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7l1f.pdb
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HEADER VIRAL PROTEIN/RNA 14-DEC-20 7L1F
TITLE SARS-COV-2 RDRP IN COMPLEX WITH 4 REMDESIVIR MONOPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA-DIRECTED RNA POLYMERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: POL, RDRP, NON-STRUCTURAL PROTEIN 12, NSP12;
COMPND 5 EC: 2.7.7.48;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NON-STRUCTURAL PROTEIN 8;
COMPND 9 CHAIN: C;
COMPND 10 SYNONYM: NSP8;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: NON-STRUCTURAL PROTEIN 7;
COMPND 14 CHAIN: D;
COMPND 15 SYNONYM: NSP7;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: RNA (5'-R(P*CP*UP*AP*AP*GP*AP*AP*GP*CP*UP*AP*UP*U*(F86)
COMPND 19 *(F86)*(F86)*(F86))-3');
COMPND 20 CHAIN: P;
COMPND 21 ENGINEERED: YES;
COMPND 22 MOL_ID: 5;
COMPND 23 MOLECULE: RNA (5'-
COMPND 24 R(P*AP*UP*UP*UP*UP*AP*AP*UP*AP*GP*CP*UP*UP*CP*UP*UP*AP*G)-3');
COMPND 25 CHAIN: T;
COMPND 26 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS
SOURCE 3 2;
SOURCE 4 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2;
SOURCE 5 ORGANISM_TAXID: 2697049;
SOURCE 6 GENE: REP, 1A-1B;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS
SOURCE 11 2;
SOURCE 12 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2;
SOURCE 13 ORGANISM_TAXID: 2697049;
SOURCE 14 GENE: REP, 1A-1B;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS
SOURCE 19 2;
SOURCE 20 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2;
SOURCE 21 ORGANISM_TAXID: 2697049;
SOURCE 22 GENE: REP, 1A-1B;
SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 25 MOL_ID: 4;
SOURCE 26 SYNTHETIC: YES;
SOURCE 27 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS
SOURCE 28 2;
SOURCE 29 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2;
SOURCE 30 ORGANISM_TAXID: 2697049;
SOURCE 31 MOL_ID: 5;
SOURCE 32 SYNTHETIC: YES;
SOURCE 33 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS
SOURCE 34 2;
SOURCE 35 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2;
SOURCE 36 ORGANISM_TAXID: 2697049
KEYWDS VIRAL PROTEIN, VIRAL PROTEIN-RNA COMPLEX
EXPDTA ELECTRON MICROSCOPY
AUTHOR J.P.K.BRAVO,D.W.TAYLOR
REVDAT 3 06-MAR-24 7L1F 1 LINK
REVDAT 2 26-MAY-21 7L1F 1 JRNL
REVDAT 1 10-FEB-21 7L1F 0
JRNL AUTH J.P.K.BRAVO,T.L.DANGERFIELD,D.W.TAYLOR,K.A.JOHNSON
JRNL TITL REMDESIVIR IS A DELAYED TRANSLOCATION INHIBITOR OF
JRNL TITL 2 SARS-COV-2 REPLICATION.
JRNL REF MOL.CELL V. 81 1548 2021
JRNL REFN ISSN 1097-2765
JRNL PMID 33631104
JRNL DOI 10.1016/J.MOLCEL.2021.01.035
REMARK 2
REMARK 2 RESOLUTION. 3.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.890
REMARK 3 NUMBER OF PARTICLES : 116748
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 7L1F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-20.
REMARK 100 THE DEPOSITION ID IS D_1000253533.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : SARS-COV-2 RDRP COMPLEX WITH
REMARK 245 TEMPLATE:PRIMER AND FOUR RMP;
REMARK 245 RNA-DIRECTED RNA POLYMERASE,
REMARK 245 NON-STRUCTURAL PROTEIN 8, NON-
REMARK 245 STRUCTURAL PROTEIN 7; RNA
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.00
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 8000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, P, T
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 THR A 51
REMARK 465 ASN A 52
REMARK 465 CYS A 53
REMARK 465 CYS A 54
REMARK 465 ARG A 55
REMARK 465 PHE A 56
REMARK 465 GLN A 57
REMARK 465 GLU A 58
REMARK 465 LYS A 59
REMARK 465 ASP A 60
REMARK 465 GLU A 61
REMARK 465 ASP A 62
REMARK 465 ASP A 63
REMARK 465 ASN A 64
REMARK 465 LEU A 65
REMARK 465 ILE A 66
REMARK 465 ASP A 67
REMARK 465 SER A 68
REMARK 465 TYR A 69
REMARK 465 PHE A 70
REMARK 465 VAL A 71
REMARK 465 VAL A 72
REMARK 465 LYS A 73
REMARK 465 ARG A 74
REMARK 465 HIS A 75
REMARK 465 THR A 76
REMARK 465 PHE A 77
REMARK 465 SER A 78
REMARK 465 ASN A 79
REMARK 465 TYR A 80
REMARK 465 GLN A 81
REMARK 465 HIS A 82
REMARK 465 GLU A 83
REMARK 465 PHE A 101
REMARK 465 PHE A 102
REMARK 465 LYS A 103
REMARK 465 PHE A 104
REMARK 465 ARG A 105
REMARK 465 ILE A 106
REMARK 465 ASP A 107
REMARK 465 GLY A 108
REMARK 465 ASP A 109
REMARK 465 MET A 110
REMARK 465 VAL A 111
REMARK 465 PRO A 112
REMARK 465 HIS A 113
REMARK 465 ILE A 114
REMARK 465 SER A 115
REMARK 465 ARG A 116
REMARK 465 GLN A 117
REMARK 465 ARG A 118
REMARK 465 THR A 896
REMARK 465 GLY A 897
REMARK 465 HIS A 898
REMARK 465 MET A 899
REMARK 465 LEU A 900
REMARK 465 ASP A 901
REMARK 465 MET A 902
REMARK 465 TYR A 903
REMARK 465 SER A 904
REMARK 465 VAL A 905
REMARK 465 MET A 906
REMARK 465 LEU A 907
REMARK 465 THR A 908
REMARK 465 ASN A 909
REMARK 465 ASP A 910
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 LEU A 207 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 ASP A 304 CB - CG - OD1 ANGL. DEV. = 11.9 DEGREES
REMARK 500 ASP A 304 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 LYS A 411 CB - CG - CD ANGL. DEV. = 15.8 DEGREES
REMARK 500 ASP A 454 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 VAL A 557 C - N - CA ANGL. DEV. = 15.8 DEGREES
REMARK 500 PRO C 183 C - N - CD ANGL. DEV. = -15.6 DEGREES
REMARK 500 A T 0 C2 - N3 - C4 ANGL. DEV. = 3.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 33 -169.14 -124.44
REMARK 500 THR A 85 56.88 -96.98
REMARK 500 CYS A 139 35.15 -98.81
REMARK 500 ASP A 161 69.20 62.38
REMARK 500 ASP A 221 20.70 -140.58
REMARK 500 SER A 384 35.36 -98.39
REMARK 500 LYS A 426 30.27 -98.61
REMARK 500 THR A 556 -81.80 -96.34
REMARK 500 TYR A 606 39.10 -94.30
