HEADER HYDROLASE/HYDROLASE INHIBITOR 23-MAR-17 5V9L
TITLE KRAS G12C IN BOUND TO QUINAZOLINE BASED SWITCH II POCKET (SWIIP)
TITLE 2 BINDER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTPASE KRAS;
COMPND 3 CHAIN: A, B, C;
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 5V9L 1 LINK
REVDAT 2 30-AUG-17 5V9L 1 JRNL
REVDAT 1 23-AUG-17 5V9L 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. 1.98 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) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 34411
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.790
REMARK 3 FREE R VALUE TEST SET COUNT : 1994
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 48.8680 - 4.7731 0.98 2492 156 0.1709 0.2200
REMARK 3 2 4.7731 - 3.7890 0.99 2476 156 0.1352 0.1435
REMARK 3 3 3.7890 - 3.3101 1.00 2512 148 0.1513 0.2110
REMARK 3 4 3.3101 - 3.0075 1.00 2491 159 0.1688 0.2497
REMARK 3 5 3.0075 - 2.7920 1.00 2509 150 0.1831 0.2445
REMARK 3 6 2.7920 - 2.6274 1.00 2484 154 0.1830 0.2308
REMARK 3 7 2.6274 - 2.4958 1.00 2481 150 0.1785 0.2570
REMARK 3 8 2.4958 - 2.3872 1.00 2516 153 0.1740 0.2446
REMARK 3 9 2.3872 - 2.2953 1.00 2481 152 0.1796 0.2364
REMARK 3 10 2.2953 - 2.2161 0.98 2480 154 0.1869 0.2755
REMARK 3 11 2.2161 - 2.1468 0.92 2273 140 0.2035 0.2600
REMARK 3 12 2.1468 - 2.0854 0.81 2019 126 0.2095 0.2896
REMARK 3 13 2.0854 - 2.0305 0.71 1761 108 0.2275 0.3066
REMARK 3 14 2.0305 - 1.9810 0.58 1442 88 0.2369 0.3312
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.05
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 : 0.008 4342
REMARK 3 ANGLE : 0.978 5885
REMARK 3 CHIRALITY : 0.054 637
REMARK 3 PLANARITY : 0.007 749
REMARK 3 DIHEDRAL : 16.687 2591
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 5V9L 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_1000227090.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
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 : 37066
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 8.100
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 1.00300
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 (%): 47.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M SODIUM PHOSPHATE MONOBASIC
REMARK 280 MONOHYDRATE, POTASSIUM PHOSPHATE DIBASIC PH7.1, EVAPORATION,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 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 65.27100
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 65.27100
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 65.27100
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 370 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 374 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 398 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 367 LIES ON A SPECIAL POSITION.
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 312 O HOH A 368 2.00
REMARK 500 CB CYS A 12 C19 91D A 203 2.00
REMARK 500 NH1 ARG B 164 O HOH B 301 2.18
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 LYS A 117 36.31 74.25
REMARK 500 LYS A 117 37.03 74.25
REMARK 500 ARG A 149 -0.75 85.80
REMARK 500 LYS B 117 30.93 70.09
REMARK 500 ARG B 149 -6.21 83.15
REMARK 500 ASP C 108 69.21 -119.55
REMARK 500 LYS C 117 30.60 70.85
REMARK 500 SER C 122 97.07 -62.36
REMARK 500 ARG C 149 -1.93 67.76
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 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 17 OG
REMARK 620 2 GDP A 201 O3B 100.2
REMARK 620 3 HOH A 301 O 93.3 85.0
REMARK 620 4 HOH A 306 O 81.1 97.0 174.3
REMARK 620 5 HOH A 322 O 88.1 170.9 90.8 87.9
REMARK 620 6 HOH A 336 O 166.7 87.1 98.4 87.1 85.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 17 OG
REMARK 620 2 GDP B 201 O3B 91.2
REMARK 620 3 HOH B 312 O 92.2 92.4
REMARK 620 4 HOH B 321 O 81.2 95.8 169.5
REMARK 620 5 HOH B 331 O 169.9 97.1 93.3 92.2
REMARK 620 6 HOH B 342 O 85.7 175.4 84.4 87.0 86.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER C 17 OG
