HEADER HYDROLASE/HYDROLASE INHIBITOR 23-MAR-17 5V9O
TITLE KRAS G12C INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTPASE KRAS;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: K-RAS 2,KI-RAS,C-K-RAS,C-KI-RAS;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: KRAS, KRAS2, RASK2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333
KEYWDS KRAS MUTANT INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.WESTOVER,J.LU
REVDAT 3 04-OCT-23 5V9O 1 LINK
REVDAT 2 30-AUG-17 5V9O 1 JRNL
REVDAT 1 23-AUG-17 5V9O 0
JRNL AUTH M.ZENG,J.LU,L.LI,F.FERU,C.QUAN,T.W.GERO,S.B.FICARRO,Y.XIONG,
JRNL AUTH 2 C.AMBROGIO,R.M.PARANAL,M.CATALANO,J.SHAO,K.K.WONG,J.A.MARTO,
JRNL AUTH 3 E.S.FISCHER,P.A.JANNE,D.A.SCOTT,K.D.WESTOVER,N.S.GRAY
JRNL TITL POTENT AND SELECTIVE COVALENT QUINAZOLINE INHIBITORS OF KRAS
JRNL TITL 2 G12C.
JRNL REF CELL CHEM BIOL V. 24 1005 2017
JRNL REFN ESSN 2451-9456
JRNL PMID 28781124
JRNL DOI 10.1016/J.CHEMBIOL.2017.06.017
REMARK 2
REMARK 2 RESOLUTION. 1.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 34369
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.770
REMARK 3 FREE R VALUE TEST SET COUNT : 1982
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 45.0983 - 3.7581 1.00 2484 156 0.1693 0.1656
REMARK 3 2 3.7581 - 2.9831 1.00 2396 150 0.1598 0.1857
REMARK 3 3 2.9831 - 2.6061 1.00 2385 147 0.1965 0.2066
REMARK 3 4 2.6061 - 2.3678 1.00 2360 142 0.1725 0.2077
REMARK 3 5 2.3678 - 2.1981 1.00 2347 144 0.1671 0.1844
REMARK 3 6 2.1981 - 2.0685 1.00 2371 145 0.1670 0.2114
REMARK 3 7 2.0685 - 1.9649 1.00 2341 141 0.1724 0.2030
REMARK 3 8 1.9649 - 1.8794 1.00 2346 145 0.1759 0.1958
REMARK 3 9 1.8794 - 1.8070 1.00 2348 148 0.1867 0.2136
REMARK 3 10 1.8070 - 1.7447 1.00 2347 143 0.1914 0.2167
REMARK 3 11 1.7447 - 1.6901 1.00 2315 138 0.2055 0.2150
REMARK 3 12 1.6901 - 1.6418 1.00 2331 141 0.2232 0.2264
REMARK 3 13 1.6418 - 1.5986 0.98 2286 144 0.2530 0.2826
REMARK 3 14 1.5986 - 1.5596 0.73 1730 98 0.3035 0.2843
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.840
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.88
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.88
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 1443
REMARK 3 ANGLE : 1.019 1957
REMARK 3 CHIRALITY : 0.054 212
REMARK 3 PLANARITY : 0.006 247
REMARK 3 DIHEDRAL : 19.567 861
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5V9O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1000227094.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35091
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.560
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 31.80
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 19.00
REMARK 200 R MERGE FOR SHELL (I) : 2.19200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4OBE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH9.0, AMMONIUM SULFATE
REMARK 280 1.6M, EVAPORATION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 510 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 523 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 529 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 530 LIES ON A SPECIAL POSITION.
