186 CG LYS A 151 -6.549 16.918 17.788 1.00 23.69 C ATOM 1187 CD LYS A 151 -7.105 15.504 17.902 1.00 27.66 C ATOM 1188 CE LYS A 151 -8.255 15.442 18.888 1.00 29.23 C ATOM 1189 NZ LYS A 151 -9.366 16.289 18.378 1.00 31.49 N ATOM 1190 N ILE A 152 -2.945 19.216 15.358 1.00 17.80 N ATOM 1191 CA ILE A 152 -1.985 19.296 14.283 1.00 16.81 C ATOM 1192 C ILE A 152 -0.594 19.058 14.826 1.00 16.19 C ATOM 1193 O ILE A 152 -0.151 19.786 15.680 1.00 16.32 O ATOM 1194 CB ILE A 152 -2.044 20.670 13.621 1.00 16.87 C ATOM 1195 CG1 ILE A 152 -3.433 20.892 13.050 1.00 17.95 C ATOM 1196 CG2 ILE A 152 -1.017 20.773 12.520 1.00 16.36 C ATOM 1197 CD1 ILE A 152 -3.690 22.313 12.656 1.00 20.82 C ATOM 1198 N ASN A 153 0.073 18.001 14.382 1.00 15.48 N ATOM 1199 CA ASN A 153 1.423 17.704 14.841 1.00 15.46 C ATOM 1200 C ASN A 153 1.591 17.515 16.348 1.00 15.14 C ATOM 1201 O ASN A 153 2.671 17.714 16.860 1.00 15.81 O ATOM 1202 CB ASN A 153 2.405 18.786 14.375 1.00 16.63 C ATOM 1203 CG ASN A 153 2.713 18.719 12.886 1.00 18.21 C ATOM 1204 OD1 ASN A 153 2.740 17.641 12.277 1.00 19.06 O ATOM 1205 ND2 ASN A 153 2.982 19.874 12.295 1.00 16.75 N ATOM 1206 N VAL A 154 0.545 17.110 17.051 1.00 14.70 N ATOM 1207 CA VAL A 154 0.636 16.884 18.486 1.00 15.18 C ATOM 1208 C VAL A 154 1.453 15.622 18.807 1.00 15.35 C ATOM 1209 O VAL A 154 2.397 15.661 19.604 1.00 14.76 O ATOM 1210 CB VAL A 154 -0.766 16.776 19.125 1.00 15.29 C ATOM 1211 CG1 VAL A 154 -0.653 16.495 20.629 1.00 16.41 C ATOM 1212 CG2 VAL A 154 -1.517 18.066 18.928 1.00 15.58 C ATOM 1213 N ASN A 155 1.138 14.511 18.142 1.00 15.52 N ATOM 1214 CA ASN A 155 1.861 13.266 18.380 1.00 15.18 C ATOM 1215 C ASN A 155 3.273 13.396 17.881 1.00 14.56 C ATOM 1216 O ASN A 155 4.198 12.859 18.471 1.00 13.31 O ATOM 1217 CB ASN A 155 1.218 12.102 17.639 1.00 17.16 C ATOM 1218 CG ASN A 155 -0.084 11.699 18.231 1.00 19.10 C ATOM 1219 OD1 ASN A 155 -0.550 12.281 19.201 1.00 21.67 O ATOM 1220 ND2 ASN A 155 -0.699 10.713 17.648 1.00 21.98 N ATOM 1221 N GLU A 156 3.440 14.147 16.805 1.00 14.43 N ATOM 1222 CA GLU A 156 4.742 14.319 16.205 1.00 15.87 C ATOM 1223 C GLU A 156 5.808 14.940 17.120 1.00 15.70 C ATOM 1224 O GLU A 156 6.969 14.563 17.056 1.00 15.46 O ATOM 1225 CB GLU A 156 4.591 15.103 14.905 1.00 18.51 C ATOM 1226 CG GLU A 156 3.955 14.321 13.744 1.00 22.67 C ATOM 1227 CD GLU A 156 2.464 13.935 13.923 1.00 26.26 C ATOM 1228 OE1 GLU A 156 1.688 14.539 14.702 1.00 25.88 O ATOM 1229 OE2 GLU A 156 2.046 12.972 13.241 1.00 29.45 O ATOM 1230 N ILE A 157 5.420 15.876 17.982 1.00 14.73 N ATOM 1231 CA ILE A 157 6.359 16.511 18.892 1.00 14.26 C ATOM 1232 C ILE A 157 7.056 15.450 19.737 1.00 13.79 C ATOM 1233 O ILE A 157 8.276 15.399 19.812 1.00 13.06 O ATOM 1234 CB ILE A 157 5.633 17.463 19.865 1.00 13.78 C ATOM 1235 CG1 ILE A 157 5.071 18.666 19.123 1.00 13.76 C ATOM 1236 CG2 ILE A 157 6.571 17.924 20.960 1.00 15.14 C ATOM 1237 CD1 ILE A 157 4.055 19.424 19.924 1.00 10.93 C ATOM 1238 N PHE A 158 6.255 14.588 20.348 1.00 14.04 N ATOM 1239 CA PHE A 158 6.761 13.541 21.227 1.00 15.11 C ATOM 1240 C PHE A 158 7.466 12.355 20.548 1.00 16.00 C ATOM 1241 O PHE A 158 8.504 11.899 21.025 1.00 16.55 O ATOM 1242 CB PHE A 158 5.644 13.123 22.189 1.00 12.69 C ATOM 1243 CG PHE A 158 5.056 14.288 22.950 1.00 12.44 C ATOM 1244 CD1 PHE A 158 5.758 14.883 23.990 1.00 12.41 C ATOM 1245 CD2 PHE A 158 3.830 14.820 22.592 1.00 10.90 C ATOM 1246 CE1 PHE A 158 5.247 15.986 24.655 1.00 10.90 C ATOM 1247 CE2 PHE A 158 3.314 15.917 23.252 1.00 10.90 C ATOM 1248 CZ PHE A 158 4.023 16.500 24.284 1.00 11.00 C ATOM 1249 N TYR A 159 6.963 11.906 19.403 1.00 17.32 N ATOM 1250 CA TYR A 159 7.612 10.807 18.684 1.00 18.12 C ATOM 1251 C TYR A 159 8.950 11.281 18.154 1.00 17.64 C ATOM 1252 O TYR A 159 9.910 10.509 18.099 1.00 19.08 O ATOM 1253 CB TYR A 159 6.798 10.362 17.480 1.00 18.38 C ATOM 1254 CG TYR A 159 5.455 9.801 17.788 1.00 20.68 C ATOM 1255 CD1 TYR A 159 5.079 9.494 19.080 1.00 21.22 C ATOM 1256 CD2 TYR A 159 4.550 9.565 16.761 1.00 23.71 C ATOM 1257 CE1 TYR A 159 3.823 8.957 19.352 1.00 23.18 C ATOM 1258 CE2 TYR A 159 3.288 9.024 17.019 1.00 24.92 C ATOM 1259 CZ TYR A 159 2.947 8.724 18.318 1.00 24.55 C ATOM 1260 OH TYR A 159 1.731 8.141 18.551 1.00 27.41 O ATOM 1261 N ASP A 160 9.021 12.525 17.691 1.00 17.17 N ATOM 1262 CA ASP A 160 10.289 13.011 17.179 1.00 16.93 C ATOM 1263 C ASP A 160 11.345 12.982 18.260 1.00 15.93 C ATOM 1264 O ASP A 160 12.486 12.624 17.997 1.00 16.01 O ATOM 1265 CB ASP A 160 10.194 14.427 16.595 1.00 19.49 C ATOM 1266 CG ASP A 160 11.346 14.729 15.646 1.00 21.55 C ATOM 1267 OD1 ASP A 160 11.417 14.049 14.598 1.00 25.50 O ATOM 1268 OD2 ASP A 160 12.228 15.556 15.949 1.00 21.71 O ATOM 1269 N LEU A 161 10.989 13.395 19.469 1.00 14.49 N ATOM 1270 CA LEU A 161 11.948 13.375 20.566 1.00 13.65 C ATOM 1271 C LEU A 161 12.397 11.939 20.880 1.00 13.46 C ATOM 1272 O LEU A 161 13.564 11.699 21.189 1.00 12.83 O ATOM 1273 CB LEU A 161 11.355 14.042 21.806 1.00 13.60 C ATOM 1274 CG LEU A 161 11.281 15.571 21.809 1.00 11.90 C ATOM 1275 CD1 LEU A 161 10.586 16.022 23.088 1.00 10.79 C ATOM 1276 CD2 LEU A 161 12.682 16.168 21.692 1.00 10.33 C ATOM 1277 N VAL A 162 11.468 10.991 20.811 1.00 13.75 N ATOM 1278 CA VAL A 162 11.808 9.596 21.037 1.00 14.85 C ATOM 1279 C VAL A 162 12.797 9.172 19.936 1.00 16.16 C ATOM 1280 O VAL A 162 13.807 8.532 20.220 1.00 16.45 O ATOM 1281 CB VAL A 162 10.555 8.696 21.007 1.00 15.02 C ATOM 1282 CG1 VAL A 162 10.946 7.225 20.921 1.00 14.55 C ATOM 1283 CG2 VAL A 162 9.737 8.919 22.258 1.00 14.10 C ATOM 1284 N ARG A 163 12.539 9.574 18.693 1.00 16.92 N ATOM 1285 CA ARG A 163 13.427 9.235 17.580 1.00 17.37 C ATOM 1286 C ARG A 163 14.838 9.808 17.687 1.00 17.37 C ATOM 1287 O ARG A 163 15.796 9.123 17.339 1.00 18.78 O ATOM 1288 CB ARG A 163 12.798 9.610 16.234 1.00 17.51 C ATOM 1289 CG ARG A 163 11.630 8.727 15.856 1.00 19.57 C ATOM 1290 CD ARG A 163 10.981 9.130 14.533 1.00 20.54 C ATOM 1291 NE ARG A 163 9.748 8.364 14.321 1.00 22.48 N ATOM 1292 CZ ARG A 163 8.549 8.901 14.122 1.00 23.24 C ATOM 1293 NH1 ARG A 163 8.398 10.215 14.097 1.00 24.80 N ATOM 1294 NH2 ARG A 163 7.487 8.123 13.964 1.00 25.33 N ATOM 1295 N GLN A 164 14.980 11.032 18.185 1.00 16.70 N ATOM 1296 CA GLN A 164 16.296 11.666 18.334 1.00 16.38 C ATOM 1297 C GLN A 164 17.091 11.009 19.422 1.00 17.79 C ATOM 1298 O GLN A 164 18.313 11.040 19.393 1.00 17.95 O ATOM 1299 CB GLN A 164 16.172 13.151 18.684 1.00 15.26 C ATOM 1300 CG GLN A 164 15.492 13.968 17.628 1.00 15.07 C ATOM 1301 CD GLN A 164 15.417 15.418 17.981 1.00 