HEADER HYDROLASE 13-FEB-17 5US4
TITLE CRYSTAL STRUCTURE OF HUMAN KRAS G12D MUTANT 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;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS KRAS, GTPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.TRAN,A.KAPLAN,B.R.STOCKWELL,L.TONG
REVDAT 4 06-MAR-24 5US4 1 LINK
REVDAT 3 07-MAR-18 5US4 1 REMARK
REVDAT 2 27-SEP-17 5US4 1 REMARK
REVDAT 1 22-MAR-17 5US4 0
JRNL AUTH M.E.WELSCH,A.KAPLAN,J.M.CHAMBERS,M.E.STOKES,P.H.BOS,A.ZASK,
JRNL AUTH 2 Y.ZHANG,M.SANCHEZ-MARTIN,M.A.BADGLEY,C.S.HUANG,T.H.TRAN,
JRNL AUTH 3 H.AKKIRAJU,L.M.BROWN,R.NANDAKUMAR,S.CREMERS,W.S.YANG,L.TONG,
JRNL AUTH 4 K.P.OLIVE,A.FERRANDO,B.R.STOCKWELL
JRNL TITL MULTIVALENT SMALL-MOLECULE PAN-RAS INHIBITORS.
JRNL REF CELL V. 168 878 2017
JRNL REFN ISSN 1097-4172
JRNL PMID 28235199
JRNL DOI 10.1016/J.CELL.2017.02.006
REMARK 2
REMARK 2 RESOLUTION. 1.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1685
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 33635
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1687
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 38.5331 - 4.1862 0.88 2449 135 0.1544 0.1742
REMARK 3 2 4.1862 - 3.3233 0.92 2547 134 0.1438 0.1943
REMARK 3 3 3.3233 - 2.9034 0.94 2611 145 0.1646 0.1825
REMARK 3 4 2.9034 - 2.6380 0.95 2666 129 0.1814 0.2059
REMARK 3 5 2.6380 - 2.4489 0.96 2690 136 0.1731 0.2172
REMARK 3 6 2.4489 - 2.3046 0.97 2677 128 0.1660 0.1914
REMARK 3 7 2.3046 - 2.1892 0.97 2674 147 0.1539 0.1962
REMARK 3 8 2.1892 - 2.0939 0.98 2765 151 0.1621 0.1940
REMARK 3 9 2.0939 - 2.0133 0.98 2712 134 0.1685 0.2166
REMARK 3 10 2.0133 - 1.9438 0.99 2730 163 0.1732 0.2620
REMARK 3 11 1.9438 - 1.8830 0.99 2745 144 0.1846 0.2364
REMARK 3 12 1.8830 - 1.8292 0.96 2682 141 0.2115 0.2610
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.590
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.020 2719
REMARK 3 ANGLE : 1.791 3673
REMARK 3 CHIRALITY : 0.262 418
REMARK 3 PLANARITY : 0.008 464
REMARK 3 DIHEDRAL : 16.714 1031
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0053 38.1037 -11.9575
REMARK 3 T TENSOR
REMARK 3 T11: 0.1092 T22: 0.1023
REMARK 3 T33: 0.1149 T12: 0.0028
REMARK 3 T13: -0.0162 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 1.1286 L22: 0.7222
REMARK 3 L33: 0.6493 L12: 0.3251
REMARK 3 L13: -0.3917 L23: -0.2345
REMARK 3 S TENSOR
REMARK 3 S11: 0.0043 S12: -0.0101 S13: -0.0178
REMARK 3 S21: 0.0028 S22: 0.0056 S23: -0.0102
REMARK 3 S31: 0.0037 S32: 0.0045 S33: -0.0145
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 5US4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1000226338.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 9.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-003
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33643
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.23900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
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 (%): 48.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM PHOSPHATE DIBASIC, 20%
REMARK 280 W/V PEG3350, PH 9.1, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
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 46.91100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.08408