REMARK 500 THR A 686 38.27 -99.52
REMARK 500 SER A 709 31.08 -95.73
REMARK 500 ARG A 733 -2.43 -142.39
REMARK 500 SER A 759 -18.67 68.64
REMARK 500 ASP A 760 -26.76 -145.12
REMARK 500 ARG D 21 65.20 60.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR A 556 VAL A 557 148.03
REMARK 500 LEU C 98 ASP C 99 -149.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-23109 RELATED DB: EMDB
REMARK 900 SARS-COV-2 RDRP IN COMPLEX WITH 4 REMDESIVIR MONOPHOSPHATE
DBREF 7L1F A 32 929 UNP P0DTD1 R1AB_SARS2 4424 5321
DBREF 7L1F C 78 191 UNP P0DTD1 R1AB_SARS2 4020 4133
DBREF 7L1F D 2 64 UNP P0DTD1 R1AB_SARS2 3861 3923
DBREF 7L1F P 1 17 PDB 7L1F 7L1F 1 17
DBREF 7L1F T 0 17 PDB 7L1F 7L1F 0 17
SEQRES 1 A 898 TYR ARG ALA PHE ASP ILE TYR ASN ASP LYS VAL ALA GLY
SEQRES 2 A 898 PHE ALA LYS PHE LEU LYS THR ASN CYS CYS ARG PHE GLN
SEQRES 3 A 898 GLU LYS ASP GLU ASP ASP ASN LEU ILE ASP SER TYR PHE
SEQRES 4 A 898 VAL VAL LYS ARG HIS THR PHE SER ASN TYR GLN HIS GLU
SEQRES 5 A 898 GLU THR ILE TYR ASN LEU LEU LYS ASP CYS PRO ALA VAL
SEQRES 6 A 898 ALA LYS HIS ASP PHE PHE LYS PHE ARG ILE ASP GLY ASP
SEQRES 7 A 898 MET VAL PRO HIS ILE SER ARG GLN ARG LEU THR LYS TYR
SEQRES 8 A 898 THR MET ALA ASP LEU VAL TYR ALA LEU ARG HIS PHE ASP
SEQRES 9 A 898 GLU GLY ASN CYS ASP THR LEU LYS GLU ILE LEU VAL THR
SEQRES 10 A 898 TYR ASN CYS CYS ASP ASP ASP TYR PHE ASN LYS LYS ASP
SEQRES 11 A 898 TRP TYR ASP PHE VAL GLU ASN PRO ASP ILE LEU ARG VAL
SEQRES 12 A 898 TYR ALA ASN LEU GLY GLU ARG VAL ARG GLN ALA LEU LEU
SEQRES 13 A 898 LYS THR VAL GLN PHE CYS ASP ALA MET ARG ASN ALA GLY
SEQRES 14 A 898 ILE VAL GLY VAL LEU THR LEU ASP ASN GLN ASP LEU ASN
SEQRES 15 A 898 GLY ASN TRP TYR ASP PHE GLY ASP PHE ILE GLN THR THR
SEQRES 16 A 898 PRO GLY SER GLY VAL PRO VAL VAL ASP SER TYR TYR SER
SEQRES 17 A 898 LEU LEU MET PRO ILE LEU THR LEU THR ARG ALA LEU THR
SEQRES 18 A 898 ALA GLU SER HIS VAL ASP THR ASP LEU THR LYS PRO TYR
SEQRES 19 A 898 ILE LYS TRP ASP LEU LEU LYS TYR ASP PHE THR GLU GLU
SEQRES 20 A 898 ARG LEU LYS LEU PHE ASP ARG TYR PHE LYS TYR TRP ASP
SEQRES 21 A 898 GLN THR TYR HIS PRO ASN CYS VAL ASN CYS LEU ASP ASP
SEQRES 22 A 898 ARG CYS ILE LEU HIS CYS ALA ASN PHE ASN VAL LEU PHE
SEQRES 23 A 898 SER THR VAL PHE PRO PRO THR SER PHE GLY PRO LEU VAL
SEQRES 24 A 898 ARG LYS ILE PHE VAL ASP GLY VAL PRO PHE VAL VAL SER
SEQRES 25 A 898 THR GLY TYR HIS PHE ARG GLU LEU GLY VAL VAL HIS ASN
SEQRES 26 A 898 GLN ASP VAL ASN LEU HIS SER SER ARG LEU SER PHE LYS
SEQRES 27 A 898 GLU LEU LEU VAL TYR ALA ALA ASP PRO ALA MET HIS ALA
SEQRES 28 A 898 ALA SER GLY ASN LEU LEU LEU ASP LYS ARG THR THR CYS
SEQRES 29 A 898 PHE SER VAL ALA ALA LEU THR ASN ASN VAL ALA PHE GLN
SEQRES 30 A 898 THR VAL LYS PRO GLY ASN PHE ASN LYS ASP PHE TYR ASP
SEQRES 31 A 898 PHE ALA VAL SER LYS GLY PHE PHE LYS GLU GLY SER SER
SEQRES 32 A 898 VAL GLU LEU LYS HIS PHE PHE PHE ALA GLN ASP GLY ASN
SEQRES 33 A 898 ALA ALA ILE SER ASP TYR ASP TYR TYR ARG TYR ASN LEU
SEQRES 34 A 898 PRO THR MET CYS ASP ILE ARG GLN LEU LEU PHE VAL VAL
SEQRES 35 A 898 GLU VAL VAL ASP LYS TYR PHE ASP CYS TYR ASP GLY GLY
SEQRES 36 A 898 CYS ILE ASN ALA ASN GLN VAL ILE VAL ASN ASN LEU ASP
SEQRES 37 A 898 LYS SER ALA GLY PHE PRO PHE ASN LYS TRP GLY LYS ALA
SEQRES 38 A 898 ARG LEU TYR TYR ASP SER MET SER TYR GLU ASP GLN ASP
SEQRES 39 A 898 ALA LEU PHE ALA TYR THR LYS ARG ASN VAL ILE PRO THR
SEQRES 40 A 898 ILE THR GLN MET ASN LEU LYS TYR ALA ILE SER ALA LYS
SEQRES 41 A 898 ASN ARG ALA ARG THR VAL ALA GLY VAL SER ILE CYS SER
SEQRES 42 A 898 THR MET THR ASN ARG GLN PHE HIS GLN LYS LEU LEU LYS
SEQRES 43 A 898 SER ILE ALA ALA THR ARG GLY ALA THR VAL VAL ILE GLY
SEQRES 44 A 898 THR SER LYS PHE TYR GLY GLY TRP HIS ASN MET LEU LYS
SEQRES 45 A 898 THR VAL TYR SER ASP VAL GLU ASN PRO HIS LEU MET GLY
SEQRES 46 A 898 TRP ASP TYR PRO LYS CYS ASP ARG ALA MET PRO ASN MET
SEQRES 47 A 898 LEU ARG ILE MET ALA SER LEU VAL LEU ALA ARG LYS HIS
SEQRES 48 A 898 THR THR CYS CYS SER LEU SER HIS ARG PHE TYR ARG LEU
SEQRES 49 A 898 ALA ASN GLU CYS ALA GLN VAL LEU SER GLU MET VAL MET
SEQRES 50 A 898 CYS GLY GLY SER LEU TYR VAL LYS PRO GLY GLY THR SER
SEQRES 51 A 898 SER GLY ASP ALA THR THR ALA TYR ALA ASN SER VAL PHE
SEQRES 52 A 898 ASN ILE CYS GLN ALA VAL THR ALA ASN VAL ASN ALA LEU
SEQRES 53 A 898 LEU SER THR ASP GLY ASN LYS ILE ALA ASP LYS TYR VAL
SEQRES 54 A 898 ARG ASN LEU GLN HIS ARG LEU TYR GLU CYS LEU TYR ARG
SEQRES 55 A 898 ASN ARG ASP VAL ASP THR ASP PHE VAL ASN GLU PHE TYR
SEQRES 56 A 898 ALA TYR LEU ARG LYS HIS PHE SER MET MET ILE LEU SER
SEQRES 57 A 898 ASP ASP ALA VAL VAL CYS PHE ASN SER THR TYR ALA SER
SEQRES 58 A 898 GLN GLY LEU VAL ALA SER ILE LYS ASN PHE LYS SER VAL
SEQRES 59 A 898 LEU TYR TYR GLN ASN ASN VAL PHE MET SER GLU ALA LYS
SEQRES 60 A 898 CYS TRP THR GLU THR ASP LEU THR LYS GLY PRO HIS GLU
SEQRES 61 A 898 PHE CYS SER GLN HIS THR MET LEU VAL LYS GLN GLY ASP
SEQRES 62 A 898 ASP TYR VAL TYR LEU PRO TYR PRO ASP PRO SER ARG ILE
SEQRES 63 A 898 LEU GLY ALA GLY CYS PHE VAL ASP ASP ILE VAL LYS THR
SEQRES 64 A 898 ASP GLY THR LEU MET ILE GLU ARG PHE VAL SER LEU ALA
SEQRES 65 A 898 ILE ASP ALA TYR PRO LEU THR LYS HIS PRO ASN GLN GLU
SEQRES 66 A 898 TYR ALA ASP VAL PHE HIS LEU TYR LEU GLN TYR ILE ARG
SEQRES 67 A 898 LYS LEU HIS ASP GLU LEU THR GLY HIS MET LEU ASP MET
SEQRES 68 A 898 TYR SER VAL MET LEU THR ASN ASP ASN THR SER ARG TYR
SEQRES 69 A 898 TRP GLU PRO GLU PHE TYR GLU ALA MET TYR THR PRO HIS
SEQRES 70 A 898 THR
SEQRES 1 C 114 ASP LYS ARG ALA LYS VAL THR SER ALA MET GLN THR MET
SEQRES 2 C 114 LEU PHE THR MET LEU ARG LYS LEU ASP ASN ASP ALA LEU