14.02 C ATOM 1302 OE1 GLN A 164 16.383 15.992 18.437 1.00 13.30 O ATOM 1303 NE2 GLN A 164 14.263 16.026 17.769 1.00 14.56 N ATOM 1304 N ILE A 165 16.389 10.541 20.452 1.00 19.14 N ATOM 1305 CA ILE A 165 17.012 9.865 21.583 1.00 20.10 C ATOM 1306 C ILE A 165 17.481 8.488 21.143 1.00 21.74 C ATOM 1307 O ILE A 165 18.460 7.981 21.658 1.00 22.30 O ATOM 1308 CB ILE A 165 16.034 9.720 22.761 1.00 18.25 C ATOM 1309 CG1 ILE A 165 15.758 11.089 23.397 1.00 18.69 C ATOM 1310 CG2 ILE A 165 16.621 8.799 23.790 1.00 18.02 C ATOM 1311 CD1 ILE A 165 14.423 11.219 24.175 1.00 17.97 C ATOM 1312 N ASN A 166 16.762 7.871 20.214 1.00 24.26 N ATOM 1313 CA ASN A 166 17.145 6.555 19.708 1.00 27.54 C ATOM 1314 C ASN A 166 18.381 6.575 18.824 1.00 30.55 C ATOM 1315 O ASN A 166 18.928 5.519 18.504 1.00 31.98 O ATOM 1316 CB ASN A 166 15.996 5.901 18.965 1.00 26.41 C ATOM 1317 CG ASN A 166 14.968 5.345 19.891 1.00 26.57 C ATOM 1318 OD1 ASN A 166 15.220 5.180 21.094 1.00 26.86 O ATOM 1319 ND2 ASN A 166 13.791 5.047 19.359 1.00 26.50 N ATOM 1320 N ARG A 167 18.797 7.757 18.384 1.00 33.64 N ATOM 1321 CA ARG A 167 19.998 7.903 17.572 1.00 36.48 C ATOM 1322 C ARG A 167 21.137 8.244 18.548 1.00 38.15 C ATOM 1323 O ARG A 167 21.255 7.526 19.568 1.00 39.21 O ATOM 1324 CB ARG A 167 19.824 9.037 16.544 1.00 37.16 C ATOM 1325 CG ARG A 167 18.611 8.879 15.640 1.00 38.54 C ATOM 1326 CD ARG A 167 18.570 9.992 14.619 1.00 40.46 C ATOM 1327 NE ARG A 167 17.197 10.362 14.255 1.00 42.64 N ATOM 1328 CZ ARG A 167 16.705 11.604 14.336 1.00 43.79 C ATOM 1329 NH1 ARG A 167 17.475 12.621 14.749 1.00 44.20 N ATOM 1330 NH2 ARG A 167 15.436 11.843 13.991 1.00 44.19 N ATOM 1331 OXT ARG A 167 21.900 9.235 18.326 1.00 40.90 O TER 1332 ARG A 167 ATOM 1333 N ASN B 56 -1.464 27.157 49.277 1.00 20.81 N ATOM 1334 CA ASN B 56 -2.726 26.378 49.442 1.00 21.42 C ATOM 1335 C ASN B 56 -2.743 25.240 48.449 1.00 19.54 C ATOM 1336 O ASN B 56 -3.651 25.134 47.629 1.00 18.98 O ATOM 1337 CB ASN B 56 -3.936 27.273 49.194 1.00 24.87 C ATOM 1338 CG ASN B 56 -4.658 27.625 50.465 1.00 29.40 C ATOM 1339 OD1 ASN B 56 -4.014 27.862 51.510 1.00 31.50 O ATOM 1340 ND2 ASN B 56 -6.004 27.626 50.417 1.00 32.34 N ATOM 1341 N THR B 57 -1.751 24.371 48.549 1.00 18.46 N ATOM 1342 CA THR B 57 -1.615 23.270 47.615 1.00 16.91 C ATOM 1343 C THR B 57 -1.399 21.964 48.336 1.00 15.59 C ATOM 1344 O THR B 57 -1.062 21.955 49.516 1.00 16.34 O ATOM 1345 CB THR B 57 -0.367 23.494 46.722 1.00 17.27 C ATOM 1346 OG1 THR B 57 0.782 23.613 47.560 1.00 17.07 O ATOM 1347 CG2 THR B 57 -0.493 24.763 45.887 1.00 16.01 C ATOM 1348 N ILE B 58 -1.570 20.866 47.602 1.00 14.77 N ATOM 1349 CA ILE B 58 -1.339 19.523 48.109 1.00 12.03 C ATOM 1350 C ILE B 58 -0.592 18.753 47.017 1.00 11.10 C ATOM 1351 O ILE B 58 -0.990 18.814 45.857 1.00 9.31 O ATOM 1352 CB ILE B 58 -2.662 18.786 48.393 1.00 12.28 C ATOM 1353 CG1 ILE B 58 -3.467 19.526 49.460 1.00 12.16 C ATOM 1354 CG2 ILE B 58 -2.368 17.351 48.849 1.00 12.37 C ATOM 1355 CD1 ILE B 58 -4.852 18.993 49.655 1.00 12.57 C ATOM 1356 N ARG B 59 0.509 18.088 47.358 1.00 9.91 N ATOM 1357 CA ARG B 59 1.214 17.285 46.369 1.00 10.51 C ATOM 1358 C ARG B 59 0.636 15.872 46.446 1.00 10.56 C ATOM 1359 O ARG B 59 0.497 15.317 47.539 1.00 9.22 O ATOM 1360 CB ARG B 59 2.735 17.232 46.608 1.00 9.08 C ATOM 1361 CG ARG B 59 3.446 16.327 45.607 1.00 9.70 C ATOM 1362 CD ARG B 59 4.952 16.451 45.646 1.00 9.86 C ATOM 1363 NE ARG B 59 5.390 17.772 45.218 1.00 9.94 N ATOM 1364 CZ ARG B 59 5.868 18.685 46.039 1.00 10.28 C ATOM 1365 NH1 ARG B 59 6.009 18.425 47.336 1.00 8.46 N ATOM 1366 NH2 ARG B 59 6.212 19.854 45.554 1.00 11.21 N ATOM 1367 N VAL B 60 0.322 15.296 45.287 1.00 10.32 N ATOM 1368 CA VAL B 60 -0.254 13.954 45.217 1.00 9.79 C ATOM 1369 C VAL B 60 0.547 13.052 44.294 1.00 10.02 C ATOM 1370 O VAL B 60 0.789 13.397 43.136 1.00 10.37 O ATOM 1371 CB VAL B 60 -1.703 13.987 44.671 1.00 10.13 C ATOM 1372 CG1 VAL B 60 -2.370 12.646 44.840 1.00 8.93 C ATOM 1373 CG2 VAL B 60 -2.506 15.087 45.332 1.00 9.48 C ATOM 1374 N PHE B 61 0.982 11.912 44.808 1.00 9.53 N ATOM 1375 CA PHE B 61 1.705 10.947 43.999 1.00 9.35 C ATOM 1376 C PHE B 61 0.635 10.022 43.449 1.00 9.90 C ATOM 1377 O PHE B 61 -0.263 9.607 44.182 1.00 10.43 O ATOM 1378 CB PHE B 61 2.729 10.208 44.840 1.00 10.00 C ATOM 1379 CG PHE B 61 3.817 11.091 45.339 1.00 12.15 C ATOM 1380 CD1 PHE B 61 4.957 11.293 44.586 1.00 13.15 C ATOM 1381 CD2 PHE B 61 3.689 11.748 46.547 1.00 11.33 C ATOM 1382 CE1 PHE B 61 5.949 12.134 45.033 1.00 13.42 C ATOM 1383 CE2 PHE B 61 4.673 12.584 46.991 1.00 12.47 C ATOM 1384 CZ PHE B 61 5.802 12.777 46.236 1.00 12.62 C ATOM 1385 N LEU B 62 0.686 9.759 42.148 1.00 9.96 N ATOM 1386 CA LEU B 62 -0.332 8.958 41.481 1.00 10.35 C ATOM 1387 C LEU B 62 0.227 7.657 40.935 1.00 10.50 C ATOM 1388 O LEU B 62 1.421 7.467 40.927 1.00 10.48 O ATOM 1389 CB LEU B 62 -0.888 9.771 40.311 1.00 9.50 C ATOM 1390 CG LEU B 62 -1.520 11.114 40.639 1.00 9.53 C ATOM 1391 CD1 LEU B 62 -1.642 11.944 39.387 1.00 9.10 C ATOM 1392 CD2 LEU B 62 -2.865 10.888 41.274 1.00 8.61 C ATOM 1393 N PRO B 63 -0.641 6.724 40.509 1.00 11.85 N ATOM 1394 CA PRO B 63 -0.093 5.473 39.967 1.00 12.14 C ATOM 1395 C PRO B 63 0.680 5.696 38.654 1.00 11.90 C ATOM 1396 O PRO B 63 0.563 6.751 38.027 1.00 11.63 O ATOM 1397 CB PRO B 63 -1.335 4.580 39.801 1.00 11.45 C ATOM 1398 CG PRO B 63 -2.485 5.495 39.820 1.00 12.50 C ATOM 1399 CD PRO B 63 -2.087 6.592 40.776 1.00 12.13 C ATOM 1400 N ASN B 64 1.475 4.702 38.263 1.00 11.09 N ATOM 1401 CA ASN B 64 2.312 4.741 37.061 1.00 11.88 C ATOM 1402 C ASN B 64 3.368 5.826 37.183 1.00 12.00 C ATOM 1403 O ASN B 64 3.757 6.445 36.206 1.00 11.04 O ATOM 1404 CB ASN B 64 1.494 4.897 35.770 1.00 10.55 C ATOM 1405 CG ASN B 64 2.276 4.459 34.514 1.00 11.66 C ATOM 1406 OD1 ASN B 64 3.378 3.918 34.592 1.00 11.72 O ATOM 1407 ND2 ASN B 64 1.692 4.679 33.361 1.00 11.04 N ATOM 1408 N LYS B 65 3.851 6.012 38.406 1.00 12.75 N ATOM 1409 CA LYS B 65 4.879 6.995 38.725 1.00 13.61 C ATOM 1410 C LYS B 65 4.553 8.420 38.285 1.00 12.86 C ATOM 1411 O LYS B 65 5.413 9.125 37.764 1.00 13.21 O ATOM 1412 CB LYS B 65 6.233 6.568 38.161 1.00 16.12 C ATOM 1413 CG LYS B 65 6.655 5.138 38.506 1.00 19.75 C ATOM 1414 CD LYS B 65 7.987 4.798 37.798 1.00 22.76 C ATOM 1415 CE LYS B 65 8.424 3.339 38.016 1.00 25.28 C ATOM 1416 NZ LYS B 65 9.701 3.034 37.248 1.00 28.49 N ATOM 1417 N GLN B 66 3.323 8.854 38.540 1.00 11.28 N ATOM 1418 CA GLN B 66 2.907 10.193 38.181 1.00 9.77 C ATOM 1419 C GLN B 66 2.712 11.064 39.410 1.00 9.33 C ATOM 1420 O GLN B 66 2.633 10.574 