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.45067
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 46.91100
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 27.08408
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 40.45067
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 46.91100
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 27.08408
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 40.45067
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 54.16816
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 80.90133
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 54.16816
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 80.90133
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 54.16816
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 80.90133
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 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 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 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 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 GLY A 60
REMARK 465 GLN A 61
REMARK 465 GLU A 62
REMARK 465 GLU A 63
REMARK 465 TYR A 64
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 GLY B 60
REMARK 465 GLN B 61
REMARK 465 GLU B 62
REMARK 465 GLU B 63
REMARK 465 TYR B 64
REMARK 465 SER B 65
REMARK 465 ALA B 66
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 OD1 ASP B 12 O HOH B 301 1.81
REMARK 500 OD1 ASP A 12 O HOH A 301 1.82
REMARK 500 O HOH A 322 O HOH A 409 2.14
REMARK 500 OD1 ASP B 108 O HOH B 302 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 LYS A 104 CD - CE - NZ ANGL. DEV. = 16.2 DEGREES
REMARK 500 ARG A 135 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG B 135 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 31 58.30 -142.41
REMARK 500 ASP A 33 115.36 -37.49
REMARK 500 ARG A 149 -1.55 72.25
REMARK 500 ASP B 33 114.78 -38.27
REMARK 500 ASP B 108 79.19 -112.80
REMARK 500 ARG B 149 -1.63 72.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 17 OG
REMARK 620 2 GDP A 201 O2B 92.3
REMARK 620 3 HOH A 310 O 173.6 88.7
REMARK 620 4 HOH A 312 O 94.7 84.8 91.6
REMARK 620 5 HOH A 327 O 84.8 96.8 88.9 178.4
REMARK 620 6 HOH A 338 O 90.6 172.7 89.2 88.3 90.2
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 92.4
REMARK 620 3 HOH B 314 O 174.4 88.1
REMARK 620 4 HOH B 324 O 91.1 172.7 89.0
REMARK 620 5 HOH B 333 O 84.7 97.2 89.7 89.5
REMARK 620 6 HOH B 344 O 93.7 84.9 91.9 88.5 177.4
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 GOL 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 GOL B 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UQW RELATED DB: PDB
REMARK 900 RELATED ID: 5USJ RELATED DB: PDB
DBREF 5US4 A 1 169 UNP P01116 RASK_HUMAN 1 169
DBREF 5US4 B 1 169 UNP P01116 RASK_HUMAN 1 169
SEQADV 5US4 MET A -19 UNP P01116 EXPRESSION TAG
SEQADV 5US4 GLY A -18 UNP P01116 EXPRESSION TAG
SEQADV 5US4 SER A -17 UNP P01116 EXPRESSION TAG
SEQADV 5US4 SER A -16 UNP P01116 EXPRESSION TAG
SEQADV 5US4 HIS A -15 UNP P01116 EXPRESSION TAG
SEQADV 5US4 HIS A -14 UNP P01116 EXPRESSION TAG
SEQADV 5US4 HIS A -13 UNP P01116 EXPRESSION TAG
SEQADV 5US4 HIS A -12 UNP P01116 EXPRESSION TAG
SEQADV 5US4 HIS A -11 UNP P01116 EXPRESSION TAG
