HEADER HYDROLASE 05-JUN-17 5W22
TITLE CRYSTAL STRUCTURE OF HUMAN WT-KRAS IN COMPLEX WITH GDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTPASE KRAS;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: K-RAS 2,KI-RAS,C-K-RAS,C-KI-RAS;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.XU,B.LONG,G.BORIS,S.NI,M.A.KENNEDY
REVDAT 3 13-MAR-24 5W22 1 LINK
REVDAT 2 20-DEC-17 5W22 1 JRNL
REVDAT 1 06-DEC-17 5W22 0
JRNL AUTH S.XU,B.N.LONG,G.H.BORIS,A.CHEN,S.NI,M.A.KENNEDY
JRNL TITL STRUCTURAL INSIGHT INTO THE REARRANGEMENT OF THE SWITCH I
JRNL TITL 2 REGION IN GTP-BOUND G12A K-RAS.
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 73 970 2017
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 29199977
JRNL DOI 10.1107/S2059798317015418
REMARK 2
REMARK 2 RESOLUTION. 1.76 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 36084
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1752
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.76
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2686
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.3210
REMARK 3 BIN FREE R VALUE SET COUNT : 126
REMARK 3 BIN FREE R VALUE : 0.3200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2719
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 156
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.88000
REMARK 3 B22 (A**2) : -0.88000
REMARK 3 B33 (A**2) : 2.87000
REMARK 3 B12 (A**2) : -0.44000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.110
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.104
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.098
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.389
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2823 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2578 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3818 ; 1.452 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5988 ; 0.771 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 338 ; 6.107 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 139 ;37.203 ;24.388
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 508 ;12.640 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;14.708 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 424 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3098 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 566 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 0 A 169 1
REMARK 3 1 B 0 B 169 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 1 A (A**2): 1359 ; 0.690 ; 0.500
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5W22 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1000228304.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-FEB-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97931
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.22
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37841
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.762
REMARK 200 RESOLUTION RANGE LOW (A) : 29.536
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.16300
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) : 1.76
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.93600
REMARK 200 R SYM FOR SHELL (I) : 0.93600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.700
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 MOL/L SODIUM ACETATE, 0.1 MOL/L
REMARK 280 TRIS PH 8.5, 24% PEG 4,000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
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+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 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 46.58850
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.89788
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 39.47700
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 46.58850
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 26.89788
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 39.47700
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 46.58850
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 26.89788
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 39.47700
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.79577
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 78.95400
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 53.79577
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 78.95400
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 53.79577
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 78.95400
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP B 153 OD2
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 GLN A 61 -162.00 -116.02
REMARK 500 GLU A 62 103.65 78.03
REMARK 500 GLU A 63 77.19 52.51
REMARK 500 ASP A 108 77.84 -110.28
REMARK 500 ARG A 149 -2.36 71.93
REMARK 500 GLN B 61 -162.01 -116.87
REMARK 500 GLU B 62 104.07 77.48
REMARK 500 GLU B 63 75.00 52.64
REMARK 500 ASP B 108 78.90 -108.06
REMARK 500 ARG B 149 -1.58 73.99
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 88.6
REMARK 620 3 HOH A 306 O 90.8 85.7
REMARK 620 4 HOH A 320 O 78.8 95.0 169.6
REMARK 620 5 HOH A 321 O 88.1 171.7 86.7 91.9