40.525 1.00 8.54 O ATOM 1421 CB GLN B 66 1.635 10.135 37.349 1.00 9.40 C ATOM 1422 CG GLN B 66 1.816 9.395 36.028 1.00 9.18 C ATOM 1423 CD GLN B 66 0.507 9.183 35.299 1.00 8.03 C ATOM 1424 OE1 GLN B 66 0.249 9.821 34.292 1.00 10.99 O ATOM 1425 NE2 GLN B 66 -0.318 8.297 35.801 1.00 8.05 N ATOM 1426 N ARG B 67 2.673 12.369 39.216 1.00 8.90 N ATOM 1427 CA ARG B 67 2.482 13.259 40.339 1.00 11.12 C ATOM 1428 C ARG B 67 1.826 14.549 39.896 1.00 9.96 C ATOM 1429 O ARG B 67 1.889 14.918 38.721 1.00 9.94 O ATOM 1430 CB ARG B 67 3.812 13.540 41.051 1.00 13.43 C ATOM 1431 CG ARG B 67 4.711 14.517 40.333 1.00 19.37 C ATOM 1432 CD ARG B 67 5.974 14.828 41.120 1.00 24.12 C ATOM 1433 NE ARG B 67 6.764 13.615 41.274 1.00 30.11 N ATOM 1434 CZ ARG B 67 7.774 13.492 42.124 1.00 32.38 C ATOM 1435 NH1 ARG B 67 8.107 14.520 42.894 1.00 33.53 N ATOM 1436 NH2 ARG B 67 8.441 12.339 42.225 1.00 33.38 N ATOM 1437 N THR B 68 1.152 15.199 40.835 1.00 9.74 N ATOM 1438 CA THR B 68 0.486 16.458 40.578 1.00 9.64 C ATOM 1439 C THR B 68 0.448 17.278 41.859 1.00 10.35 C ATOM 1440 O THR B 68 0.580 16.735 42.939 1.00 9.81 O ATOM 1441 CB THR B 68 -0.965 16.238 40.054 1.00 8.30 C ATOM 1442 OG1 THR B 68 -1.523 17.486 39.653 1.00 8.26 O ATOM 1443 CG2 THR B 68 -1.868 15.639 41.111 1.00 7.41 C ATOM 1444 N VAL B 69 0.395 18.598 41.712 1.00 11.13 N ATOM 1445 CA VAL B 69 0.265 19.494 42.847 1.00 11.19 C ATOM 1446 C VAL B 69 -0.991 20.247 42.503 1.00 11.87 C ATOM 1447 O VAL B 69 -1.056 20.888 41.450 1.00 12.71 O ATOM 1448 CB VAL B 69 1.445 20.466 42.997 1.00 10.35 C ATOM 1449 CG1 VAL B 69 1.136 21.511 44.055 1.00 9.08 C ATOM 1450 CG2 VAL B 69 2.659 19.725 43.434 1.00 9.35 C ATOM 1451 N VAL B 70 -2.017 20.102 43.336 1.00 12.56 N ATOM 1452 CA VAL B 70 -3.284 20.782 43.099 1.00 13.05 C ATOM 1453 C VAL B 70 -3.530 21.958 44.042 1.00 14.12 C ATOM 1454 O VAL B 70 -2.992 22.004 45.152 1.00 13.59 O ATOM 1455 CB VAL B 70 -4.498 19.812 43.182 1.00 13.57 C ATOM 1456 CG1 VAL B 70 -4.416 18.779 42.093 1.00 13.27 C ATOM 1457 CG2 VAL B 70 -4.579 19.155 44.537 1.00 12.57 C ATOM 1458 N ASN B 71 -4.360 22.887 43.580 1.00 15.34 N ATOM 1459 CA ASN B 71 -4.754 24.064 44.344 1.00 17.61 C ATOM 1460 C ASN B 71 -6.004 23.649 45.085 1.00 17.98 C ATOM 1461 O ASN B 71 -6.840 22.911 44.538 1.00 17.33 O ATOM 1462 CB ASN B 71 -5.189 25.217 43.423 1.00 20.56 C ATOM 1463 CG ASN B 71 -4.050 25.874 42.706 1.00 21.78 C ATOM 1464 OD1 ASN B 71 -4.069 25.994 41.484 1.00 25.92 O ATOM 1465 ND2 ASN B 71 -3.082 26.350 43.444 1.00 22.71 N ATOM 1466 N VAL B 72 -6.158 24.152 46.304 1.00 18.34 N ATOM 1467 CA VAL B 72 -7.335 23.841 47.096 1.00 19.21 C ATOM 1468 C VAL B 72 -8.101 25.116 47.361 1.00 20.54 C ATOM 1469 O VAL B 72 -7.563 26.070 47.918 1.00 20.17 O ATOM 1470 CB VAL B 72 -6.985 23.226 48.467 1.00 19.41 C ATOM 1471 CG1 VAL B 72 -8.253 22.949 49.244 1.00 18.98 C ATOM 1472 CG2 VAL B 72 -6.183 21.967 48.298 1.00 18.61 C ATOM 1473 N ARG B 73 -9.343 25.149 46.914 1.00 22.12 N ATOM 1474 CA ARG B 73 -10.210 26.286 47.150 1.00 24.25 C ATOM 1475 C ARG B 73 -11.077 25.848 48.315 1.00 24.82 C ATOM 1476 O ARG B 73 -11.536 24.690 48.350 1.00 24.15 O ATOM 1477 CB ARG B 73 -11.048 26.561 45.915 1.00 25.20 C ATOM 1478 CG ARG B 73 -10.204 27.138 44.830 1.00 29.68 C ATOM 1479 CD ARG B 73 -10.894 27.217 43.472 1.00 32.84 C ATOM 1480 NE ARG B 73 -9.859 27.593 42.511 1.00 36.11 N ATOM 1481 CZ ARG B 73 -9.529 26.886 41.436 1.00 36.72 C ATOM 1482 NH1 ARG B 73 -10.179 25.762 41.146 1.00 37.03 N ATOM 1483 NH2 ARG B 73 -8.441 27.223 40.749 1.00 37.49 N ATOM 1484 N ASN B 74 -11.268 26.738 49.291 1.00 24.73 N ATOM 1485 CA ASN B 74 -12.060 26.403 50.475 1.00 24.63 C ATOM 1486 C ASN B 74 -13.403 25.827 50.082 1.00 22.25 C ATOM 1487 O ASN B 74 -14.061 26.316 49.164 1.00 21.14 O ATOM 1488 CB ASN B 74 -12.256 27.625 51.395 1.00 28.42 C ATOM 1489 CG ASN B 74 -11.251 27.675 52.530 1.00 32.06 C ATOM 1490 OD1 ASN B 74 -10.208 27.004 52.499 1.00 33.41 O ATOM 1491 ND2 ASN B 74 -11.536 28.516 53.534 1.00 35.19 N ATOM 1492 N GLY B 75 -13.765 24.726 50.729 1.00 19.83 N ATOM 1493 CA GLY B 75 -15.027 24.094 50.421 1.00 16.42 C ATOM 1494 C GLY B 75 -14.876 22.831 49.613 1.00 14.54 C ATOM 1495 O GLY B 75 -15.766 22.007 49.666 1.00 14.57 O ATOM 1496 N MET B 76 -13.795 22.679 48.853 1.00 12.89 N ATOM 1497 CA MET B 76 -13.592 21.472 48.041 1.00 12.20 C ATOM 1498 C MET B 76 -13.376 20.226 48.872 1.00 11.55 C ATOM 1499 O MET B 76 -12.725 20.272 49.908 1.00 11.92 O ATOM 1500 CB MET B 76 -12.357 21.602 47.150 1.00 12.54 C ATOM 1501 CG MET B 76 -12.514 22.420 45.896 1.00 13.12 C ATOM 1502 SD MET B 76 -10.919 22.519 45.052 1.00 17.77 S ATOM 1503 CE MET B 76 -11.486 22.663 43.401 1.00 15.30 C ATOM 1504 N SER B 77 -13.926 19.114 48.421 1.00 12.05 N ATOM 1505 CA SER B 77 -13.702 17.853 49.097 1.00 12.75 C ATOM 1506 C SER B 77 -12.476 17.304 48.380 1.00 13.21 C ATOM 1507 O SER B 77 -12.101 17.818 47.321 1.00 11.07 O ATOM 1508 CB SER B 77 -14.894 16.919 48.922 1.00 14.97 C ATOM 1509 OG SER B 77 -14.891 16.286 47.649 1.00 17.46 O ATOM 1510 N LEU B 78 -11.835 16.290 48.955 1.00 12.76 N ATOM 1511 CA LEU B 78 -10.647 15.679 48.359 1.00 12.79 C ATOM 1512 C LEU B 78 -10.923 15.232 46.912 1.00 12.94 C ATOM 1513 O LEU B 78 -10.088 15.390 46.027 1.00 12.18 O ATOM 1514 CB LEU B 78 -10.183 14.524 49.243 1.00 13.47 C ATOM 1515 CG LEU B 78 -8.760 14.016 49.110 1.00 16.15 C ATOM 1516 CD1 LEU B 78 -7.784 15.177 49.183 1.00 15.96 C ATOM 1517 CD2 LEU B 78 -8.513 13.019 50.210 1.00 14.73 C ATOM 1518 N HIS B 79 -12.130 14.719 46.683 1.00 13.06 N ATOM 1519 CA HIS B 79 -12.622 14.284 45.377 1.00 14.14 C ATOM 1520 C HIS B 79 -12.739 15.476 44.391 1.00 13.96 C ATOM 1521 O HIS B 79 -12.440 15.350 43.205 1.00 13.75 O ATOM 1522 CB HIS B 79 -13.998 13.655 45.591 1.00 18.37 C ATOM 1523 CG HIS B 79 -14.569 12.998 44.380 1.00 23.13 C ATOM 1524 ND1 HIS B 79 -15.161 13.707 43.356 1.00 25.78 N ATOM 1525 CD2 HIS B 79 -14.662 11.690 44.036 1.00 25.55 C ATOM 1526 CE1 HIS B 79 -15.591 12.868 42.430 1.00 26.22 C ATOM 1527 NE2 HIS B 79 -15.301 11.638 42.820 1.00 27.58 N ATOM 1528 N ASP B 80 -13.173 16.637 44.868 1.00 12.89 N ATOM 1529 CA ASP B 80 -13.308 17.801 43.992 1.00 12.37 C ATOM 1530 C ASP B 80 -11.985 18.362 43.549 1.00 12.28 C ATOM 1531 O ASP B 80 -11.868 18.797 42.414 1.00 13.24 O ATOM 1532 CB ASP B 80 -14.075 18.953 44.650 1.00 11.81 C ATOM 1533 CG ASP B 80 -15.476 18.592 45.027 1.00 12.56 C ATOM 1534 OD1 ASP B 80 -16.262 18.145 44.174 1.00 13.36 O ATOM 1535 OD2 ASP B 80 -15.811 18.773 46.204 1.00 13.17 O ATOM 1536 N CYS B 81 -10.979 18.368 44.418 