REMARK 620 2 GDP C 201 O3B 95.9
REMARK 620 3 HOH C 317 O 81.3 98.5
REMARK 620 4 HOH C 322 O 170.0 91.3 90.7
REMARK 620 5 HOH C 323 O 96.4 88.0 173.3 90.9
REMARK 620 6 HOH C 338 O 87.8 169.3 92.0 86.4 81.6
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 91D A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 91D B 203 and CYS B
REMARK 800 12
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 91D C 203 and CYS C
REMARK 800 12
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5V9O RELATED DB: PDB
DBREF 5V9L A 1 168 UNP P01116 RASK_HUMAN 1 168
DBREF 5V9L B 1 168 UNP P01116 RASK_HUMAN 1 168
DBREF 5V9L C 1 168 UNP P01116 RASK_HUMAN 1 168
SEQADV 5V9L GLY A 0 UNP P01116 EXPRESSION TAG
SEQADV 5V9L CYS A 12 UNP P01116 GLY 12 ENGINEERED MUTATION
SEQADV 5V9L GLY B 0 UNP P01116 EXPRESSION TAG
SEQADV 5V9L CYS B 12 UNP P01116 GLY 12 ENGINEERED MUTATION
SEQADV 5V9L GLY C 0 UNP P01116 EXPRESSION TAG
SEQADV 5V9L CYS C 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
SEQRES 1 B 169 GLY MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA CYS
SEQRES 2 B 169 GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN
SEQRES 3 B 169 ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP
SEQRES 4 B 169 SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS
SEQRES 5 B 169 LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR
SEQRES 6 B 169 SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY
SEQRES 7 B 169 PHE LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE
SEQRES 8 B 169 GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL
SEQRES 9 B 169 LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN
SEQRES 10 B 169 LYS CYS ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN
SEQRES 11 B 169 ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE
SEQRES 12 B 169 GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA
SEQRES 13 B 169 PHE TYR THR LEU VAL ARG GLU ILE ARG LYS HIS LYS GLU
SEQRES 1 C 169 GLY MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA CYS
SEQRES 2 C 169 GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN
SEQRES 3 C 169 ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP
SEQRES 4 C 169 SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS
SEQRES 5 C 169 LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR
SEQRES 6 C 169 SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY
SEQRES 7 C 169 PHE LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE
SEQRES 8 C 169 GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL
SEQRES 9 C 169 LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN
SEQRES 10 C 169 LYS CYS ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN
SEQRES 11 C 169 ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE
SEQRES 12 C 169 GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA
SEQRES 13 C 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 91D A 203 36
HET GDP B 201 28
HET MG B 202 1
HET 91D B 203 36
HET GDP C 201 28
HET MG C 202 1
HET 91D C 203 36
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM 91D N~3~-[6-CHLORO-7-(2-FLUOROPHENYL)-4-(4-
HETNAM 2 91D PROPANOYLPIPERAZIN-1-YL)QUINAZOLIN-2-YL]-N,N-DIMETHYL-
HETNAM 3 91D BETA-ALANINAMIDE
FORMUL 4 GDP 3(C10 H15 N5 O11 P2)
FORMUL 5 MG 3(MG 2+)
FORMUL 6 91D 3(C26 H30 CL F N6 O2)
FORMUL 13 HOH *240(H2 O)
HELIX 1 AA1 GLY A 15 ASN A 26 1 12
HELIX 2 AA2 SER A 65 GLY A 75 1 11
HELIX 3 AA3 ASN A 86 ASP A 92 1 7
HELIX 4 AA4 ASP A 92 ASP A 105 1 14
HELIX 5 AA5 ASP A 126 GLY A 138 1 13
HELIX 6 AA6 GLY A 151 GLU A 168 1 18
HELIX 7 AA7 GLY B 15 ASN B 26 1 12
HELIX 8 AA8 SER B 65 GLY B 75 1 11
HELIX 9 AA9 ASN B 86 ASP B 92 1 7
HELIX 10 AB1 ASP B 92 ASP B 105 1 14
HELIX 11 AB2 ASP B 126 GLY B 138 1 13
HELIX 12 AB3 GLY B 151 GLU B 168 1 18
HELIX 13 AB4 GLY C 15 ASN C 26 1 12
HELIX 14 AB5 SER C 65 GLY C 75 1 11
HELIX 15 AB6 ASN C 86 ASP C 92 1 7