REMARK 620 6 HOH A 331 O 172.9 92.6 96.2 94.1 91.6
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 O2B 90.4
REMARK 620 3 HOH B 314 O 91.8 87.2
REMARK 620 4 HOH B 317 O 80.1 94.3 171.8
REMARK 620 5 HOH B 327 O 88.3 171.5 84.5 93.7
REMARK 620 6 HOH B 340 O 172.1 91.1 96.0 92.0 91.3
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 GDP B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 202
DBREF 5W22 A 1 169 UNP P01116 RASK_HUMAN 1 169
DBREF 5W22 B 1 169 UNP P01116 RASK_HUMAN 1 169
SEQADV 5W22 HIS A 0 UNP P01116 EXPRESSION TAG
SEQADV 5W22 SER A 118 UNP P01116 CYS 118 ENGINEERED MUTATION
SEQADV 5W22 HIS B 0 UNP P01116 EXPRESSION TAG
SEQADV 5W22 SER B 118 UNP P01116 CYS 118 ENGINEERED MUTATION
SEQRES 1 A 170 HIS MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY
SEQRES 2 A 170 GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN
SEQRES 3 A 170 ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP
SEQRES 4 A 170 SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS
SEQRES 5 A 170 LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR
SEQRES 6 A 170 SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY
SEQRES 7 A 170 PHE LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE
SEQRES 8 A 170 GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL
SEQRES 9 A 170 LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN
SEQRES 10 A 170 LYS SER ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN
SEQRES 11 A 170 ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE
SEQRES 12 A 170 GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA
SEQRES 13 A 170 PHE TYR THR LEU VAL ARG GLU ILE ARG LYS HIS LYS GLU
SEQRES 14 A 170 LYS
SEQRES 1 B 170 HIS MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY
SEQRES 2 B 170 GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN
SEQRES 3 B 170 ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP
SEQRES 4 B 170 SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS
SEQRES 5 B 170 LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR
SEQRES 6 B 170 SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY
SEQRES 7 B 170 PHE LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE
SEQRES 8 B 170 GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL
SEQRES 9 B 170 LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN
SEQRES 10 B 170 LYS SER ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN
SEQRES 11 B 170 ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE
SEQRES 12 B 170 GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA
SEQRES 13 B 170 PHE TYR THR LEU VAL ARG GLU ILE ARG LYS HIS LYS GLU
SEQRES 14 B 170 LYS
HET GDP A 201 28
HET MG A 202 1
HET GDP B 201 28
HET MG B 202 1
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 3 GDP 2(C10 H15 N5 O11 P2)
FORMUL 4 MG 2(MG 2+)
FORMUL 7 HOH *156(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 LYS A 167 1 17
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 LYS B 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 ILE A 55 N TYR A 40
SHEET 3 AA1 6 THR A 2 GLY A 10 1 N TYR A 4 O ASP A 54
SHEET 4 AA1 6 GLY A 77 ALA A 83 1 O LEU A 79 N VAL A 7
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
SHEET 1 AA2 6 ASP B 38 ILE B 46 0
SHEET 2 AA2 6 GLU B 49 ASP B 57 -1 O CYS B 51 N VAL B 44
SHEET 3 AA2 6 THR B 2 GLY B 10 1 N TYR B 4 O ASP B 54
SHEET 4 AA2 6 GLY B 77 ALA B 83 1 O VAL B 81 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
LINK OG SER A 17 MG MG A 202 1555 1555 2.12
LINK O3B GDP A 201 MG MG A 202 1555 1555 2.12
LINK MG MG A 202 O HOH A 306 1555 1555 2.16
LINK MG MG A 202 O HOH A 320 1555 1555 2.01
LINK MG MG A 202 O HOH A 321 1555 1555 2.14
LINK MG MG A 202 O HOH A 331 1555 1555 2.07
LINK OG SER B 17 MG MG B 202 1555 1555 2.13
LINK O2B GDP B 201 MG MG B 202 1555 1555 2.09
LINK MG MG B 202 O HOH B 314 1555 1555 2.10
LINK MG MG B 202 O HOH B 317 1555 1555 2.03
LINK MG MG B 202 O HOH B 327 1555 1555 2.13
LINK MG MG B 202 O HOH B 340 1555 1555 2.08
SITE 1 AC1 21 GLY A 13 VAL A 14 GLY A 15 LYS A 16
SITE 2 AC1 21 SER A 17 ALA A 18 PHE A 28 VAL A 29
SITE 3 AC1 21 ASP A 30 ASN A 116 LYS A 117 ASP A 119
SITE 4 AC1 21 LEU A 120 SER A 145 ALA A 146 LYS A 147
SITE 5 AC1 21 MG A 202 HOH A 306 HOH A 313 HOH A 320
SITE 6 AC1 21 HOH A 331
SITE 1 AC2 6 SER A 17 GDP A 201 HOH A 306 HOH A 320
SITE 2 AC2 6 HOH A 321 HOH A 331
SITE 1 AC3 22 GLY B 13 VAL B 14 GLY B 15 LYS B 16
SITE 2 AC3 22 SER B 17 ALA B 18 PHE B 28 VAL B 29
SITE 3 AC3 22 ASP B 30 ASN B 116 LYS B 117 ASP B 119
SITE 4 AC3 22 LEU B 120 SER B 145 ALA B 146 LYS B 147
SITE 5 AC3 22 MG B 202 HOH B 314 HOH B 317 HOH B 319
SITE 6 AC3 22 HOH B 340 HOH B 361
SITE 1 AC4 6 SER B 17 GDP B 201 HOH B 314 HOH B 317
SITE 2 AC4 6 HOH B 327 HOH B 340
CRYST1 93.177 93.177 118.431 90.00 90.00 120.00 H 3 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 0.010732 0.006196 0.000000 0.00000
SCALE2 0.000000 0.012393 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008444 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.500010 -0.866019 -0.000084 46.58545 1
MTRIX2 2 -0.866019 0.500010 0.000689 26.88253 1
MTRIX3 2 -0.000555 0.000417 -1.000000 23.32969 1
(ATOM LINES ARE NOT SHOWN.)
END