SEQRES 3 C 114 ASN ASN ILE ILE ASN ASN ALA ARG ASP GLY CYS VAL PRO
SEQRES 4 C 114 LEU ASN ILE ILE PRO LEU THR THR ALA ALA LYS LEU MET
SEQRES 5 C 114 VAL VAL ILE PRO ASP TYR ASN THR TYR LYS ASN THR CYS
SEQRES 6 C 114 ASP GLY THR THR PHE THR TYR ALA SER ALA LEU TRP GLU
SEQRES 7 C 114 ILE GLN GLN VAL VAL ASP ALA ASP SER LYS ILE VAL GLN
SEQRES 8 C 114 LEU SER GLU ILE SER MET ASP ASN SER PRO ASN LEU ALA
SEQRES 9 C 114 TRP PRO LEU ILE VAL THR ALA LEU ARG ALA
SEQRES 1 D 63 LYS MET SER ASP VAL LYS CYS THR SER VAL VAL LEU LEU
SEQRES 2 D 63 SER VAL LEU GLN GLN LEU ARG VAL GLU SER SER SER LYS
SEQRES 3 D 63 LEU TRP ALA GLN CYS VAL GLN LEU HIS ASN ASP ILE LEU
SEQRES 4 D 63 LEU ALA LYS ASP THR THR GLU ALA PHE GLU LYS MET VAL
SEQRES 5 D 63 SER LEU LEU SER VAL LEU LEU SER MET GLN GLY
SEQRES 1 P 17 C U A A G A A G C U A U U
SEQRES 2 P 17 F86 F86 F86 F86
SEQRES 1 T 18 A U U U U A A U A G C U U
SEQRES 2 T 18 C U U A G
HET F86 P 14 24
HET F86 P 15 24
HET F86 P 16 24
HET F86 P 17 24
HETNAM F86 [(2~{R},3~{S},4~{R},5~{R})-5-(4-AZANYLPYRROLO[2,1-F][1,
HETNAM 2 F86 2,4]TRIAZIN-7-YL)-5-CYANO-3,4-BIS(OXIDANYL)OXOLAN-2-
HETNAM 3 F86 YL]METHYL DIHYDROGEN PHOSPHATE
HETSYN F86 REMDESIVIR, BOUND FORM
FORMUL 4 F86 4(C12 H14 N5 O7 P)
HELIX 1 AA1 THR A 123 ALA A 130 1 8
HELIX 2 AA2 CYS A 139 TYR A 149 1 11
HELIX 3 AA3 ASP A 170 ALA A 176 1 7
HELIX 4 AA4 LEU A 178 GLY A 200 1 23
HELIX 5 AA5 THR A 206 GLN A 210 5 5
HELIX 6 AA6 VAL A 234 ARG A 249 1 16
HELIX 7 AA7 THR A 276 PHE A 287 1 12
HELIX 8 AA8 ARG A 305 SER A 318 1 14
HELIX 9 AA9 SER A 367 ASP A 377 1 11
HELIX 10 AB1 PRO A 378 ALA A 383 1 6
HELIX 11 AB2 ASN A 416 VAL A 424 1 9
HELIX 12 AB3 ASN A 447 ASP A 454 1 8
HELIX 13 AB4 TYR A 455 ASN A 459 5 5
HELIX 14 AB5 ILE A 466 VAL A 476 1 11
HELIX 15 AB6 ASP A 477 PHE A 480 5 4
HELIX 16 AB7 ASN A 489 VAL A 493 5 5
HELIX 17 AB8 PRO A 505 TRP A 509 5 5
HELIX 18 AB9 ARG A 513 SER A 518 1 6
HELIX 19 AC1 SER A 520 THR A 531 1 12
HELIX 20 AC2 SER A 561 ALA A 580 1 20
HELIX 21 AC3 GLY A 596 TYR A 606 1 11
HELIX 22 AC4 PRO A 627 LEU A 638 1 12
HELIX 23 AC5 SER A 647 LEU A 663 1 17
HELIX 24 AC6 THR A 686 SER A 709 1 24
HELIX 25 AC7 ASP A 717 ARG A 733 1 17
HELIX 26 AC8 ASP A 738 HIS A 752 1 15
HELIX 27 AC9 SER A 778 GLN A 789 1 12
HELIX 28 AD1 ASP A 833 CYS A 842 1 10
HELIX 29 AD2 ILE A 847 THR A 850 5 4
HELIX 30 AD3 ASP A 851 ALA A 866 1 16
HELIX 31 AD4 ASN A 874 LEU A 895 1 22
HELIX 32 AD5 GLU A 917 TYR A 925 1 9
HELIX 33 AD6 LYS C 79 MET C 94 1 16
HELIX 34 AD7 ASN C 100 ASN C 108 1 9
HELIX 35 AD8 PRO C 116 ASN C 118 5 3
HELIX 36 AD9 ILE C 119 ALA C 125 1 7
HELIX 37 AE1 ASP C 134 CYS C 142 1 9
HELIX 38 AE2 SER C 173 SER C 177 5 5
HELIX 39 AE3 MET D 3 GLN D 19 1 17
HELIX 40 AE4 SER D 25 LEU D 40 1 16
HELIX 41 AE5 THR D 45 MET D 62 1 18
SHEET 1 AA1 2 ALA A 34 TYR A 38 0
SHEET 2 AA1 2 ALA A 43 LYS A 47 -1 O GLY A 44 N ILE A 37
SHEET 1 AA2 3 ILE A 223 GLN A 224 0
SHEET 2 AA2 3 ILE A 201 VAL A 204 -1 N VAL A 202 O ILE A 223
SHEET 3 AA2 3 PRO A 232 VAL A 233 1 O VAL A 233 N GLY A 203
SHEET 1 AA3 3 GLY A 327 PRO A 328 0
SHEET 2 AA3 3 GLY A 345 HIS A 347 -1 O HIS A 347 N GLY A 327
SHEET 3 AA3 3 VAL A 353 HIS A 355 -1 O VAL A 354 N TYR A 346
SHEET 1 AA4 2 LYS A 332 VAL A 335 0
SHEET 2 AA4 2 VAL A 338 VAL A 341 -1 O PHE A 340 N ILE A 333
SHEET 1 AA5 7 LEU A 673 TYR A 674 0
SHEET 2 AA5 7 SER A 397 ALA A 400 -1 N VAL A 398 O LEU A 673
SHEET 3 AA5 7 ASN A 386 LEU A 389 -1 N ASN A 386 O ALA A 400
SHEET 4 AA5 7 LYS C 127 ILE C 132 1 O MET C 129 N LEU A 389
SHEET 5 AA5 7 LEU C 184 ARG C 190 -1 O LEU C 184 N ILE C 132
SHEET 6 AA5 7 LEU C 153 VAL C 160 -1 N VAL C 160 O ILE C 185
SHEET 7 AA5 7 THR C 146 THR C 148 -1 N PHE C 147 O TRP C 154
SHEET 1 AA6 2 ASN A 414 PHE A 415 0
SHEET 2 AA6 2 PHE A 843 VAL A 844 -1 O VAL A 844 N ASN A 414
SHEET 1 AA7 3 PRO A 612 LEU A 614 0
SHEET 2 AA7 3 ASP A 761 ASN A 767 -1 O PHE A 766 N HIS A 613
SHEET 3 AA7 3 PHE A 753 LEU A 758 -1 N LEU A 758 O ASP A 761
SHEET 1 AA8 2 HIS A 816 THR A 817 0
SHEET 2 AA8 2 PRO A 830 TYR A 831 -1 O TYR A 831 N HIS A 816
SHEET 1 AA9 2 VAL A 820 GLN A 822 0
SHEET 2 AA9 2 ASP A 825 VAL A 827 -1 O VAL A 827 N VAL A 820
LINK O3' U P 13 P1 F86 P 14 1555 1555 1.56
LINK O3 F86 P 14 P1 F86 P 15 1555 1555 1.56
LINK O3 F86 P 15 P1 F86 P 16 1555 1555 1.56
LINK O3 F86 P 16 P1 F86 P 17 1555 1555 1.56
CISPEP 1 PHE A 504 PRO A 505 0 -2.21
CISPEP 2 TRP C 182 PRO C 183 0 -16.52
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
ATOM 1 N TYR A 32 185.062 195.073 207.225 1.00 98.85 N
ATOM 2 CA TYR A 32 184.200 194.774 206.082 1.00 98.85 C
ATOM 3 C TYR A 32 184.019 193.283 205.826 1.00 98.85 C
ATOM 4 O TYR A 32 184.947 192.590 205.417 1.00 98.85 O
ATOM 5 CB TYR A 32 184.727 195.445 204.809 1.00 98.85 C
ATOM 6 CG TYR A 32 184.632 196.959 204.755 1.00 98.85 C
ATOM 7 CD1 TYR A 32 183.827 197.669 205.648 1.00 98.85 C
ATOM 8 CD2 TYR A 32 185.341 197.677 203.789 1.00 98.85 C
ATOM 9 CE1 TYR A 32 183.728 199.048 205.584 1.00 98.85 C
ATOM 10 CE2 TYR A 32 185.256 199.065 203.720 1.00 98.85 C
ATOM 11 CZ TYR A 32 184.448 199.739 204.624 1.00 98.85 C
ATOM 12 OH TYR A 32 184.355 201.111 204.567 1.00 98.85 O
ATOM 13 N ARG A 33 182.804 192.805 206.078 1.00101.51 N
ATOM 14 CA ARG A 33 182.365 191.442 205.809 1.00101.51 C
ATOM 15 C ARG A 33 181.120 191.509 204.924 1.00101.51 C
ATOM 16 O ARG A 33 180.767 192.566 204.397 1.00101.51 O
ATOM 17 CB ARG A 33 182.084 190.679 207.108 1.00101.51 C
ATOM 18 CG ARG A 33 183.184 190.755 208.157 1.00101.51 C
ATOM 19 CD ARG A 33 184.431 190.001 207.716 1.00101.51 C
ATOM 20 NE ARG A 33 185.495 190.074 208.712 1.00101.51 N