1.00 12.64 N ATOM 1537 CA CYS B 81 -9.697 18.957 44.039 1.00 14.46 C ATOM 1538 C CYS B 81 -8.774 18.117 43.169 1.00 13.01 C ATOM 1539 O CYS B 81 -7.957 18.658 42.445 1.00 13.44 O ATOM 1540 CB CYS B 81 -8.956 19.559 45.248 1.00 16.28 C ATOM 1541 SG CYS B 81 -7.860 18.501 46.148 1.00 24.69 S ATOM 1542 N LEU B 82 -9.003 16.813 43.143 1.00 12.18 N ATOM 1543 CA LEU B 82 -8.194 15.896 42.373 1.00 11.77 C ATOM 1544 C LEU B 82 -8.907 15.418 41.113 1.00 11.48 C ATOM 1545 O LEU B 82 -8.303 14.803 40.247 1.00 11.18 O ATOM 1546 CB LEU B 82 -7.824 14.709 43.268 1.00 12.28 C ATOM 1547 CG LEU B 82 -6.581 14.878 44.139 1.00 12.63 C ATOM 1548 CD1 LEU B 82 -6.397 13.693 45.070 1.00 11.62 C ATOM 1549 CD2 LEU B 82 -5.422 14.984 43.163 1.00 13.72 C ATOM 1550 N MET B 83 -10.175 15.771 40.990 1.00 11.44 N ATOM 1551 CA MET B 83 -11.004 15.383 39.859 1.00 14.61 C ATOM 1552 C MET B 83 -10.351 15.565 38.471 1.00 13.62 C ATOM 1553 O MET B 83 -10.247 14.620 37.692 1.00 12.87 O ATOM 1554 CB MET B 83 -12.324 16.154 39.950 1.00 18.45 C ATOM 1555 CG MET B 83 -13.405 15.675 39.026 1.00 25.18 C ATOM 1556 SD MET B 83 -14.927 16.591 39.367 1.00 34.96 S ATOM 1557 CE MET B 83 -14.592 18.180 38.420 1.00 32.19 C ATOM 1558 N LYS B 84 -9.936 16.791 38.162 1.00 12.89 N ATOM 1559 CA LYS B 84 -9.300 17.090 36.897 1.00 12.58 C ATOM 1560 C LYS B 84 -7.972 16.343 36.689 1.00 11.80 C ATOM 1561 O LYS B 84 -7.721 15.832 35.608 1.00 11.53 O ATOM 1562 CB LYS B 84 -9.098 18.597 36.739 1.00 13.55 C ATOM 1563 CG LYS B 84 -8.554 18.953 35.358 1.00 16.38 C ATOM 1564 CD LYS B 84 -8.076 20.389 35.203 1.00 17.80 C ATOM 1565 CE LYS B 84 -7.288 20.527 33.891 1.00 20.44 C ATOM 1566 NZ LYS B 84 -6.872 21.932 33.640 1.00 21.47 N ATOM 1567 N ALA B 85 -7.122 16.267 37.707 1.00 11.20 N ATOM 1568 CA ALA B 85 -5.847 15.566 37.566 1.00 10.75 C ATOM 1569 C ALA B 85 -6.024 14.080 37.270 1.00 11.02 C ATOM 1570 O ALA B 85 -5.234 13.476 36.559 1.00 10.79 O ATOM 1571 CB ALA B 85 -4.997 15.754 38.821 1.00 10.73 C ATOM 1572 N LEU B 86 -7.040 13.474 37.857 1.00 11.13 N ATOM 1573 CA LEU B 86 -7.303 12.061 37.631 1.00 12.08 C ATOM 1574 C LEU B 86 -7.890 11.839 36.235 1.00 12.62 C ATOM 1575 O LEU B 86 -7.501 10.911 35.535 1.00 11.70 O ATOM 1576 CB LEU B 86 -8.260 11.536 38.695 1.00 12.98 C ATOM 1577 CG LEU B 86 -7.742 11.577 40.127 1.00 14.10 C ATOM 1578 CD1 LEU B 86 -8.724 10.890 41.034 1.00 15.59 C ATOM 1579 CD2 LEU B 86 -6.405 10.920 40.198 1.00 13.60 C ATOM 1580 N LYS B 87 -8.813 12.707 35.834 1.00 13.52 N ATOM 1581 CA LYS B 87 -9.449 12.616 34.527 1.00 14.28 C ATOM 1582 C LYS B 87 -8.500 12.710 33.351 1.00 13.38 C ATOM 1583 O LYS B 87 -8.630 11.945 32.406 1.00 12.52 O ATOM 1584 CB LYS B 87 -10.518 13.686 34.380 1.00 16.99 C ATOM 1585 CG LYS B 87 -11.097 13.784 32.971 1.00 21.67 C ATOM 1586 CD LYS B 87 -12.125 14.910 32.874 1.00 26.63 C ATOM 1587 CE LYS B 87 -13.498 14.516 33.456 1.00 30.03 C ATOM 1588 NZ LYS B 87 -13.495 13.850 34.808 1.00 32.38 N ATOM 1589 N VAL B 88 -7.544 13.633 33.397 1.00 13.14 N ATOM 1590 CA VAL B 88 -6.608 13.791 32.289 1.00 12.38 C ATOM 1591 C VAL B 88 -5.591 12.669 32.206 1.00 12.56 C ATOM 1592 O VAL B 88 -4.824 12.603 31.264 1.00 13.47 O ATOM 1593 CB VAL B 88 -5.934 15.203 32.249 1.00 11.58 C ATOM 1594 CG1 VAL B 88 -6.976 16.263 32.011 1.00 10.69 C ATOM 1595 CG2 VAL B 88 -5.213 15.502 33.540 1.00 11.30 C ATOM 1596 N ARG B 89 -5.594 11.778 33.191 1.00 12.15 N ATOM 1597 CA ARG B 89 -4.690 10.623 33.193 1.00 12.61 C ATOM 1598 C ARG B 89 -5.491 9.312 33.047 1.00 13.24 C ATOM 1599 O ARG B 89 -4.928 8.225 33.087 1.00 13.85 O ATOM 1600 CB ARG B 89 -3.831 10.599 34.471 1.00 10.13 C ATOM 1601 CG ARG B 89 -2.772 11.705 34.506 1.00 9.75 C ATOM 1602 CD ARG B 89 -2.033 11.774 35.851 1.00 8.32 C ATOM 1603 NE ARG B 89 -1.009 12.815 35.902 1.00 5.98 N ATOM 1604 CZ ARG B 89 -1.243 14.092 36.152 1.00 5.02 C ATOM 1605 NH1 ARG B 89 -2.463 14.531 36.370 1.00 5.61 N ATOM 1606 NH2 ARG B 89 -0.235 14.922 36.254 1.00 4.84 N ATOM 1607 N GLY B 90 -6.809 9.437 32.888 1.00 15.17 N ATOM 1608 CA GLY B 90 -7.687 8.286 32.741 1.00 16.15 C ATOM 1609 C GLY B 90 -7.871 7.456 33.998 1.00 17.71 C ATOM 1610 O GLY B 90 -8.193 6.272 33.920 1.00 18.79 O ATOM 1611 N LEU B 91 -7.695 8.075 35.160 1.00 17.75 N ATOM 1612 CA LEU B 91 -7.819 7.368 36.423 1.00 17.93 C ATOM 1613 C LEU B 91 -9.203 7.667 36.974 1.00 19.39 C ATOM 1614 O LEU B 91 -9.705 8.772 36.836 1.00 19.96 O ATOM 1615 CB LEU B 91 -6.726 7.839 37.391 1.00 16.10 C ATOM 1616 CG LEU B 91 -5.270 7.781 36.908 1.00 15.62 C ATOM 1617 CD1 LEU B 91 -4.381 8.564 37.838 1.00 14.63 C ATOM 1618 CD2 LEU B 91 -4.789 6.354 36.808 1.00 16.73 C ATOM 1619 N GLN B 92 -9.849 6.671 37.563 1.00 21.15 N ATOM 1620 CA GLN B 92 -11.181 6.874 38.095 1.00 22.17 C ATOM 1621 C GLN B 92 -11.094 6.680 39.595 1.00 21.05 C ATOM 1622 O GLN B 92 -10.668 5.625 40.047 1.00 20.65 O ATOM 1623 CB GLN B 92 -12.117 5.848 37.464 1.00 25.36 C ATOM 1624 CG GLN B 92 -12.045 5.823 35.935 1.00 29.76 C ATOM 1625 CD GLN B 92 -12.467 4.490 35.337 1.00 33.01 C ATOM 1626 OE1 GLN B 92 -11.835 3.980 34.399 1.00 35.50 O ATOM 1627 NE2 GLN B 92 -13.551 3.923 35.854 1.00 34.87 N ATOM 1628 N PRO B 93 -11.483 7.694 40.396 1.00 20.47 N ATOM 1629 CA PRO B 93 -11.421 7.568 41.860 1.00 20.41 C ATOM 1630 C PRO B 93 -12.063 6.343 42.508 1.00 20.23 C ATOM 1631 O PRO B 93 -11.544 5.815 43.486 1.00 19.28 O ATOM 1632 CB PRO B 93 -12.040 8.888 42.359 1.00 19.48 C ATOM 1633 CG PRO B 93 -12.730 9.446 41.176 1.00 19.65 C ATOM 1634 CD PRO B 93 -11.841 9.073 40.040 1.00 20.04 C ATOM 1635 N GLU B 94 -13.163 5.867 41.941 1.00 21.24 N ATOM 1636 CA GLU B 94 -13.864 4.696 42.465 1.00 22.87 C ATOM 1637 C GLU B 94 -13.026 3.408 42.458 1.00 21.63 C ATOM 1638 O GLU B 94 -13.338 2.456 43.180 1.00 21.00 O ATOM 1639 CB GLU B 94 -15.177 4.486 41.690 1.00 25.88 C ATOM 1640 CG GLU B 94 -15.027 4.430 40.159 1.00 31.74 C ATOM 1641 CD GLU B 94 -15.185 5.785 39.461 1.00 34.26 C ATOM 1642 OE1 GLU B 94 -15.093 6.848 40.115 1.00 36.03 O ATOM 1643 OE2 GLU B 94 -15.417 5.794 38.227 1.00 37.96 O ATOM 1644 N CYS B 95 -11.950 3.397 41.669 1.00 20.67 N ATOM 1645 CA CYS B 95 -11.057 2.244 41.546 1.00 19.91 C ATOM 1646 C CYS B 95 -9.774 2.468 42.327 1.00 18.49 C ATOM 1647 O CYS B 95 -8.877 1.621 42.306 1.00 17.62 O ATOM 1648 CB CYS B 95 -10.657 2.017 40.079 1.00 21.47 C ATOM 1649 SG CYS B 95 -11.994 1.955 38.849 1.00 26.73 S ATOM 1650 N CYS B 96 -9.686 3.594 43.027 1.00 16.74 N ATOM 1651 CA CYS B 96 -8.484 3.936 43.780 1.00 15.43 C ATOM 1652 C CYS B 96 -8.718 4.276 45.243 1.00 14.50 C ATOM 1653 O CYS B 96 -9.814 4.671 45.628 