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 GLY A 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 344 O HOH A 486 1.97
REMARK 500 O HOH A 400 O HOH A 491 1.99
REMARK 500 O HOH A 450 O HOH A 522 2.03
REMARK 500 O HOH A 440 O HOH A 491 2.04
REMARK 500 O HOH A 444 O HOH A 517 2.05
REMARK 500 O HOH A 470 O HOH A 517 2.09
REMARK 500 O HOH A 403 O HOH A 439 2.09
REMARK 500 O HOH A 309 O HOH A 403 2.15
REMARK 500 O HOH A 476 O HOH A 503 2.15
REMARK 500 O HOH A 474 O HOH A 493 2.15
REMARK 500 NZ LYS A 5 O HOH A 301 2.16
REMARK 500 O HOH A 324 O HOH A 390 2.18
REMARK 500 O HOH A 416 O HOH A 517 2.19
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 GLU A 31 41.37 -141.12
REMARK 500 ASP A 33 116.71 -39.53
REMARK 500 ALA A 59 -24.79 -150.46
REMARK 500 LYS A 117 33.93 71.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 529 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A 530 DISTANCE = 5.85 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 17 OG
REMARK 620 2 GDP A 201 O1B 91.2
REMARK 620 3 HOH A 335 O 91.8 84.9
REMARK 620 4 HOH A 337 O 84.1 96.1 175.8
REMARK 620 5 HOH A 365 O 91.8 170.5 85.9 93.2
REMARK 620 6 HOH A 373 O 173.2 91.2 94.8 89.3 86.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 91G A 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5V9L RELATED DB: PDB
DBREF 5V9O A 1 168 UNP P01116 RASK_HUMAN 1 168
SEQADV 5V9O GLY A 0 UNP P01116 EXPRESSION TAG
SEQADV 5V9O CYS A 12 UNP P01116 GLY 12 ENGINEERED MUTATION
SEQRES 1 A 169 GLY MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA CYS
SEQRES 2 A 169 GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN
SEQRES 3 A 169 ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP
SEQRES 4 A 169 SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS
SEQRES 5 A 169 LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR
SEQRES 6 A 169 SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY
SEQRES 7 A 169 PHE LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE
SEQRES 8 A 169 GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL
SEQRES 9 A 169 LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN
SEQRES 10 A 169 LYS CYS ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN
SEQRES 11 A 169 ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE
SEQRES 12 A 169 GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA
SEQRES 13 A 169 PHE TYR THR LEU VAL ARG GLU ILE ARG LYS HIS LYS GLU
HET GDP A 201 28
HET MG A 202 1
HET 91G A 203 40
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM 91G N~3~-[6-CHLORO-7-(3-HYDROXYNAPHTHALEN-1-YL)-4-(4-
HETNAM 2 91G PROPANOYLPIPERAZIN-1-YL)QUINAZOLIN-2-YL]-N,N-DIMETHYL-
HETNAM 3 91G BETA-ALANINAMIDE
FORMUL 2 GDP C10 H15 N5 O11 P2
FORMUL 3 MG MG 2+
FORMUL 4 91G C30 H33 CL N6 O3
FORMUL 5 HOH *230(H2 O)
HELIX 1 AA1 GLY A 15 ASN A 26 1 12
HELIX 2 AA2 SER A 65 THR A 74 1 10
HELIX 3 AA3 ASN A 86 LYS A 104 1 19
HELIX 4 AA4 ASP A 126 GLY A 138 1 13
HELIX 5 AA5 GLY A 151 GLU A 168 1 18
SHEET 1 AA1 6 ASP A 38 ILE A 46 0
SHEET 2 AA1 6 GLU A 49 ASP A 57 -1 O LEU A 53 N LYS A 42
SHEET 3 AA1 6 GLU A 3 VAL A 9 1 N VAL A 8 O LEU A 56
SHEET 4 AA1 6 GLY A 77 ALA A 83 1 O LEU A 79 N VAL A 9
SHEET 5 AA1 6 MET A 111 ASN A 116 1 O ASN A 116 N PHE A 82
SHEET 6 AA1 6 PHE A 141 GLU A 143 1 O ILE A 142 N LEU A 113
LINK SG CYS A 12 C20 91G A 203 1555 1555 1.41
LINK OG SER A 17 MG MG A 202 1555 1555 2.03
LINK O1B GDP A 201 MG MG A 202 1555 1555 2.08
LINK MG MG A 202 O HOH A 335 1555 1555 2.18
LINK MG MG A 202 O HOH A 337 1555 1555 2.08
LINK MG MG A 202 O HOH A 365 1555 1555 2.10
LINK MG MG A 202 O HOH A 373 1555 1555 2.12
SITE 1 AC1 27 GLY A 13 VAL A 14 GLY A 15 LYS A 16
SITE 2 AC1 27 SER A 17 ALA A 18 PHE A 28 VAL A 29
SITE 3 AC1 27 ASP A 30 ASN A 116 LYS A 117 ASP A 119
SITE 4 AC1 27 LEU A 120 SER A 145 ALA A 146 LYS A 147
SITE 5 AC1 27 MG A 202 91G A 203 HOH A 321 HOH A 330
SITE 6 AC1 27 HOH A 335 HOH A 337 HOH A 373 HOH A 374
SITE 7 AC1 27 HOH A 398 HOH A 412 HOH A 431
SITE 1 AC2 6 SER A 17 GDP A 201 HOH A 335 HOH A 337
SITE 2 AC2 6 HOH A 365 HOH A 373
SITE 1 AC3 18 GLY A 10 CYS A 12 LYS A 16 ALA A 59
SITE 2 AC3 18 GLY A 60 GLN A 61 GLU A 62 GLU A 63
SITE 3 AC3 18 ARG A 68 ASP A 69 MET A 72 ASP A 92
SITE 4 AC3 18 HIS A 95 TYR A 96 GLN A 99 ILE A 100
SITE 5 AC3 18 GDP A 201 HOH A 338
CRYST1 90.159 90.159 90.159 90.00 90.00 90.00 P 2 3 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011092 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011092 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011092 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