ATOM 21 CZ ARG A 33 185.616 189.248 209.746 1.00101.51 C
ATOM 22 NH1 ARG A 33 184.744 188.266 209.926 1.00101.51 N
ATOM 23 NH2 ARG A 33 186.619 189.399 210.600 1.00101.51 N
ATOM 24 N ALA A 34 180.452 190.371 204.761 1.00103.07 N
ATOM 25 CA ALA A 34 179.235 190.287 203.966 1.00103.07 C
ATOM 26 C ALA A 34 178.071 189.835 204.836 1.00103.07 C
ATOM 27 O ALA A 34 178.229 188.967 205.699 1.00103.07 O
ATOM 28 CB ALA A 34 179.406 189.327 202.793 1.00103.07 C
ATOM 29 N PHE A 35 176.902 190.430 204.604 1.00 98.97 N
ATOM 30 CA PHE A 35 175.719 190.179 205.412 1.00 98.97 C
ATOM 31 C PHE A 35 174.504 190.028 204.505 1.00 98.97 C
ATOM 32 O PHE A 35 174.429 190.644 203.439 1.00 98.97 O
ATOM 33 CB PHE A 35 175.485 191.313 206.419 1.00 98.97 C
ATOM 34 CG PHE A 35 176.629 191.530 207.364 1.00 98.97 C
ATOM 35 CD1 PHE A 35 177.573 192.522 207.114 1.00 98.97 C
ATOM 36 CD2 PHE A 35 176.773 190.731 208.493 1.00 98.97 C
ATOM 37 CE1 PHE A 35 178.642 192.722 207.983 1.00 98.97 C
ATOM 38 CE2 PHE A 35 177.836 190.919 209.370 1.00 98.97 C
ATOM 39 CZ PHE A 35 178.771 191.917 209.112 1.00 98.97 C
ATOM 40 N ASP A 36 173.552 189.199 204.938 1.00 95.01 N
ATOM 41 CA ASP A 36 172.280 189.007 204.244 1.00 95.01 C
ATOM 42 C ASP A 36 171.190 189.694 205.058 1.00 95.01 C
ATOM 43 O ASP A 36 170.910 189.293 206.191 1.00 95.01 O
ATOM 44 CB ASP A 36 171.970 187.523 204.072 1.00 95.01 C
ATOM 45 CG ASP A 36 170.883 187.271 203.047 1.00 95.01 C
ATOM 46 OD1 ASP A 36 170.535 188.212 202.302 1.00 95.01 O
ATOM 47 OD2 ASP A 36 170.371 186.133 202.988 1.00 95.01 O
ATOM 48 N ILE A 37 170.570 190.720 204.484 1.00 90.08 N
ATOM 49 CA ILE A 37 169.704 191.627 205.226 1.00 90.08 C
ATOM 50 C ILE A 37 168.287 191.505 204.679 1.00 90.08 C
ATOM 51 O ILE A 37 168.082 191.549 203.461 1.00 90.08 O
ATOM 52 CB ILE A 37 170.213 193.082 205.138 1.00 90.08 C
ATOM 53 CG1 ILE A 37 171.670 193.195 205.605 1.00 90.08 C
ATOM 54 CG2 ILE A 37 169.360 194.035 205.973 1.00 90.08 C
ATOM 55 CD1 ILE A 37 171.916 192.745 207.031 1.00 90.08 C
ATOM 56 N TYR A 38 167.317 191.329 205.578 1.00 89.44 N
ATOM 57 CA TYR A 38 165.897 191.479 205.261 1.00 89.44 C
ATOM 58 C TYR A 38 165.302 192.457 206.264 1.00 89.44 C
ATOM 59 O TYR A 38 164.788 192.062 207.313 1.00 89.44 O
ATOM 60 CB TYR A 38 165.158 190.138 205.263 1.00 89.44 C
ATOM 61 CG TYR A 38 163.711 190.257 204.820 1.00 89.44 C
ATOM 62 CD1 TYR A 38 163.393 190.524 203.496 1.00 89.44 C
ATOM 63 CD2 TYR A 38 162.664 190.072 205.728 1.00 89.44 C
ATOM 64 CE1 TYR A 38 162.082 190.633 203.073 1.00 89.44 C
ATOM 65 CE2 TYR A 38 161.333 190.175 205.317 1.00 89.44 C
ATOM 66 CZ TYR A 38 161.058 190.459 203.987 1.00 89.44 C
ATOM 67 OH TYR A 38 159.750 190.565 203.570 1.00 89.44 O
ATOM 68 N ASN A 39 165.382 193.736 205.947 1.00 92.75 N
ATOM 69 CA ASN A 39 164.711 194.769 206.711 1.00 92.75 C
ATOM 70 C ASN A 39 163.702 195.457 205.806 1.00 92.75 C
ATOM 71 O ASN A 39 163.607 195.166 204.613 1.00 92.75 O
ATOM 72 CB ASN A 39 165.707 195.783 207.278 1.00 92.75 C
ATOM 73 CG ASN A 39 166.590 195.194 208.351 1.00 92.75 C
ATOM 74 OD1 ASN A 39 166.325 194.106 208.857 1.00 92.75 O
ATOM 75 ND2 ASN A 39 167.656 195.906 208.698 1.00 92.75 N
ATOM 76 N ASP A 40 162.949 196.386 206.386 1.00 99.99 N
ATOM 77 CA ASP A 40 162.014 197.181 205.606 1.00 99.99 C
ATOM 78 C ASP A 40 162.708 198.247 204.771 1.00 99.99 C
ATOM 79 O ASP A 40 162.165 198.664 203.743 1.00 99.99 O
ATOM 80 CB ASP A 40 160.989 197.835 206.534 1.00 99.99 C
ATOM 81 CG ASP A 40 161.640 198.599 207.673 1.00 99.99 C
ATOM 82 OD1 ASP A 40 162.818 198.322 207.988 1.00 99.99 O
ATOM 83 OD2 ASP A 40 160.976 199.489 208.245 1.00 99.99 O
ATOM 84 N LYS A 41 163.884 198.698 205.188 1.00 95.11 N
ATOM 85 CA LYS A 41 164.581 199.773 204.479 1.00 95.11 C
ATOM 86 C LYS A 41 165.381 199.220 203.303 1.00 95.11 C
ATOM 87 O LYS A 41 165.091 199.523 202.143 1.00 95.11 O
ATOM 88 CB LYS A 41 165.489 200.524 205.453 1.00 95.11 C
ATOM 89 CG LYS A 41 164.759 201.194 206.604 1.00 95.11 C
ATOM 90 CD LYS A 41 163.885 202.335 206.123 1.00 95.11 C
ATOM 91 CE LYS A 41 163.227 203.042 207.296 1.00 95.11 C
ATOM 92 NZ LYS A 41 162.326 204.141 206.858 1.00 95.11 N
ATOM 93 N VAL A 42 166.392 198.403 203.598 1.00 89.87 N
ATOM 94 CA VAL A 42 167.357 197.911 202.621 1.00 89.87 C
ATOM 95 C VAL A 42 167.325 196.391 202.658 1.00 89.87 C
ATOM 96 O VAL A 42 167.432 195.794 203.736 1.00 89.87 O
ATOM 97 CB VAL A 42 168.783 198.425 202.920 1.00 89.87 C
ATOM 98 CG1 VAL A 42 169.786 197.919 201.888 1.00 89.87 C
ATOM 99 CG2 VAL A 42 168.839 199.953 202.991 1.00 89.87 C
ATOM 100 N ALA A 43 167.180 195.764 201.495 1.00 86.36 N
ATOM 101 CA ALA A 43 167.259 194.318 201.381 1.00 86.36 C
ATOM 102 C ALA A 43 168.293 193.948 200.331 1.00 86.36 C
ATOM 103 O ALA A 43 168.406 194.617 199.301 1.00 86.36 O
ATOM 104 CB ALA A 43 165.903 193.718 201.017 1.00 86.36 C
ATOM 105 N GLY A 44 169.049 192.893 200.589 1.00 89.62 N
ATOM 106 CA GLY A 44 169.992 192.405 199.606 1.00 89.62 C
ATOM 107 C GLY A 44 171.124 191.643 200.264 1.00 89.62 C
ATOM 108 O GLY A 44 171.021 191.223 201.412 1.00 89.62 O
ATOM 109 N PHE A 45 172.203 191.478 199.497 1.00 85.90 N
ATOM 110 CA PHE A 45 173.396 190.749 199.924 1.00 85.90 C
ATOM 111 C PHE A 45 174.619 191.565 199.516 1.00 85.90 C
ATOM 112 O PHE A 45 175.069 191.473 198.371 1.00 85.90 O
ATOM 113 CB PHE A 45 173.437 189.363 199.296 1.00 85.90 C
ATOM 114 CG PHE A 45 174.416 188.438 199.943 1.00 85.90 C
ATOM 115 CD1 PHE A 45 174.181 187.959 201.227 1.00 85.90 C
ATOM 116 CD2 PHE A 45 175.573 188.053 199.278 1.00 85.90 C
ATOM 117 CE1 PHE A 45 175.072 187.100 201.839 1.00 85.90 C