1.00 13.54 O ATOM 1654 CB CYS B 96 -7.828 5.157 43.142 1.00 16.33 C ATOM 1655 SG CYS B 96 -7.409 4.993 41.421 1.00 16.74 S ATOM 1656 N ALA B 97 -7.680 4.082 46.052 1.00 13.34 N ATOM 1657 CA ALA B 97 -7.692 4.437 47.472 1.00 12.96 C ATOM 1658 C ALA B 97 -6.737 5.625 47.573 1.00 12.97 C ATOM 1659 O ALA B 97 -5.771 5.715 46.809 1.00 13.32 O ATOM 1660 CB ALA B 97 -7.179 3.301 48.319 1.00 11.87 C ATOM 1661 N VAL B 98 -7.021 6.560 48.468 1.00 12.74 N ATOM 1662 CA VAL B 98 -6.145 7.706 48.638 1.00 12.43 C ATOM 1663 C VAL B 98 -5.614 7.712 50.077 1.00 12.46 C ATOM 1664 O VAL B 98 -6.353 7.436 51.022 1.00 12.06 O ATOM 1665 CB VAL B 98 -6.841 9.034 48.214 1.00 11.80 C ATOM 1666 CG1 VAL B 98 -8.099 9.254 48.983 1.00 12.61 C ATOM 1667 CG2 VAL B 98 -5.898 10.213 48.389 1.00 12.61 C ATOM 1668 N PHE B 99 -4.315 7.967 50.227 1.00 11.75 N ATOM 1669 CA PHE B 99 -3.666 7.950 51.521 1.00 11.69 C ATOM 1670 C PHE B 99 -2.941 9.213 51.840 1.00 12.57 C ATOM 1671 O PHE B 99 -2.495 9.926 50.962 1.00 12.92 O ATOM 1672 CB PHE B 99 -2.615 6.844 51.585 1.00 10.22 C ATOM 1673 CG PHE B 99 -3.122 5.502 51.205 1.00 12.43 C ATOM 1674 CD1 PHE B 99 -3.171 5.121 49.871 1.00 12.56 C ATOM 1675 CD2 PHE B 99 -3.549 4.610 52.174 1.00 12.97 C ATOM 1676 CE1 PHE B 99 -3.644 3.875 49.501 1.00 14.07 C ATOM 1677 CE2 PHE B 99 -4.028 3.349 51.815 1.00 13.83 C ATOM 1678 CZ PHE B 99 -4.076 2.980 50.476 1.00 13.17 C ATOM 1679 N ARG B 100 -2.719 9.397 53.125 1.00 12.88 N ATOM 1680 CA ARG B 100 -1.976 10.513 53.647 1.00 13.86 C ATOM 1681 C ARG B 100 -0.633 9.865 54.004 1.00 13.34 C ATOM 1682 O ARG B 100 -0.602 8.778 54.590 1.00 13.24 O ATOM 1683 CB ARG B 100 -2.701 10.996 54.883 1.00 16.04 C ATOM 1684 CG ARG B 100 -2.072 12.121 55.561 1.00 20.20 C ATOM 1685 CD ARG B 100 -2.861 12.448 56.808 1.00 21.56 C ATOM 1686 NE ARG B 100 -1.924 12.945 57.789 1.00 24.42 N ATOM 1687 CZ ARG B 100 -1.831 12.512 59.036 1.00 24.57 C ATOM 1688 NH1 ARG B 100 -2.633 11.558 59.510 1.00 24.88 N ATOM 1689 NH2 ARG B 100 -0.887 13.021 59.789 1.00 25.86 N ATOM 1690 N LEU B 101 0.468 10.471 53.583 1.00 12.96 N ATOM 1691 CA LEU B 101 1.772 9.916 53.862 1.00 13.74 C ATOM 1692 C LEU B 101 2.225 10.303 55.244 1.00 14.95 C ATOM 1693 O LEU B 101 2.226 11.487 55.587 1.00 14.17 O ATOM 1694 CB LEU B 101 2.791 10.363 52.810 1.00 13.73 C ATOM 1695 CG LEU B 101 2.504 9.900 51.365 1.00 15.10 C ATOM 1696 CD1 LEU B 101 3.684 10.217 50.439 1.00 14.59 C ATOM 1697 CD2 LEU B 101 2.216 8.417 51.364 1.00 15.65 C ATOM 1698 N LEU B 102 2.545 9.302 56.062 1.00 16.85 N ATOM 1699 CA LEU B 102 3.002 9.540 57.437 1.00 20.05 C ATOM 1700 C LEU B 102 4.523 9.540 57.418 1.00 22.14 C ATOM 1701 O LEU B 102 5.158 8.501 57.214 1.00 23.43 O ATOM 1702 CB LEU B 102 2.463 8.462 58.380 1.00 18.83 C ATOM 1703 CG LEU B 102 0.938 8.239 58.352 1.00 18.90 C ATOM 1704 CD1 LEU B 102 0.570 7.052 59.202 1.00 18.44 C ATOM 1705 CD2 LEU B 102 0.186 9.450 58.835 1.00 17.70 C ATOM 1706 N HIS B 103 5.108 10.724 57.555 1.00 24.24 N ATOM 1707 CA HIS B 103 6.562 10.858 57.517 1.00 26.69 C ATOM 1708 C HIS B 103 7.151 10.533 58.870 1.00 29.84 C ATOM 1709 O HIS B 103 8.264 10.067 58.941 1.00 29.74 O ATOM 1710 CB HIS B 103 6.977 12.277 57.089 1.00 23.98 C ATOM 1711 CG HIS B 103 6.334 12.741 55.819 1.00 20.69 C ATOM 1712 ND1 HIS B 103 6.353 11.999 54.659 1.00 18.00 N ATOM 1713 CD2 HIS B 103 5.609 13.852 55.545 1.00 18.71 C ATOM 1714 CE1 HIS B 103 5.663 12.627 53.724 1.00 18.32 C ATOM 1715 NE2 HIS B 103 5.201 13.754 54.237 1.00 17.23 N ATOM 1716 N GLU B 104 6.366 10.735 59.927 1.00 34.47 N ATOM 1717 CA GLU B 104 6.777 10.464 61.304 1.00 38.80 C ATOM 1718 C GLU B 104 7.009 8.994 61.574 1.00 40.83 C ATOM 1719 O GLU B 104 7.889 8.635 62.352 1.00 42.14 O ATOM 1720 CB GLU B 104 5.709 10.962 62.274 1.00 41.16 C ATOM 1721 CG GLU B 104 5.680 12.458 62.437 1.00 44.99 C ATOM 1722 CD GLU B 104 6.975 12.985 63.004 1.00 47.75 C ATOM 1723 OE1 GLU B 104 7.943 13.139 62.217 1.00 49.23 O ATOM 1724 OE2 GLU B 104 7.036 13.241 64.240 1.00 49.98 O ATOM 1725 N HIS B 105 6.161 8.156 60.983 1.00 43.03 N ATOM 1726 CA HIS B 105 6.229 6.704 61.132 1.00 45.01 C ATOM 1727 C HIS B 105 6.837 6.033 59.912 1.00 46.03 C ATOM 1728 O HIS B 105 6.165 5.248 59.230 1.00 46.61 O ATOM 1729 CB HIS B 105 4.831 6.146 61.349 1.00 46.22 C ATOM 1730 CG HIS B 105 4.100 6.801 62.471 1.00 48.20 C ATOM 1731 ND1 HIS B 105 2.778 6.536 62.755 1.00 49.41 N ATOM 1732 CD2 HIS B 105 4.505 7.728 63.372 1.00 48.78 C ATOM 1733 CE1 HIS B 105 2.396 7.272 63.784 1.00 49.90 C ATOM 1734 NE2 HIS B 105 3.427 8.005 64.176 1.00 50.27 N ATOM 1735 N LYS B 106 8.086 6.379 59.621 1.00 46.46 N ATOM 1736 CA LYS B 106 8.845 5.837 58.491 1.00 46.79 C ATOM 1737 C LYS B 106 8.164 4.941 57.448 1.00 46.45 C ATOM 1738 O LYS B 106 8.279 3.695 57.480 1.00 46.81 O ATOM 1739 CB LYS B 106 10.112 5.139 59.004 1.00 48.38 C ATOM 1740 CG LYS B 106 10.937 4.423 57.903 1.00 49.96 C ATOM 1741 CD LYS B 106 11.507 5.404 56.877 1.00 50.80 C ATOM 1742 CE LYS B 106 11.410 4.845 55.462 1.00 51.22 C ATOM 1743 NZ LYS B 106 12.126 5.724 54.483 1.00 52.39 N ATOM 1744 N GLY B 107 7.478 5.568 56.498 1.00 45.29 N ATOM 1745 CA GLY B 107 6.863 4.794 55.432 1.00 43.10 C ATOM 1746 C GLY B 107 5.408 4.376 55.531 1.00 40.99 C ATOM 1747 O GLY B 107 4.919 3.681 54.631 1.00 41.55 O ATOM 1748 N LYS B 108 4.708 4.739 56.601 1.00 37.61 N ATOM 1749 CA LYS B 108 3.308 4.350 56.671 1.00 34.05 C ATOM 1750 C LYS B 108 2.431 5.354 55.942 1.00 30.47 C ATOM 1751 O LYS B 108 2.845 6.495 55.680 1.00 29.70 O ATOM 1752 CB LYS B 108 2.850 4.157 58.118 1.00 35.02 C ATOM 1753 CG LYS B 108 3.215 2.769 58.706 1.00 37.24 C ATOM 1754 CD LYS B 108 4.411 2.849 59.668 1.00 38.70 C ATOM 1755 CE LYS B 108 4.842 1.456 60.181 1.00 40.22 C ATOM 1756 NZ LYS B 108 5.407 0.618 59.049 1.00 40.96 N ATOM 1757 N LYS B 109 1.262 4.882 55.524 1.00 26.44 N ATOM 1758 CA LYS B 109 0.260 5.685 54.845 1.00 22.93 C ATOM 1759 C LYS B 109 -0.981 5.465 55.677 1.00 20.34 C ATOM 1760 O LYS B 109 -1.154 4.401 56.268 1.00 20.74 O ATOM 1761 CB LYS B 109 -0.080 5.136 53.463 1.00 23.42 C ATOM 1762 CG LYS B 109 1.035 4.653 52.625 1.00 24.08 C ATOM 1763 CD LYS B 109 0.423 4.156 51.321 1.00 25.60 C ATOM 1764 CE LYS B 109 1.397 3.273 50.576 1.00 28.07 C ATOM 1765 NZ LYS B 109 0.898 2.978 49.204 1.00 29.85 N ATOM 1766 N ALA B 110 -1.866 6.437 55.699 1.00 17.30 N ATOM 1767 CA ALA B 110 -3.101 6.301 56.440 1.00 15.19 C ATOM 1768 C ALA B 110 -4.184 6.619 55.438 1.00 13.62 C ATOM 1769 O ALA B 110 -4.205 7.713 54.897 1.00 12.36 O ATOM 1770 CB ALA B 110 -3.127 7.293 57.598 1.00 15.59 C ATOM 1771 N ARG B 111 -5.071 5.663 55.181 1.00 12.63 N ATOM 1772 CA ARG B 111 -6.144 5.832 54.217 1.00 12.60 C ATOM 1773 C ARG B 111 -7.170 6.892 54.582 1.00 13.35 C ATOM 1774 O ARG B 111 -7.608 6.977 55.732 1.00 14.22 O ATOM 1775 CB ARG B 111 -6.827 4.497 53.932 1.00 12.03 C ATOM 1776 CG ARG B 111 -7.753 4.513 52.728 1.00 11.72 C ATOM 1777 CD ARG B 111 -8.131 3.115 52.312 1.00 12.80 C ATOM 1778 NE ARG B 111 -9.203 3.119 51.318 1.00 15.32 N ATOM 1779 CZ ARG B 111 -9.905 2.050 50.951 1.00 15.55 C ATOM 1780 NH1 ARG B 111 -9.665 0.860 51.478 1.00 17.11 N ATOM 1781 NH2 ARG B 111 -10.889 2.184 50.087 1.00 16.30 N ATOM 1782 N LEU B 112 -7.578 7.662 53.572 1.00 12.92 N ATOM 1783 CA LEU B 112 -8.539 8.753 53.695 1.00 12.63 C ATOM 1784 C LEU B 112 -9.784 8.511 52.871 1.00 13.18 C ATOM 1785 O LEU B 112 -9.763 7.758 51.919 1.00 12.36 O ATOM 1786 CB LEU B 112 -7.907 10.044 53.189 1.00 11.86 C ATOM 1787 CG LEU B 112 -6.814 10.700 54.016 1.00 12.73 C ATOM 1788 CD1 LEU B 112 -6.044 11.642 53.143 1.00 14.02 C ATOM 1789 CD2 LEU B 112 -7.406 11.451 55.165 1.00 13.05 C ATOM 1790 N ASP B 113 -10.888 9.121 53.285 1.00 14.24 N ATOM 1791 CA ASP B 113 -12.166 9.059 52.573 1.00 14.07 C ATOM 1792 C ASP B 113 -12.063 10.092 51.433 1.00 13.42 C ATOM 1793 O ASP B 113 -11.551 11.201 51.645 1.00 11.39 O ATOM 1794 CB ASP B 113 -13.266 9.517 53.543 1.00 17.59 C ATOM 1795 CG ASP B 113 -14.669 9.159 53.093 1.00 20.00 C ATOM 1796 OD1 ASP B 113 -15.022 9.338 51.920 1.00 21.56 O ATOM 1797 OD2 ASP B 113 -15.460 8.719 53.952 1.00 25.48 O ATOM 1798 N TRP B 114 -12.591 9.759 50.257 1.00 11.69 N ATOM 1799 CA TRP B 114 -12.588 10.662 49.116 1.00 12.98 C ATOM 1800 C TRP B 114 -13.391 11.941 49.394 1.00 12.76 C ATOM 1801 O TRP B 114 -13.215 12.956 48.737 1.00 12.19 O ATOM 1802 CB TRP B 114 -13.144 9.955 47.863 1.00 12.72 C ATOM 1803 CG TRP B 114 -12.095 9.156 47.122 1.00 12.62 C ATOM 1804 CD1 TRP B 114 -11.997 7.810 47.057 1.00 13.00 C ATOM 1805 CD2 TRP B 114 -10.965 9.675 46.409 1.00 12.99 C ATOM 1806 NE1 TRP B 114 -10.875 7.447 46.356 1.00 13.23 N ATOM 1807 CE2 TRP B 114 -10.220 8.576 45.949 1.00 14.19 C ATOM 1808 CE3 TRP B 114 -10.507 10.966 46.123 1.00 12.91 C ATOM 1809 CZ2 TRP B 114 -9.039 8.720 45.212 1.00 15.10 C ATOM 1810 CZ3 TRP B 114 -9.331 11.111 45.389 1.00 15.28 C ATOM 1811 CH2 TRP B 114 -8.613 9.993 44.942 1.00 15.08 C ATOM 1812 N ASN B 115 -14.299 11.863 50.351 1.00 13.42 N ATOM 1813 CA ASN B 115 -15.136 12.986 50.722 1.00 13.69 C ATOM 1814 C ASN B 115 -14.518 13.871 51.796 1.00 12.84 C ATOM 1815 O ASN B 115 -15.181 14.769 52.291 1.00 12.43 O ATOM 1816 CB ASN B 115 -16.502 12.494 51.191 1.00 17.95 C ATOM 1817 CG ASN B 115 -17.226 11.691 50.123 1.00 22.76 C ATOM 1818 OD1 ASN B 115 -17.091 11.966 48.929 1.00 24.15 O ATOM 1819 ND2 ASN B 115 -17.978 10.656 50.545 1.00 25.86 N ATOM 1820 N THR B 116 -13.266 13.630 52.172 1.00 11.66 N ATOM 1821 CA THR B 116 -12.607 14.480 53.169 1.00 11.51 C ATOM 1822 C THR B 116 -12.509 15.957 52.693 1.00 11.37 C ATOM 1823 O THR B 116 -12.338 16.255 51.507 1.00 11.09 O ATOM 1824 CB THR B 116 -11.158 13.988 53.471 1.00 11.19 C ATOM 1825 OG1 THR B 116 -11.186 12.617 53.874 1.00 13.72 O ATOM 1826 CG2 THR B 116 -10.506 14.813 54.561 1.00 10.19 C ATOM 1827 N ASP B 117 -12.636 16.881 53.631 1.00 11.05 N ATOM 1828 CA ASP B 117 -12.511 18.286 53.318 1.00 10.29 C ATOM 1829 C ASP B 117 -11.057 18.511 52.899 1.00 9.94 C ATOM 1830 O ASP B 117 -10.146 18.222 53.661 1.00 8.47 O ATOM 1831 CB ASP B 117 -12.847 19.094 54.562 1.00 11.66 C ATOM 1832 CG ASP B 117 -12.748 20.556 54.338 1.00 11.28 C ATOM 1833 OD1 ASP B 117 -13.488 21.088 53.504 1.00 13.85 O ATOM 1834 OD2 ASP B 117 -11.910 21.168 54.985 1.00 11.84 O ATOM 1835 N ALA B 118 -10.837 19.043 51.702 1.00 9.91 N ATOM 1836 CA ALA B 118 -9.479 19.247 51.202 1.00 11.51 C ATOM 1837 C ALA B 118 -8.636 20.306 51.913 1.00 12.21 C ATOM 1838 O ALA B 118 -7.434 20.128 52.064 1.00 12.97 O ATOM 1839 CB ALA B 118 -9.489 19.500 49.687 1.00 10.68 C ATOM 1840 N ALA B 119 -9.248 21.393 52.368 1.00 12.18 N ATOM 1841 CA ALA B 119 -8.505 22.457 53.044 1.00 12.66 C ATOM 1842 C ALA B 119 -7.858 21.979 54.333 1.00 12.47 C ATOM 1843 O ALA B 119 -6.885 22.561 54.789 1.00 13.26 O ATOM 1844 CB ALA B 119 -9.411 23.667 53.309 1.00 12.10 C ATOM 1845 N SER B 120 -8.373 20.891 54.895 1.00 13.01 N ATOM 1846 CA SER B 120 -7.841 20.308 56.126 1.00 11.98 C ATOM 1847 C SER B 120 -6.562 19.558 55.861 1.00 11.66 C ATOM 1848 O SER B 120 -5.862 19.182 56.791 1.00 12.53 O ATOM 1849 CB SER B 120 -8.838 19.331 56.744 1.00 12.91 C ATOM 1850 OG SER B 120 -10.007 19.991 57.154 1.00 15.90 O ATOM 1851 N LEU B 121 -6.258 19.348 54.591 1.00 11.24 N ATOM 1852 CA LEU B 121 -5.079 18.603 54.188 1.00 11.57 C ATOM 1853 C LEU B 121 -3.960 19.420 53.560 1.00 11.81 C ATOM 1854 O LEU B 121 -3.011 18.845 53.033 1.00 11.45 O ATOM 1855 CB LEU B 121 -5.488 17.461 53.251 1.00 10.69 C ATOM 1856 CG LEU B 121 -6.299 16.348 53.916 1.00 10.13 C ATOM 1857 CD1 LEU B 121 -6.969 15.527 52.852 1.00 11.51 C ATOM 1858 CD2 LEU B 121 -5.391 15.495 54.777 1.00 10.28 C ATOM 1859 N ILE B 122 -4.054 20.748 53.623 1.00 11.98 N ATOM 1860 CA ILE B 122 -3.026 21.617 53.055 1.00 12.49 C ATOM 1861 C ILE B 122 -1.718 21.285 53.752 1.00 13.01 C ATOM 1862 O ILE B 122 -1.687 21.085 54.948 1.00 13.58 O ATOM 1863 CB ILE B 122 -3.397 23.119 53.220 1.00 12.91 C ATOM 1864 CG1 ILE B 122 -4.547 23.470 52.279 1.00 13.16 C ATOM 1865 CG2 ILE B 122 -2.208 24.024 52.897 1.00 12.49 C ATOM 1866 CD1 ILE B 122 -5.239 24.766 52.642 1.00 13.93 C ATOM 1867 N GLY B 123 -0.652 21.148 52.985 1.00 13.78 N ATOM 1868 CA GLY B 123 0.620 20.799 53.584 1.00 14.86 C ATOM 1869 C GLY B 123 0.865 19.302 53.662 1.00 14.51 C ATOM 1870 O GLY B 123 2.006 18.887 53.829 1.00 15.90 O ATOM 1871 N GLU B 124 -0.172 18.483 53.563 1.00 14.09 N ATOM 1872 CA GLU B 124 0.006 17.036 53.625 1.00 13.79 C ATOM 1873 C GLU B 124 0.333 16.507 52.243 1.00 13.21 C ATOM 1874 O GLU B 124 -0.094 17.079 51.254 1.00 13.69 O ATOM 1875 CB GLU B 124 -1.268 16.347 54.113 1.00 14.07 C ATOM 1876 CG GLU B 124 -1.690 16.688 55.531 1.00 17.53 C ATOM 1877 CD GLU B 124 -0.701 16.237 56.581 1.00 19.10 C ATOM 1878 OE1 GLU B 124 -0.296 15.064 56.576 1.00 20.28 O ATOM 1879 OE2 GLU B 124 -0.343 17.057 57.437 1.00 20.46 O ATOM 1880 N GLU B 125 1.146 15.459 52.180 1.00 12.04 N ATOM 1881 CA GLU B 125 1.490 14.835 50.916 1.00 10.30 C ATOM 1882 C GLU B 125 0.662 13.569 50.857 1.00 9.82 C ATOM 1883 O GLU B 125 0.559 12.846 51.828 1.00 8.71 O ATOM 1884 CB GLU B 125 2.983 14.520 50.826 1.00 10.56 C ATOM 1885 CG GLU B 125 3.868 15.745 50.669 