HELIX 16 AB7 ASP C 92 ASP C 105 1 14
HELIX 17 AB8 ASP C 126 GLY C 138 1 13
HELIX 18 AB9 GLY C 151 LYS C 167 1 17
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 GLY A 10 1 N VAL A 8 O LEU A 56
SHEET 4 AA1 6 GLY A 77 ALA A 83 1 O VAL A 81 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 GLY A 115
SHEET 1 AA2 6 ASP B 38 ILE B 46 0
SHEET 2 AA2 6 GLU B 49 ASP B 57 -1 O ILE B 55 N TYR B 40
SHEET 3 AA2 6 THR B 2 GLY B 10 1 N LEU B 6 O ASP B 54
SHEET 4 AA2 6 GLY B 77 ALA B 83 1 O LEU B 79 N VAL B 9
SHEET 5 AA2 6 MET B 111 ASN B 116 1 O ASN B 116 N PHE B 82
SHEET 6 AA2 6 PHE B 141 GLU B 143 1 O ILE B 142 N LEU B 113
SHEET 1 AA3 6 ASP C 38 ILE C 46 0
SHEET 2 AA3 6 GLU C 49 ASP C 57 -1 O CYS C 51 N VAL C 44
SHEET 3 AA3 6 GLU C 3 GLY C 10 1 N VAL C 8 O LEU C 56
SHEET 4 AA3 6 GLY C 77 ALA C 83 1 O VAL C 81 N VAL C 9
SHEET 5 AA3 6 MET C 111 ASN C 116 1 O ASN C 116 N PHE C 82
SHEET 6 AA3 6 PHE C 141 GLU C 143 1 O ILE C 142 N GLY C 115
LINK SG CYS A 12 C19 91D A 203 1555 1555 1.60
LINK SG CYS B 12 C19 91D B 203 1555 1555 1.62
LINK SG CYS C 12 C19 91D C 203 1555 1555 1.61
LINK OG SER A 17 MG MG A 202 1555 1555 2.04
LINK O3B GDP A 201 MG MG A 202 1555 1555 1.93
LINK MG MG A 202 O HOH A 301 1555 1555 2.21
LINK MG MG A 202 O HOH A 306 1555 1555 2.22
LINK MG MG A 202 O HOH A 322 1555 1555 2.25
LINK MG MG A 202 O HOH A 336 1555 1555 2.22
LINK OG SER B 17 MG MG B 202 1555 1555 2.12
LINK O3B GDP B 201 MG MG B 202 1555 1555 1.98
LINK MG MG B 202 O HOH B 312 1555 1555 2.11
LINK MG MG B 202 O HOH B 321 1555 1555 2.00
LINK MG MG B 202 O HOH B 331 1555 1555 2.04
LINK MG MG B 202 O HOH B 342 1555 1555 2.28
LINK OG SER C 17 MG MG C 202 1555 1555 2.15
LINK O3B GDP C 201 MG MG C 202 1555 1555 1.90
LINK MG MG C 202 O HOH C 317 1555 1555 2.07
LINK MG MG C 202 O HOH C 322 1555 1555 2.15
LINK MG MG C 202 O HOH C 323 1555 1555 2.09
LINK MG MG C 202 O HOH C 338 1555 1555 2.09
SITE 1 AC1 24 CYS A 12 GLY A 13 VAL A 14 GLY A 15
SITE 2 AC1 24 LYS A 16 SER A 17 ALA A 18 PHE A 28
SITE 3 AC1 24 VAL A 29 ASP A 30 TYR A 32 ASN A 116
SITE 4 AC1 24 LYS A 117 ASP A 119 LEU A 120 SER A 145
SITE 5 AC1 24 ALA A 146 LYS A 147 MG A 202 91D A 203
SITE 6 AC1 24 HOH A 301 HOH A 315 HOH A 336 HOH A 356
SITE 1 AC2 6 SER A 17 GDP A 201 HOH A 301 HOH A 306
SITE 2 AC2 6 HOH A 322 HOH A 336
SITE 1 AC3 11 VAL A 9 GLY A 10 CYS A 12 LYS A 16
SITE 2 AC3 11 ALA A 59 GLY A 60 HIS A 95 TYR A 96
SITE 3 AC3 11 VAL A 103 GDP A 201 HOH A 336
SITE 1 AC4 24 GLY B 13 VAL B 14 GLY B 15 LYS B 16
SITE 2 AC4 24 SER B 17 ALA B 18 PHE B 28 VAL B 29
SITE 3 AC4 24 ASP B 30 ASN B 116 LYS B 117 ASP B 119
SITE 4 AC4 24 LEU B 120 SER B 145 ALA B 146 LYS B 147
SITE 5 AC4 24 MG B 202 HOH B 312 HOH B 318 HOH B 321
SITE 6 AC4 24 HOH B 324 HOH B 325 HOH B 331 HOH B 378
SITE 1 AC5 6 SER B 17 GDP B 201 HOH B 312 HOH B 321
SITE 2 AC5 6 HOH B 331 HOH B 342
SITE 1 AC6 22 GLY C 13 VAL C 14 GLY C 15 LYS C 16
SITE 2 AC6 22 SER C 17 ALA C 18 PHE C 28 VAL C 29
SITE 3 AC6 22 ASP C 30 ASN C 116 LYS C 117 ASP C 119
SITE 4 AC6 22 LEU C 120 SER C 145 ALA C 146 LYS C 147
SITE 5 AC6 22 MG C 202 HOH C 313 HOH C 317 HOH C 322
SITE 6 AC6 22 HOH C 323 HOH C 327
SITE 1 AC7 6 SER C 17 GDP C 201 HOH C 317 HOH C 322
SITE 2 AC7 6 HOH C 323 HOH C 338
SITE 1 AC8 16 GLY A 48 VAL B 9 GLY B 10 ALA B 11
SITE 2 AC8 16 GLY B 13 VAL B 14 LYS B 16 PRO B 34
SITE 3 AC8 16 THR B 58 ALA B 59 GLY B 60 HIS B 95
SITE 4 AC8 16 TYR B 96 VAL B 103 HOH B 307 HOH B 380
SITE 1 AC9 16 VAL C 9 GLY C 10 ALA C 11 GLY C 13
SITE 2 AC9 16 VAL C 14 LYS C 16 PRO C 34 THR C 58
SITE 3 AC9 16 ALA C 59 GLY C 60 MET C 72 HIS C 95
SITE 4 AC9 16 TYR C 96 VAL C 103 HOH C 322 HOH C 343
CRYST1 85.062 85.062 130.542 90.00 90.00 120.00 P 63 18
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 0.011756 0.006787 0.000000 0.00000
SCALE2 0.000000 0.013575 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007660 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