ATOM 118 CE2 PHE A 45 176.481 187.192 199.885 1.00 85.90 C
ATOM 119 CZ PHE A 45 176.226 186.720 201.171 1.00 85.90 C
ATOM 120 N ALA A 46 175.170 192.345 200.443 1.00 89.73 N
ATOM 121 CA ALA A 46 176.256 193.251 200.101 1.00 89.73 C
ATOM 122 C ALA A 46 177.137 193.494 201.315 1.00 89.73 C
ATOM 123 O ALA A 46 176.779 193.154 202.444 1.00 89.73 O
ATOM 124 CB ALA A 46 175.725 194.584 199.561 1.00 89.73 C
ATOM 125 N LYS A 47 178.315 194.062 201.058 1.00 92.06 N
ATOM 126 CA LYS A 47 179.188 194.534 202.122 1.00 92.06 C
ATOM 127 C LYS A 47 178.579 195.735 202.832 1.00 92.06 C
ATOM 128 O LYS A 47 177.791 196.490 202.262 1.00 92.06 O
ATOM 129 CB LYS A 47 180.555 194.930 201.574 1.00 92.06 C
ATOM 130 CG LYS A 47 181.399 193.809 201.002 1.00 92.06 C
ATOM 131 CD LYS A 47 182.826 194.311 200.788 1.00 92.06 C
ATOM 132 CE LYS A 47 183.735 193.254 200.193 1.00 92.06 C
ATOM 133 NZ LYS A 47 185.166 193.646 200.274 1.00 92.06 N
ATOM 134 N PHE A 48 178.951 195.901 204.095 1.00 97.70 N
ATOM 135 CA PHE A 48 178.531 197.045 204.887 1.00 97.70 C
ATOM 136 C PHE A 48 179.685 197.481 205.771 1.00 97.70 C
ATOM 137 O PHE A 48 180.723 196.822 205.844 1.00 97.70 O
ATOM 138 CB PHE A 48 177.311 196.735 205.763 1.00 97.70 C
ATOM 139 CG PHE A 48 176.054 196.479 204.991 1.00 97.70 C
ATOM 140 CD1 PHE A 48 175.645 195.176 204.726 1.00 97.70 C
ATOM 141 CD2 PHE A 48 175.277 197.540 204.533 1.00 97.70 C
ATOM 142 CE1 PHE A 48 174.479 194.929 204.009 1.00 97.70 C
ATOM 143 CE2 PHE A 48 174.108 197.307 203.817 1.00 97.70 C
ATOM 144 CZ PHE A 48 173.710 195.998 203.556 1.00 97.70 C
ATOM 145 N LEU A 49 179.485 198.597 206.460 1.00101.03 N
ATOM 146 CA LEU A 49 180.428 199.100 207.451 1.00101.03 C
ATOM 147 C LEU A 49 179.918 198.721 208.836 1.00101.03 C
ATOM 148 O LEU A 49 178.860 199.193 209.264 1.00101.03 O
ATOM 149 CB LEU A 49 180.589 200.613 207.317 1.00101.03 C
ATOM 150 CG LEU A 49 181.345 201.393 208.399 1.00101.03 C
ATOM 151 CD1 LEU A 49 182.785 200.942 208.559 1.00101.03 C
ATOM 152 CD2 LEU A 49 181.279 202.884 208.098 1.00101.03 C
ATOM 153 N LYS A 50 180.666 197.872 209.533 1.00102.21 N
ATOM 154 CA LYS A 50 180.312 197.488 210.896 1.00102.21 C
ATOM 155 C LYS A 50 181.532 197.443 211.801 1.00102.21 C
ATOM 156 O LYS A 50 181.509 197.952 212.920 0.00102.21 O
ATOM 157 CB LYS A 50 179.603 196.133 210.913 1.00102.21 C
ATOM 158 CG LYS A 50 178.101 196.214 210.681 1.00102.21 C
ATOM 159 CD LYS A 50 177.435 194.859 210.852 1.00102.21 C
ATOM 160 CE LYS A 50 175.944 194.933 210.564 1.00102.21 C
ATOM 161 NZ LYS A 50 175.266 193.626 210.789 1.00102.21 N
ATOM 162 N GLU A 84 168.486 187.339 224.205 1.00 69.39 N
ATOM 163 CA GLU A 84 167.474 187.062 225.211 1.00 69.39 C
ATOM 164 C GLU A 84 167.922 185.903 226.074 1.00 69.39 C
ATOM 165 O GLU A 84 169.056 185.446 225.962 1.00 69.39 O
ATOM 166 CB GLU A 84 166.135 186.743 224.557 1.00 69.39 C
ATOM 167 CG GLU A 84 165.476 187.908 223.865 1.00 69.39 C
ATOM 168 CD GLU A 84 164.673 187.475 222.664 1.00 69.39 C
ATOM 169 OE1 GLU A 84 165.003 186.426 222.081 1.00 69.39 O
ATOM 170 OE2 GLU A 84 163.709 188.175 222.303 1.00 69.39 O
ATOM 171 N THR A 85 167.031 185.438 226.942 1.00 78.20 N
ATOM 172 CA THR A 85 167.267 184.220 227.715 1.00 78.20 C
ATOM 173 C THR A 85 166.599 183.016 227.050 1.00 78.20 C
ATOM 174 O THR A 85 165.763 182.324 227.634 1.00 78.20 O
ATOM 175 CB THR A 85 166.780 184.394 229.147 1.00 78.20 C
ATOM 176 OG1 THR A 85 165.351 184.315 229.174 1.00 78.20 O
ATOM 177 CG2 THR A 85 167.223 185.733 229.697 1.00 78.20 C
ATOM 178 N ILE A 86 166.968 182.783 225.789 1.00 74.89 N
ATOM 179 CA ILE A 86 166.722 181.499 225.143 1.00 74.89 C
ATOM 180 C ILE A 86 167.942 180.600 225.212 1.00 74.89 C
ATOM 181 O ILE A 86 167.864 179.433 224.794 1.00 74.89 O
ATOM 182 CB ILE A 86 166.279 181.672 223.675 1.00 74.89 C
ATOM 183 CG1 ILE A 86 167.464 182.021 222.780 1.00 74.89 C
ATOM 184 CG2 ILE A 86 165.231 182.751 223.566 1.00 74.89 C
ATOM 185 CD1 ILE A 86 167.199 181.787 221.338 1.00 74.89 C
ATOM 186 N TYR A 87 169.061 181.104 225.739 1.00 82.61 N
ATOM 187 CA TYR A 87 170.295 180.335 225.824 1.00 82.61 C
ATOM 188 C TYR A 87 170.196 179.227 226.863 1.00 82.61 C
ATOM 189 O TYR A 87 170.808 178.167 226.696 1.00 82.61 O
ATOM 190 CB TYR A 87 171.463 181.277 226.134 1.00 82.61 C
ATOM 191 CG TYR A 87 172.778 180.582 226.418 1.00 82.61 C
ATOM 192 CD1 TYR A 87 173.478 179.934 225.400 1.00 82.61 C
ATOM 193 CD2 TYR A 87 173.309 180.560 227.710 1.00 82.61 C
ATOM 194 CE1 TYR A 87 174.680 179.288 225.658 1.00 82.61 C
ATOM 195 CE2 TYR A 87 174.509 179.915 227.978 1.00 82.61 C
ATOM 196 CZ TYR A 87 175.184 179.285 226.947 1.00 82.61 C
ATOM 197 OH TYR A 87 176.371 178.648 227.210 1.00 82.61 O
ATOM 198 N ASN A 88 169.381 179.416 227.896 1.00 79.34 N
ATOM 199 CA ASN A 88 169.193 178.403 228.923 1.00 79.34 C
ATOM 200 C ASN A 88 168.123 177.376 228.563 1.00 79.34 C
ATOM 201 O ASN A 88 167.814 176.509 229.385 1.00 79.34 O
ATOM 202 CB ASN A 88 168.862 179.071 230.251 1.00 79.34 C
ATOM 203 CG ASN A 88 169.915 180.068 230.662 1.00 79.34 C
ATOM 204 OD1 ASN A 88 170.836 180.354 229.900 1.00 79.34 O
ATOM 205 ND2 ASN A 88 169.789 180.605 231.869 1.00 79.34 N
ATOM 206 N LEU A 89 167.548 177.464 227.364 1.00 79.06 N
ATOM 207 CA LEU A 89 166.781 176.388 226.752 1.00 79.06 C
ATOM 208 C LEU A 89 167.662 175.485 225.900 1.00 79.06 C
ATOM 209 O LEU A 89 167.501 174.261 225.918 1.00 79.06 O
ATOM 210 CB LEU A 89 165.661 176.972 225.891 1.00 79.06 C
ATOM 211 CG LEU A 89 164.705 176.000 225.209 1.00 79.06 C
ATOM 212 CD1 LEU A 89 163.938 175.192 226.242 1.00 79.06 C
ATOM 213 CD2 LEU A 89 163.756 176.755 224.297 1.00 79.06 C