1.00 11.31 C ATOM 1886 CD GLU B 125 3.968 16.574 51.919 1.00 11.17 C ATOM 1887 OE1 GLU B 125 3.986 16.020 53.024 1.00 14.05 O ATOM 1888 OE2 GLU B 125 4.034 17.804 51.812 1.00 12.82 O ATOM 1889 N LEU B 126 0.033 13.342 49.723 1.00 9.69 N ATOM 1890 CA LEU B 126 -0.846 12.205 49.544 1.00 9.89 C ATOM 1891 C LEU B 126 -0.394 11.221 48.482 1.00 9.79 C ATOM 1892 O LEU B 126 0.432 11.518 47.637 1.00 8.80 O ATOM 1893 CB LEU B 126 -2.256 12.693 49.178 1.00 10.25 C ATOM 1894 CG LEU B 126 -2.975 13.772 49.985 1.00 11.13 C ATOM 1895 CD1 LEU B 126 -4.367 13.925 49.409 1.00 10.93 C ATOM 1896 CD2 LEU B 126 -3.051 13.414 51.471 1.00 10.19 C ATOM 1897 N GLN B 127 -0.996 10.046 48.521 1.00 11.75 N ATOM 1898 CA GLN B 127 -0.717 8.999 47.558 1.00 12.13 C ATOM 1899 C GLN B 127 -2.002 8.321 47.130 1.00 11.48 C ATOM 1900 O GLN B 127 -2.829 7.984 47.970 1.00 11.22 O ATOM 1901 CB GLN B 127 0.240 7.971 48.145 1.00 15.18 C ATOM 1902 CG GLN B 127 0.301 6.698 47.330 1.00 20.16 C ATOM 1903 CD GLN B 127 1.644 6.065 47.359 1.00 23.27 C ATOM 1904 OE1 GLN B 127 2.653 6.750 47.358 1.00 26.51 O ATOM 1905 NE2 GLN B 127 1.680 4.748 47.356 1.00 24.66 N ATOM 1906 N VAL B 128 -2.210 8.221 45.818 1.00 11.81 N ATOM 1907 CA VAL B 128 -3.375 7.543 45.246 1.00 10.86 C ATOM 1908 C VAL B 128 -2.888 6.203 44.687 1.00 11.71 C ATOM 1909 O VAL B 128 -1.909 6.159 43.946 1.00 10.22 O ATOM 1910 CB VAL B 128 -4.036 8.381 44.120 1.00 11.04 C ATOM 1911 CG1 VAL B 128 -5.225 7.621 43.507 1.00 10.80 C ATOM 1912 CG2 VAL B 128 -4.500 9.719 44.669 1.00 8.14 C ATOM 1913 N ASP B 129 -3.527 5.114 45.108 1.00 12.73 N ATOM 1914 CA ASP B 129 -3.189 3.758 44.657 1.00 14.00 C ATOM 1915 C ASP B 129 -4.424 3.056 44.147 1.00 14.12 C ATOM 1916 O ASP B 129 -5.544 3.405 44.493 1.00 13.89 O ATOM 1917 CB ASP B 129 -2.680 2.879 45.797 1.00 16.80 C ATOM 1918 CG ASP B 129 -1.282 3.188 46.215 1.00 19.69 C ATOM 1919 OD1 ASP B 129 -0.486 3.676 45.400 1.00 23.38 O ATOM 1920 OD2 ASP B 129 -0.956 2.908 47.383 1.00 23.66 O ATOM 1921 N PHE B 130 -4.220 2.012 43.364 1.00 15.04 N ATOM 1922 CA PHE B 130 -5.344 1.245 42.857 1.00 15.00 C ATOM 1923 C PHE B 130 -5.772 0.243 43.920 1.00 15.40 C ATOM 1924 O PHE B 130 -4.966 -0.208 44.726 1.00 14.62 O ATOM 1925 CB PHE B 130 -4.951 0.417 41.629 1.00 14.03 C ATOM 1926 CG PHE B 130 -4.806 1.203 40.397 1.00 12.65 C ATOM 1927 CD1 PHE B 130 -5.909 1.786 39.814 1.00 11.79 C ATOM 1928 CD2 PHE B 130 -3.558 1.360 39.806 1.00 12.73 C ATOM 1929 CE1 PHE B 130 -5.790 2.517 38.668 1.00 13.03 C ATOM 1930 CE2 PHE B 130 -3.427 2.094 38.654 1.00 12.92 C ATOM 1931 CZ PHE B 130 -4.556 2.676 38.084 1.00 12.93 C ATOM 1932 N LEU B 131 -7.052 -0.105 43.889 1.00 16.09 N ATOM 1933 CA LEU B 131 -7.591 -1.115 44.768 1.00 16.97 C ATOM 1934 C LEU B 131 -7.294 -2.486 44.113 1.00 17.94 C ATOM 1935 O LEU B 131 -7.003 -2.566 42.892 1.00 17.74 O ATOM 1936 CB LEU B 131 -9.088 -0.893 44.928 1.00 15.59 C ATOM 1937 CG LEU B 131 -9.394 0.295 45.826 1.00 16.46 C ATOM 1938 CD1 LEU B 131 -10.863 0.638 45.745 1.00 16.17 C ATOM 1939 CD2 LEU B 131 -8.956 -0.014 47.248 1.00 15.55 C ATOM 1940 OXT LEU B 131 -7.299 -3.488 44.840 1.00 20.33 O TER 1941 LEU B 131 HETATM 1942 MG MG A 171 0.461 24.373 32.026 1.00 10.43 MG HETATM 1943 PG GNP A 170 1.177 27.591 32.183 1.00 11.26 P HETATM 1944 O1G GNP A 170 2.560 27.522 32.104 1.00 8.86 O HETATM 1945 O2G GNP A 170 0.708 28.515 33.185 1.00 9.11 O HETATM 1946 O3G GNP A 170 0.889 26.245 32.873 1.00 8.39 O HETATM 1947 N3B GNP A 170 0.346 27.509 30.817 1.00 9.05 N HETATM 1948 PB GNP A 170 0.484 26.457 29.501 1.00 8.71 P HETATM 1949 O1B GNP A 170 1.595 26.701 28.613 1.00 5.80 O HETATM 1950 O2B GNP A 170 0.420 25.053 29.910 1.00 9.12 O HETATM 1951 O3A GNP A 170 -0.828 26.664 28.725 1.00 7.57 O HETATM 1952 PA GNP A 170 -2.145 25.943 28.660 1.00 10.37 P HETATM 1953 O1A GNP A 170 -2.948 26.043 29.844 1.00 10.46 O HETATM 1954 O2A GNP A 170 -2.016 24.636 28.090 1.00 9.20 O HETATM 1955 O5' GNP A 170 -2.913 26.755 27.652 1.00 9.72 O HETATM 1956 C5' GNP A 170 -3.274 28.163 27.818 1.00 10.91 C HETATM 1957 C4' GNP A 170 -4.510 28.480 27.074 1.00 11.11 C HETATM 1958 O4' GNP A 170 -4.326 28.413 25.630 1.00 12.23 O HETATM 1959 C3' GNP A 170 -5.650 27.554 27.338 1.00 11.73 C HETATM 1960 O3' GNP A 170 -6.876 28.270 27.328 1.00 11.77 O HETATM 1961 C2' GNP A 170 -5.683 26.629 26.163 1.00 12.31 C HETATM 1962 O2' GNP A 170 -6.969 26.110 25.872 1.00 11.55 O HETATM 1963 C1' GNP A 170 -5.288 27.500 25.050 1.00 11.81 C HETATM 1964 N9 GNP A 170 -4.676 26.653 23.974 1.00 13.15 N HETATM 1965 C8 GNP A 170 -3.642 25.754 24.042 1.00 12.33 C HETATM 1966 N7 GNP A 170 -3.185 25.309 22.932 1.00 12.64 N HETATM 1967 C5 GNP A 170 -3.980 25.933 22.030 1.00 12.06 C HETATM 1968 C6 GNP A 170 -3.979 25.850 20.676 1.00 12.27 C HETATM 1969 O6 GNP A 170 -3.180 25.195 20.019 1.00 13.40 O HETATM 1970 N1 GNP A 170 -4.936 26.554 20.074 1.00 10.82 N HETATM 1971 C2 GNP A 170 -5.760 27.397 20.703 1.00 11.48 C HETATM 1972 N2 GNP A 170 -6.733 28.008 20.077 1.00 12.12 N HETATM 1973 N3 GNP A 170 -5.775 27.529 21.989 1.00 12.39 N HETATM 1974 C4 GNP A 170 -4.846 26.791 22.614 1.00 12.84 C HETATM 1975 CA CA B 132 4.118 18.090 54.501 1.00 14.32 CA HETATM 1976 O HOH A 501 -1.701 24.781 32.219 1.00 8.65 O HETATM 1977 O HOH A 502 2.484 23.746 31.839 1.00 6.38 O HETATM 1978 O HOH A 503 -5.148 25.005 31.082 1.00 11.32 O HETATM 1979 O HOH A 504 -5.543 19.479 25.524 1.00 11.22 O HETATM 1980 O HOH A 505 6.068 20.099 36.756 1.00 18.74 O HETATM 1981 O HOH A 511 -0.854 19.626 32.892 1.00 13.63 O HETATM 1982 O HOH A 512 0.952 -0.561 22.297 1.00 29.93 O HETATM 1983 O HOH A 513 6.331 30.317 14.139 1.00 8.70 O HETATM 1984 O HOH A 521 7.461 30.070 25.453 1.00 8.08 O HETATM 1985 O HOH A 522 1.030 33.057 25.895 1.00 14.37 O HETATM 1986 O HOH A 523 -0.659 32.529 23.841 1.00 14.62 O HETATM 1987 O HOH A 524 -0.312 21.610 38.713 1.00 10.23 O HETATM 1988 O HOH A 525 2.539 27.970 38.916 1.00 25.01 O HETATM 1989 O HOH A 526 2.328 28.294 35.323 1.00 7.88 O HETATM 1990 O HOH A 532 -1.157 21.442 34.696 1.00 11.95 O HETATM 1991 O HOH A 533 -0.191 3.841 29.811 1.00 21.70 O HETATM 1992 O HOH A 534 2.778 39.725 20.937 1.00 18.37 O HETATM 1993 O HOH A 535 1.403 25.980 10.347 1.00 19.59 O HETATM 1994 O HOH A 536 -0.982 14.710 15.868 1.00 22.38 O HETATM 1995 O HOH A 537 0.654 31.135 33.215 1.00 19.00 O HETATM 1996 O HOH A 538 -0.928 6.586 31.746 1.00 24.59 O HETATM 1997 O HOH A 539 6.915 -4.734 24.053 1.00 18.84 O HETATM 1998 O HOH A 540 6.038 35.747 27.729 1.00 27.51 O HETATM 1999 O HOH A 541 -0.958 37.756 11.171 1.00 16.59 O HETATM 2000 O