ATOM 214 N LEU A 90 168.608 176.070 225.167 1.00 78.06 N
ATOM 215 CA LEU A 90 169.492 175.341 224.268 1.00 78.06 C
ATOM 216 C LEU A 90 170.889 175.163 224.847 1.00 78.06 C
ATOM 217 O LEU A 90 171.858 175.039 224.092 1.00 78.06 O
ATOM 218 CB LEU A 90 169.569 176.058 222.924 1.00 78.06 C
ATOM 219 CG LEU A 90 168.270 176.062 222.132 1.00 78.06 C
ATOM 220 CD1 LEU A 90 168.378 176.996 220.955 1.00 78.06 C
ATOM 221 CD2 LEU A 90 167.927 174.657 221.673 1.00 78.06 C
ATOM 222 N LYS A 91 171.017 175.149 226.176 1.00 85.58 N
ATOM 223 CA LYS A 91 172.333 175.102 226.804 1.00 85.58 C
ATOM 224 C LYS A 91 172.964 173.716 226.781 1.00 85.58 C
ATOM 225 O LYS A 91 174.174 173.600 226.999 1.00 85.58 O
ATOM 226 CB LYS A 91 172.255 175.588 228.255 1.00 85.58 C
ATOM 227 CG LYS A 91 171.383 174.738 229.165 1.00 85.58 C
ATOM 228 CD LYS A 91 171.567 175.130 230.623 1.00 85.58 C
ATOM 229 CE LYS A 91 170.411 174.644 231.480 1.00 85.58 C
ATOM 230 NZ LYS A 91 169.140 175.345 231.150 1.00 85.58 N
ATOM 231 N ASP A 92 172.186 172.671 226.525 1.00 85.79 N
ATOM 232 CA ASP A 92 172.677 171.302 226.547 1.00 85.79 C
ATOM 233 C ASP A 92 172.576 170.666 225.167 1.00 85.79 C
ATOM 234 O ASP A 92 172.198 169.503 225.020 1.00 85.79 O
ATOM 235 CB ASP A 92 171.926 170.477 227.588 1.00 85.79 C
ATOM 236 CG ASP A 92 170.435 170.738 227.571 1.00 85.79 C
ATOM 237 OD1 ASP A 92 169.991 171.626 226.816 1.00 85.79 O
ATOM 238 OD2 ASP A 92 169.705 170.057 228.319 1.00 85.79 O
ATOM 239 N CYS A 93 172.913 171.432 224.135 1.00 82.18 N
ATOM 240 CA CYS A 93 172.980 170.927 222.780 1.00 82.18 C
ATOM 241 C CYS A 93 174.373 171.201 222.233 1.00 82.18 C
ATOM 242 O CYS A 93 174.932 172.273 222.490 1.00 82.18 O
ATOM 243 CB CYS A 93 171.922 171.590 221.893 1.00 82.18 C
ATOM 244 SG CYS A 93 170.223 171.200 222.360 1.00 82.18 S
ATOM 245 N PRO A 94 174.977 170.252 221.474 1.00 81.71 N
ATOM 246 CA PRO A 94 176.364 170.409 221.020 1.00 81.71 C
ATOM 247 C PRO A 94 176.507 171.172 219.705 1.00 81.71 C
ATOM 248 O PRO A 94 177.174 170.720 218.771 1.00 81.71 O
ATOM 249 CB PRO A 94 176.833 168.957 220.877 1.00 81.71 C
ATOM 250 CG PRO A 94 175.611 168.244 220.425 1.00 81.71 C
ATOM 251 CD PRO A 94 174.438 168.929 221.101 1.00 81.71 C
ATOM 252 N ALA A 95 175.893 172.355 219.633 1.00 76.47 N
ATOM 253 CA ALA A 95 175.954 173.195 218.446 1.00 76.47 C
ATOM 254 C ALA A 95 176.219 174.659 218.739 1.00 76.47 C
ATOM 255 O ALA A 95 176.544 175.402 217.811 1.00 76.47 O
ATOM 256 CB ALA A 95 174.649 173.083 217.650 1.00 76.47 C
ATOM 257 N VAL A 96 176.108 175.096 219.983 1.00 75.68 N
ATOM 258 CA VAL A 96 176.203 176.499 220.348 1.00 75.68 C
ATOM 259 C VAL A 96 177.445 176.659 221.208 1.00 75.68 C
ATOM 260 O VAL A 96 177.575 175.998 222.246 1.00 75.68 O
ATOM 261 CB VAL A 96 174.938 176.960 221.090 1.00 75.68 C
ATOM 262 CG1 VAL A 96 175.135 178.307 221.727 1.00 75.68 C
ATOM 263 CG2 VAL A 96 173.758 176.989 220.141 1.00 75.68 C
ATOM 264 N ALA A 97 178.374 177.500 220.759 1.00 76.35 N
ATOM 265 CA ALA A 97 179.495 177.886 221.602 1.00 76.35 C
ATOM 266 C ALA A 97 178.995 178.770 222.730 1.00 76.35 C
ATOM 267 O ALA A 97 178.118 179.613 222.524 1.00 76.35 O
ATOM 268 CB ALA A 97 180.558 178.620 220.789 1.00 76.35 C
ATOM 269 N LYS A 98 179.551 178.556 223.923 1.00 76.50 N
ATOM 270 CA LYS A 98 179.039 179.174 225.140 1.00 76.50 C
ATOM 271 C LYS A 98 179.318 180.671 225.166 1.00 76.50 C
ATOM 272 O LYS A 98 180.324 181.148 224.636 1.00 76.50 O
ATOM 273 CB LYS A 98 179.630 178.486 226.376 1.00 76.50 C
ATOM 274 CG LYS A 98 181.147 178.535 226.505 0.00 76.50 C
ATOM 275 CD LYS A 98 181.604 177.940 227.827 0.00 76.50 C
ATOM 276 CE LYS A 98 181.526 176.423 227.812 0.00 76.50 C
ATOM 277 NZ LYS A 98 182.505 175.829 226.861 0.00 76.50 N
ATOM 278 N HIS A 99 178.386 181.413 225.722 1.00 80.09 N
ATOM 279 CA HIS A 99 178.396 182.850 225.577 1.00 80.09 C
ATOM 280 C HIS A 99 179.025 183.506 226.795 1.00 80.09 C
ATOM 281 O HIS A 99 179.540 182.845 227.699 1.00 80.09 O
ATOM 282 CB HIS A 99 176.977 183.365 225.325 1.00 80.09 C
ATOM 283 CG HIS A 99 176.444 183.028 223.968 1.00 80.09 C
ATOM 284 ND1 HIS A 99 175.779 181.852 223.698 1.00 80.09 N
ATOM 285 CD2 HIS A 99 176.479 183.717 222.802 1.00 80.09 C
ATOM 286 CE1 HIS A 99 175.427 181.831 222.425 1.00 80.09 C
ATOM 287 NE2 HIS A 99 175.841 182.950 221.859 1.00 80.09 N
ATOM 288 N ASP A 100 178.972 184.828 226.811 1.00 75.35 N
ATOM 289 CA ASP A 100 179.591 185.646 227.829 1.00 75.35 C
ATOM 290 C ASP A 100 178.657 185.713 229.030 1.00 75.35 C
ATOM 291 O ASP A 100 177.506 185.284 228.964 0.00 75.35 O
ATOM 292 CB ASP A 100 179.872 187.047 227.268 0.00 75.35 C
ATOM 293 CG ASP A 100 180.727 187.018 225.998 0.00 75.35 C
ATOM 294 OD1 ASP A 100 181.654 186.194 225.911 0.00 75.35 O
ATOM 295 OD2 ASP A 100 180.441 187.801 225.069 0.00 75.35 O
ATOM 296 N LEU A 119 185.903 181.657 218.818 1.00 90.97 N
ATOM 297 CA LEU A 119 185.261 181.512 217.519 1.00 90.97 C
ATOM 298 C LEU A 119 186.331 181.345 216.452 1.00 90.97 C
ATOM 299 O LEU A 119 187.432 180.875 216.727 1.00 90.97 O
ATOM 300 CB LEU A 119 184.392 182.729 217.192 1.00 90.97 C
ATOM 301 CG LEU A 119 183.291 183.166 218.160 1.00 90.97 C
ATOM 302 CD1 LEU A 119 182.618 184.421 217.636 1.00 90.97 C
ATOM 303 CD2 LEU A 119 182.268 182.079 218.435 1.00 90.97 C
ATOM 304 N THR A 120 185.991 181.731 215.228 1.00 91.70 N
ATOM 305 CA THR A 120 186.957 181.970 214.169 1.00 91.70 C
ATOM 306 C THR A 120 186.630 183.350 213.610 1.00 91.70 C
ATOM 307 O THR A 120 185.463 183.755 213.605 1.00 91.70 O
ATOM 308 CB THR A 120 186.888 180.859 213.099 1.00 91.70 C