HOH A 542 -3.030 17.355 35.730 1.00 16.21 O HETATM 2001 O HOH A 544 8.623 26.212 31.499 1.00 17.23 O HETATM 2002 O HOH A 545 3.585 34.299 28.835 1.00 25.61 O HETATM 2003 O HOH A 546 -0.777 32.882 35.116 1.00 23.98 O HETATM 2004 O HOH A 547 5.854 25.414 40.592 1.00 22.92 O HETATM 2005 O HOH A 550 10.953 13.937 32.766 1.00 25.74 O HETATM 2006 O HOH A 551 -3.322 22.456 35.215 1.00 24.71 O HETATM 2007 O HOH A 552 -11.630 20.138 28.477 1.00 29.52 O HETATM 2008 O HOH A 553 -9.233 27.906 24.556 1.00 24.70 O HETATM 2009 O HOH A 554 8.164 -3.774 21.118 1.00 29.34 O HETATM 2010 O HOH A 555 11.718 25.825 41.808 1.00 31.65 O HETATM 2011 O HOH A 556 -1.554 38.055 18.596 1.00 15.37 O HETATM 2012 O HOH A 557 5.242 22.733 10.805 1.00 19.49 O HETATM 2013 O HOH A 566 13.063 15.344 33.897 1.00 24.58 O HETATM 2014 O HOH A 567 10.742 23.779 35.115 1.00 38.16 O HETATM 2015 O HOH A 568 -4.862 19.134 35.934 1.00 29.79 O HETATM 2016 O HOH A 569 4.220 39.703 23.306 1.00 25.23 O HETATM 2017 O HOH A 570 -9.332 28.107 16.613 1.00 30.75 O HETATM 2018 O HOH A 572 14.032 34.203 13.866 1.00 26.06 O HETATM 2019 O HOH A 573 1.484 23.293 10.972 1.00 21.78 O HETATM 2020 O HOH A 575 15.864 6.055 27.225 1.00 25.65 O HETATM 2021 O HOH A 577 1.598 35.664 26.543 1.00 26.63 O HETATM 2022 O HOH A 578 16.868 18.131 16.495 1.00 28.11 O HETATM 2023 O HOH A 579 5.071 -3.806 15.800 1.00 21.28 O HETATM 2024 O HOH A 583 14.479 15.197 14.326 1.00 31.34 O HETATM 2025 O HOH A 585 -12.478 21.996 30.211 1.00 13.09 O HETATM 2026 O HOH A 586 -5.558 30.684 23.200 1.00 24.18 O HETATM 2027 O HOH B 506 1.544 14.116 54.808 1.00 8.26 O HETATM 2028 O HOH B 507 -9.629 5.725 50.077 1.00 12.77 O HETATM 2029 O HOH B 508 6.803 15.931 48.483 1.00 14.20 O HETATM 2030 O HOH B 509 -1.050 9.653 31.975 1.00 18.62 O HETATM 2031 O HOH B 510 -4.635 22.572 32.598 1.00 14.34 O HETATM 2032 O HOH B 514 -11.966 22.435 51.505 1.00 15.45 O HETATM 2033 O HOH B 515 -7.188 18.311 39.950 1.00 11.09 O HETATM 2034 O HOH B 516 -4.459 -3.051 41.752 1.00 15.30 O HETATM 2035 O HOH B 517 3.200 16.485 55.798 1.00 15.12 O HETATM 2036 O HOH B 518 1.789 19.047 49.914 1.00 20.48 O HETATM 2037 O HOH B 519 -10.880 10.600 55.914 1.00 12.80 O HETATM 2038 O HOH B 520 -7.693 21.603 42.020 1.00 18.72 O HETATM 2039 O HOH B 527 -10.302 19.150 39.903 1.00 18.23 O HETATM 2040 O HOH B 528 -2.527 7.167 33.936 1.00 13.99 O HETATM 2041 O HOH B 529 -7.507 5.174 57.825 1.00 17.21 O HETATM 2042 O HOH B 530 -13.131 16.133 56.499 1.00 12.86 O HETATM 2043 O HOH B 531 4.909 20.190 53.774 1.00 19.48 O HETATM 2044 O HOH B 543 3.035 13.179 57.648 1.00 30.25 O HETATM 2045 O HOH B 548 -13.741 20.358 41.053 1.00 26.18 O HETATM 2046 O HOH B 549 -5.757 20.239 38.237 1.00 39.82 O HETATM 2047 O HOH B 558 0.676 5.194 43.616 1.00 30.29 O HETATM 2048 O HOH B 559 3.551 5.025 41.191 1.00 25.13 O HETATM 2049 O HOH B 560 -12.435 4.399 46.473 1.00 28.14 O HETATM 2050 O HOH B 561 -11.633 4.737 48.834 1.00 24.65 O HETATM 2051 O HOH B 562 -13.876 6.800 49.928 1.00 20.54 O HETATM 2052 O HOH B 563 -1.129 1.589 42.768 1.00 20.87 O HETATM 2053 O HOH B 564 -8.917 4.234 37.066 1.00 25.64 O HETATM 2054 O HOH B 565 -7.603 2.777 35.157 1.00 25.38 O HETATM 2055 O HOH B 571 -3.354 20.275 57.178 1.00 29.86 O HETATM 2056 O HOH B 574 3.525 19.261 56.416 1.00 29.40 O HETATM 2057 O HOH B 576 4.427 23.415 45.769 1.00 33.80 O HETATM 2058 O HOH B 580 -10.791 10.481 31.007 1.00 29.31 O HETATM 2059 O HOH B 581 -5.461 22.363 40.909 1.00 21.08 O HETATM 2060 O HOH B 582 4.716 8.768 41.899 1.00 24.32 O HETATM 2061 O HOH B 584 2.432 21.811 48.456 1.00 33.03 O HETATM 2062 O HOH B 587 -2.944 8.167 61.310 1.00 25.66 O HETATM 2063 O HOH B 588 -8.417 -0.867 41.233 1.00 20.49 O HETATM 2064 O HOH B 589 -12.547 17.683 58.428 1.00 39.15 O CONECT 123 1942 CONECT 266 1942 CONECT 1870 1975 CONECT 1887 1975 CONECT 1888 1975 CONECT 1942 123 266 1946 1950 CONECT 1942 1976 1977 CONECT 1943 1944 1945 1946 1947 CONECT 1944 1943 CONECT 1945 1943 CONECT 1946 1942 1943 CONECT 1947 1943 1948 CONECT 1948 1947 1949 1950 1951 CONECT 1949 1948 CONECT 1950 1942 1948 CONECT 1951 1948 1952 CONECT 1952 1951 1953 1954 1955 CONECT 1953 1952 CONECT 1954 1952 CONECT 1955 1952 1956 CONECT 1956 1955 1957 CONECT 1957 1956 1958 1959 CONECT 1958 1957 1963 CONECT 1959 1957 1960 1961 CONECT 1960 1959 CONECT 1961 1959 1962 1963 CONECT 1962 1961 CONECT 1963 1958 1961 1964 CONECT 1964 1963 1965 1974 CONECT 1965 1964 1966 CONECT 1966 1965 1967 CONECT 1967 1966 1968 1974 CONECT 1968 1967 1969 1970 CONECT 1969 1968 CONECT 1970 1968 1971 CONECT 1971 1970 1972 1973 CONECT 1972 1971 CONECT 1973 1971 1974 CONECT 1974 1964 1967 1973 CONECT 1975 1870 1887 1888 2035 CONECT 1975 2043 2056 CONECT 1976 1942 CONECT 1977 1942 CONECT 2035 1975 CONECT 2043 1975 CONECT 2056 1975 MASTER 314 0 3 9 11 0 11 6 2062 2 46 20 END
Display Options:
Goto PDB code:
3D presentation of molecule is powered by
3Dmol
, which supports all modern browsers and mobile devices via WebGL.
Hold mouse button:
left to rotate,middle to shift,right to zoom
Related entries of code: 1gua
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
3kuc
RCSB PDB
PDBbind
81aa, >3KUC_2|Chain... at 97%
3kud
RCSB PDB
PDBbind
81aa, >3KUD_2|Chain... at 98%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
1e96
RCSB PDB
PDBbind
protein
1efx
RCSB PDB
PDBbind
protein
1ffx
RCSB PDB
PDBbind
protein
1i4d
RCSB PDB
PDBbind
protein
1j2j
RCSB PDB
PDBbind
protein
1kxp
RCSB PDB
PDBbind
protein
1mi5
RCSB PDB
PDBbind
protein
1nf3
RCSB PDB
PDBbind
protein
1p1z
RCSB PDB
PDBbind
protein
1p4l
RCSB PDB
PDBbind
protein
1rv6
RCSB PDB
PDBbind
protein
1shz
RCSB PDB
PDBbind
protein
1t44
RCSB PDB
PDBbind
protein
1uad
RCSB PDB
PDBbind
protein
1vg0
RCSB PDB
PDBbind
protein
1w1w
RCSB PDB
PDBbind
protein
1w72
RCSB PDB
PDBbind
protein
1y4a
RCSB PDB
PDBbind
protein
1zc3
RCSB PDB
PDBbind
protein
1zc4
RCSB PDB
PDBbind
protein
2a78
RCSB PDB
PDBbind
protein
Entry Information
PDB ID
1gua
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
rap1a
Ligand Name
protein
EC.Number
E.C.2.7.1.0
Resolution
2(Å)
Affinity (Kd/Ki/IC50)
Kd=40nM
Release Year
1997
Protein/NA Sequence
Check fasta file
Primary Reference
Nat.Struct.Biol. v3 pp. 723-9, 1996
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P04049
P62834
Entrez Gene ID
NCBI Entrez Gene ID:
5894
5906
ASD
Information of known allosteric effects of PDB entries
This site has been visited
times since Nov 2007.
Copyright ©2007-2024 涓婃捣鐩堣禌鎬濅俊鎭鎶鏈夐檺鍏徃 缃戠珯澶囨鍙凤細
娌狪CP澶2021015625鍙-3
娌叕缃戝畨澶囷細
姝e湪鐢宠涓
Technical Support锛堟妧鏈敮鎸侊級:
yingsaisi@foxmail.com