ATOM 309 OG1 THR A 120 186.964 179.586 213.748 1.00 91.70 O
ATOM 310 CG2 THR A 120 188.058 180.931 212.136 1.00 91.70 C
ATOM 311 N LYS A 121 187.678 184.089 213.214 1.00 92.03 N
ATOM 312 CA LYS A 121 187.558 185.492 212.821 1.00 92.03 C
ATOM 313 C LYS A 121 186.742 185.669 211.544 1.00 92.03 C
ATOM 314 O LYS A 121 185.915 186.582 211.455 1.00 92.03 O
ATOM 315 CB LYS A 121 188.955 186.087 212.652 1.00 92.03 C
ATOM 316 CG LYS A 121 189.002 187.588 212.459 1.00 92.03 C
ATOM 317 CD LYS A 121 190.441 188.070 212.399 1.00 92.03 C
ATOM 318 CE LYS A 121 190.518 189.477 211.852 1.00 92.03 C
ATOM 319 NZ LYS A 121 189.778 189.593 210.568 1.00 92.03 N
ATOM 320 N TYR A 122 186.936 184.800 210.563 1.00 90.73 N
ATOM 321 CA TYR A 122 186.226 184.912 209.300 1.00 90.73 C
ATOM 322 C TYR A 122 185.012 183.996 209.285 1.00 90.73 C
ATOM 323 O TYR A 122 185.084 182.842 209.713 1.00 90.73 O
ATOM 324 CB TYR A 122 187.165 184.586 208.146 1.00 90.73 C
ATOM 325 CG TYR A 122 188.401 185.445 208.179 1.00 90.73 C
ATOM 326 CD1 TYR A 122 188.333 186.794 207.839 1.00 90.73 C
ATOM 327 CD2 TYR A 122 189.630 184.920 208.579 1.00 90.73 C
ATOM 328 CE1 TYR A 122 189.458 187.598 207.878 1.00 90.73 C
ATOM 329 CE2 TYR A 122 190.767 185.718 208.624 1.00 90.73 C
ATOM 330 CZ TYR A 122 190.668 187.054 208.272 1.00 90.73 C
ATOM 331 OH TYR A 122 191.782 187.859 208.310 1.00 90.73 O
ATOM 332 N THR A 123 183.892 184.526 208.802 1.00 87.39 N
ATOM 333 CA THR A 123 182.620 183.823 208.804 1.00 87.39 C
ATOM 334 C THR A 123 182.453 182.963 207.554 1.00 87.39 C
ATOM 335 O THR A 123 183.272 182.980 206.634 1.00 87.39 O
ATOM 336 CB THR A 123 181.470 184.812 208.893 1.00 87.39 C
ATOM 337 OG1 THR A 123 181.391 185.546 207.669 1.00 87.39 O
ATOM 338 CG2 THR A 123 181.700 185.780 210.037 1.00 87.39 C
ATOM 339 N MET A 124 181.361 182.197 207.537 1.00 85.10 N
ATOM 340 CA MET A 124 181.051 181.313 206.420 1.00 85.10 C
ATOM 341 C MET A 124 180.501 182.081 205.228 1.00 85.10 C
ATOM 342 O MET A 124 180.757 181.707 204.074 1.00 85.10 O
ATOM 343 CB MET A 124 180.056 180.245 206.882 1.00 85.10 C
ATOM 344 CG MET A 124 179.735 179.139 205.880 1.00 85.10 C
ATOM 345 SD MET A 124 181.129 178.068 205.490 1.00 85.10 S
ATOM 346 CE MET A 124 180.641 177.450 203.882 1.00 85.10 C
ATOM 347 N ALA A 125 179.798 183.186 205.480 1.00 85.81 N
ATOM 348 CA ALA A 125 179.195 183.958 204.402 1.00 85.81 C
ATOM 349 C ALA A 125 180.217 184.753 203.607 1.00 85.81 C
ATOM 350 O ALA A 125 179.918 185.172 202.490 1.00 85.81 O
ATOM 351 CB ALA A 125 178.134 184.908 204.954 1.00 85.81 C
ATOM 352 N ASP A 126 181.406 184.971 204.159 1.00 86.51 N
ATOM 353 CA ASP A 126 182.482 185.589 203.405 1.00 86.51 C
ATOM 354 C ASP A 126 183.048 184.579 202.411 1.00 86.51 C
ATOM 355 O ASP A 126 183.434 184.948 201.301 1.00 86.51 O
ATOM 356 CB ASP A 126 183.522 186.095 204.411 1.00 86.51 C
ATOM 357 CG ASP A 126 184.609 186.979 203.810 1.00 86.51 C
ATOM 358 OD1 ASP A 126 184.663 187.246 202.593 1.00 86.51 O
ATOM 359 OD2 ASP A 126 185.424 187.457 204.623 1.00 86.51 O
ATOM 360 N LEU A 127 183.041 183.297 202.777 1.00 78.50 N
ATOM 361 CA LEU A 127 183.397 182.238 201.841 1.00 78.50 C
ATOM 362 C LEU A 127 182.290 182.016 200.818 1.00 78.50 C
ATOM 363 O LEU A 127 182.555 181.552 199.701 1.00 78.50 O
ATOM 364 CB LEU A 127 183.699 180.957 202.618 1.00 78.50 C
ATOM 365 CG LEU A 127 184.166 179.675 201.931 1.00 78.50 C
ATOM 366 CD1 LEU A 127 185.503 179.898 201.247 1.00 78.50 C
ATOM 367 CD2 LEU A 127 184.253 178.531 202.930 1.00 78.50 C
ATOM 368 N VAL A 128 181.048 182.340 201.182 1.00 81.65 N
ATOM 369 CA VAL A 128 179.972 182.394 200.196 1.00 81.65 C
ATOM 370 C VAL A 128 180.179 183.573 199.251 1.00 81.65 C
ATOM 371 O VAL A 128 180.014 183.450 198.030 1.00 81.65 O
ATOM 372 CB VAL A 128 178.608 182.452 200.916 1.00 81.65 C
ATOM 373 CG1 VAL A 128 177.445 182.618 199.942 1.00 81.65 C
ATOM 374 CG2 VAL A 128 178.399 181.190 201.731 1.00 81.65 C
ATOM 375 N TYR A 129 180.626 184.704 199.790 1.00 80.66 N
ATOM 376 CA TYR A 129 180.623 185.969 199.067 1.00 80.66 C
ATOM 377 C TYR A 129 181.777 186.058 198.078 1.00 80.66 C
ATOM 378 O TYR A 129 181.586 186.457 196.927 1.00 80.66 O
ATOM 379 CB TYR A 129 180.709 187.115 200.068 1.00 80.66 C
ATOM 380 CG TYR A 129 180.660 188.501 199.475 1.00 80.66 C
ATOM 381 CD1 TYR A 129 179.452 189.038 199.036 1.00 80.66 C
ATOM 382 CD2 TYR A 129 181.816 189.273 199.345 1.00 80.66 C
ATOM 383 CE1 TYR A 129 179.388 190.317 198.499 1.00 80.66 C
ATOM 384 CE2 TYR A 129 181.764 190.546 198.793 1.00 80.66 C
ATOM 385 CZ TYR A 129 180.546 191.057 198.374 1.00 80.66 C
ATOM 386 OH TYR A 129 180.486 192.318 197.834 1.00 80.66 O
ATOM 387 N ALA A 130 182.980 185.691 198.514 1.00 77.17 N
ATOM 388 CA ALA A 130 184.190 185.910 197.735 1.00 77.17 C
ATOM 389 C ALA A 130 184.345 184.943 196.577 1.00 77.17 C
ATOM 390 O ALA A 130 185.155 185.207 195.683 1.00 77.17 O
ATOM 391 CB ALA A 130 185.422 185.822 198.633 1.00 77.17 C
ATOM 392 N LEU A 131 183.610 183.840 196.563 1.00 77.68 N
ATOM 393 CA LEU A 131 183.510 183.026 195.363 1.00 77.68 C
ATOM 394 C LEU A 131 182.335 183.431 194.491 1.00 77.68 C
ATOM 395 O LEU A 131 182.149 182.848 193.420 1.00 77.68 O
ATOM 396 CB LEU A 131 183.398 181.537 195.703 1.00 77.68 C
ATOM 397 CG LEU A 131 184.631 180.668 195.984 1.00 77.68 C
ATOM 398 CD1 LEU A 131 185.495 180.603 194.731 1.00 77.68 C
ATOM 399 CD2 LEU A 131 185.457 181.054 197.214 1.00 77.68 C
ATOM 400 N ARG A 132 181.548 184.419 194.917 1.00 80.71 N
ATOM 401 CA ARG A 132 180.452 184.943 194.121 1.00 80.71 C
ATOM 402 C ARG A 132 180.707 186.352 193.609 1.00 80.71 C
ATOM 403 O ARG A 132 179.991 186.803 192.710 1.00 80.71 O
ATOM 404 CB ARG A 132 179.154 184.938 194.943 1.00 80.71 C
ATOM 405 CG ARG A 132 178.416 183.607 194.958 1.00 80.71 C
ATOM 406 CD ARG A 132 177.267 183.623 195.961 1.00 80.71 C
ATOM 407 NE ARG A 132 176.014 184.087 195.374 1.00 80.71 N
ATOM 408 CZ ARG A 132 174.823 183.556 195.633 1.00 80.71 C
ATOM 409 NH1 ARG A 132 174.716 182.538 196.474 1.00 80.71 N
ATOM 410 NH2 ARG A 132 173.738 184.043 195.051 1.00 80.71 N
ATOM 411 N HIS A 133 181.698 187.054 194.152 1.00 76.81 N
ATOM 412 CA HIS A 133 181.945 188.467 193.887 1.00 76.81 C
ATOM 413 C HIS A 133 183.415 188.707 193.600 1.00 76.81 C
ATOM 414 O HIS A 133 184.049 189.596 194.169 1.00 76.81 O
ATOM 415 CB HIS A 133 181.491 189.317 195.063 1.00 76.81 C
ATOM 416 CG HIS A 133 180.010 189.348 195.241 1.00 76.81 C
ATOM 417 ND1 HIS A 133 179.305 188.303 195.792 1.00 76.81 N
ATOM 418 CD2 HIS A 133 179.097 190.298 194.933 1.00 76.81 C
ATOM 419 CE1 HIS A 133 178.020 188.605 195.814 1.00 76.81 C
ATOM 420 NE2 HIS A 133 177.867 189.812 195.302 1.00 76.81 N
ATOM 421 N PHE A 134 183.976 187.916 192.694 1.00 84.04 N
ATOM 422 CA PHE A 134 185.421 187.805 192.547 1.00 84.04 C
ATOM 423 C PHE A 134 185.977 188.804 191.541 1.00 84.04 C
ATOM 424 O PHE A 134 185.452 188.938 190.431 1.00 84.04 O
ATOM 425 CB PHE A 134 185.794 186.391 192.116 1.00 84.04 C
ATOM 426 CG PHE A 134 187.251 186.210 191.861 1.00 84.04 C
ATOM 427 CD1 PHE A 134 188.165 186.357 192.897 1.00 84.04 C
ATOM 428 CD2 PHE A 134 187.711 185.900 190.588 1.00 84.04 C
ATOM 429 CE1 PHE A 134 189.522 186.192 192.671 1.00 84.04 C
ATOM 430 CE2 PHE A 134 189.065 185.733 190.349 1.00 84.04 C
ATOM 431 CZ PHE A 134 189.970 185.880 191.396 1.00 84.04 C
ATOM 432 N ASP A 135 187.049 189.492 191.937 1.00 88.58 N
ATOM 433 CA ASP A 135 187.862 190.291 191.030 1.00 88.58 C
ATOM 434 C ASP A 135 189.318 190.283 191.485 1.00 88.58 C
ATOM 435 O ASP A 135 189.613 190.166 192.676 1.00 88.58 O
ATOM 436 CB ASP A 135 187.283 191.716 190.845 1.00 88.58 C
ATOM 437 CG ASP A 135 187.216 192.560 192.136 1.00 88.58 C
ATOM 438 OD1 ASP A 135 187.550 192.121 193.255 1.00 88.58 O
ATOM 439 OD2 ASP A 135 186.797 193.730 192.011 1.00 88.58 O
ATOM 440 N GLU A 136 190.226 190.345 190.520 1.00 89.50 N
ATOM 441 CA GLU A 136 191.641 190.422 190.843 1.00 89.50 C
ATOM 442 C GLU A 136 191.992 191.837 191.281 1.00 89.50 C
ATOM 443 O GLU A 136 191.449 192.816 190.764 1.00 89.50 O
ATOM 444 CB GLU A 136 192.489 189.952 189.653 1.00 89.50 C
ATOM 445 CG GLU A 136 192.378 190.727 188.320 1.00 89.50 C
ATOM 446 CD GLU A 136 193.296 191.939 188.209 1.00 89.50 C
ATOM 447 OE1 GLU A 136 194.287 192.007 188.966 1.00 89.50 O
ATOM 448 OE2 GLU A 136 193.024 192.817 187.363 1.00 89.50 O
ATOM 449 N GLY A 137 192.892 191.940 192.258 1.00 92.95 N
ATOM 450 CA GLY A 137 193.299 193.206 192.827 1.00 92.95 C
ATOM 451 C GLY A 137 192.695 193.475 194.190 1.00 92.95 C
ATOM 452 O GLY A 137 193.337 194.121 195.027 1.00 92.95 O
ATOM 453 N ASN A 138 191.477 192.998 194.428 1.00 93.57 N
ATOM 454 CA ASN A 138 190.845 193.065 195.738 1.00 93.57 C
ATOM 455 C ASN A 138 190.524 191.669 196.255 1.00 93.57 C
ATOM 456 O ASN A 138 189.575 191.481 197.017 1.00 93.57 O
ATOM 457 CB ASN A 138 189.585 193.924 195.691 1.00 93.57 C
ATOM 458 CG ASN A 138 189.808 195.242 194.985 1.00 93.57 C
ATOM 459 OD1 ASN A 138 190.838 195.890 195.167 1.00 93.57 O
ATOM 460 ND2 ASN A 138 188.840 195.649 194.173 1.00 93.57 N
ATOM 461 N CYS A 139 191.316 190.682 195.845 1.00 98.17 N
ATOM 462 CA CYS A 139 191.112 189.282 196.208 1.00 98.17 C
ATOM 463 C CYS A 139 192.009 188.860 197.360 1.00 98.17 C
ATOM 464 O CYS A 139 192.483 187.723 197.409 1.00 98.17 O
ATOM 465 CB CYS A 139 191.339 188.388 194.994 1.00 98.17 C
ATOM 466 SG CYS A 139 192.974 188.540 194.233 1.00 98.17 S
ATOM 467 N ASP A 140 192.260 189.770 198.301 1.00100.03 N
ATOM 468 CA ASP A 140 193.149 189.465 199.413 1.00100.03 C
ATOM 469 C ASP A 140 192.484 188.601 200.473 1.00100.03 C
ATOM 470 O ASP A 140 193.172 187.802 201.110 1.00100.03 O
ATOM 471 CB ASP A 140 193.664 190.755 200.052 1.00100.03 C
ATOM 472 CG ASP A 140 192.566 191.770 200.293 1.00100.03 C
ATOM 473 OD1 ASP A 140 192.842 192.798 200.946 1.00100.03 O
ATOM 474 OD2 ASP A 140 191.431 191.550 199.822 1.00100.03 O
ATOM 475 N THR A 141 191.167 188.750 200.667 1.00 96.21 N
ATOM 476 CA THR A 141 190.456 188.069 201.751 1.00 96.21 C
ATOM 477 C THR A 141 190.372 186.566 201.499 1.00 96.21 C
ATOM 478 O THR A 141 190.582 185.754 202.420 1.00 96.21 O
ATOM 479 CB THR A 141 189.064 188.690 201.896 1.00 96.21 C
ATOM 480 OG1 THR A 141 189.200 190.084 202.193 1.00 96.21 O
ATOM 481 CG2 THR A 141 188.288 188.060 203.021 1.00 96.21 C
ATOM 482 N LEU A 142 190.189 186.197 200.224 1.00 94.17 N
ATOM 483 CA LEU A 142 190.293 184.814 199.762 1.00 94.17 C
ATOM 484 C LEU A 142 191.697 184.259 199.974 1.00 94.17 C
ATOM 485 O LEU A 142 191.864 183.075 200.295 1.00 94.17 O
ATOM 486 CB LEU A 142 189.924 184.756 198.281 1.00 94.17 C
ATOM 487 CG LEU A 142 190.119 183.493 197.444 1.00 94.17 C
ATOM 488 CD1 LEU A 142 188.919 182.593 197.623 1.00 94.17 C
ATOM 489 CD2 LEU A 142 190.333 183.825 195.980 1.00 94.17 C
ATOM 490 N LYS A 143 192.711 185.123 199.866 1.00 91.94 N
ATOM 491 CA LYS A 143 194.090 184.690 200.026 1.00 91.94 C
ATOM 492 C LYS A 143 194.425 184.363 201.482 1.00 91.94 C
ATOM 493 O LYS A 143 195.049 183.318 201.725 1.00 91.94 O
ATOM 494 CB LYS A 143 195.037 185.744 199.450 1.00 91.94 C
ATOM 495 CG LYS A 143 196.470 185.390 199.488 1.00 91.94 C
ATOM 496 CD LYS A 143 196.681 184.244 198.589 1.00 91.94 C