SEQADV 5US4 HIS A -10 UNP P01116 EXPRESSION TAG
SEQADV 5US4 SER A -9 UNP P01116 EXPRESSION TAG
SEQADV 5US4 SER A -8 UNP P01116 EXPRESSION TAG
SEQADV 5US4 GLY A -7 UNP P01116 EXPRESSION TAG
SEQADV 5US4 LEU A -6 UNP P01116 EXPRESSION TAG
SEQADV 5US4 VAL A -5 UNP P01116 EXPRESSION TAG
SEQADV 5US4 PRO A -4 UNP P01116 EXPRESSION TAG
SEQADV 5US4 ARG A -3 UNP P01116 EXPRESSION TAG
SEQADV 5US4 GLY A -2 UNP P01116 EXPRESSION TAG
SEQADV 5US4 SER A -1 UNP P01116 EXPRESSION TAG
SEQADV 5US4 HIS A 0 UNP P01116 EXPRESSION TAG
SEQADV 5US4 ASP A 12 UNP P01116 GLY 12 ENGINEERED MUTATION
SEQADV 5US4 MET B -19 UNP P01116 EXPRESSION TAG
SEQADV 5US4 GLY B -18 UNP P01116 EXPRESSION TAG
SEQADV 5US4 SER B -17 UNP P01116 EXPRESSION TAG
SEQADV 5US4 SER B -16 UNP P01116 EXPRESSION TAG
SEQADV 5US4 HIS B -15 UNP P01116 EXPRESSION TAG
SEQADV 5US4 HIS B -14 UNP P01116 EXPRESSION TAG
SEQADV 5US4 HIS B -13 UNP P01116 EXPRESSION TAG
SEQADV 5US4 HIS B -12 UNP P01116 EXPRESSION TAG
SEQADV 5US4 HIS B -11 UNP P01116 EXPRESSION TAG
SEQADV 5US4 HIS B -10 UNP P01116 EXPRESSION TAG
SEQADV 5US4 SER B -9 UNP P01116 EXPRESSION TAG
SEQADV 5US4 SER B -8 UNP P01116 EXPRESSION TAG
SEQADV 5US4 GLY B -7 UNP P01116 EXPRESSION TAG
SEQADV 5US4 LEU B -6 UNP P01116 EXPRESSION TAG
SEQADV 5US4 VAL B -5 UNP P01116 EXPRESSION TAG
SEQADV 5US4 PRO B -4 UNP P01116 EXPRESSION TAG
SEQADV 5US4 ARG B -3 UNP P01116 EXPRESSION TAG
SEQADV 5US4 GLY B -2 UNP P01116 EXPRESSION TAG
SEQADV 5US4 SER B -1 UNP P01116 EXPRESSION TAG
SEQADV 5US4 HIS B 0 UNP P01116 EXPRESSION TAG
SEQADV 5US4 ASP B 12 UNP P01116 GLY 12 ENGINEERED MUTATION
SEQRES 1 A 189 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 189 LEU VAL PRO ARG GLY SER HIS MET THR GLU TYR LYS LEU
SEQRES 3 A 189 VAL VAL VAL GLY ALA ASP GLY VAL GLY LYS SER ALA LEU
SEQRES 4 A 189 THR ILE GLN LEU ILE GLN ASN HIS PHE VAL ASP GLU TYR
SEQRES 5 A 189 ASP PRO THR ILE GLU ASP SER TYR ARG LYS GLN VAL VAL
SEQRES 6 A 189 ILE ASP GLY GLU THR CYS LEU LEU ASP ILE LEU ASP THR
SEQRES 7 A 189 ALA GLY GLN GLU GLU TYR SER ALA MET ARG ASP GLN TYR
SEQRES 8 A 189 MET ARG THR GLY GLU GLY PHE LEU CYS VAL PHE ALA ILE
SEQRES 9 A 189 ASN ASN THR LYS SER PHE GLU ASP ILE HIS HIS TYR ARG
SEQRES 10 A 189 GLU GLN ILE LYS ARG VAL LYS ASP SER GLU ASP VAL PRO
SEQRES 11 A 189 MET VAL LEU VAL GLY ASN LYS CYS ASP LEU PRO SER ARG
SEQRES 12 A 189 THR VAL ASP THR LYS GLN ALA GLN ASP LEU ALA ARG SER
SEQRES 13 A 189 TYR GLY ILE PRO PHE ILE GLU THR SER ALA LYS THR ARG
SEQRES 14 A 189 GLN GLY VAL ASP ASP ALA PHE TYR THR LEU VAL ARG GLU
SEQRES 15 A 189 ILE ARG LYS HIS LYS GLU LYS
SEQRES 1 B 189 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 189 LEU VAL PRO ARG GLY SER HIS MET THR GLU TYR LYS LEU
SEQRES 3 B 189 VAL VAL VAL GLY ALA ASP GLY VAL GLY LYS SER ALA LEU
SEQRES 4 B 189 THR ILE GLN LEU ILE GLN ASN HIS PHE VAL ASP GLU TYR
SEQRES 5 B 189 ASP PRO THR ILE GLU ASP SER TYR ARG LYS GLN VAL VAL
SEQRES 6 B 189 ILE ASP GLY GLU THR CYS LEU LEU ASP ILE LEU ASP THR
SEQRES 7 B 189 ALA GLY GLN GLU GLU TYR SER ALA MET ARG ASP GLN TYR
SEQRES 8 B 189 MET ARG THR GLY GLU GLY PHE LEU CYS VAL PHE ALA ILE
SEQRES 9 B 189 ASN ASN THR LYS SER PHE GLU ASP ILE HIS HIS TYR ARG
SEQRES 10 B 189 GLU GLN ILE LYS ARG VAL LYS ASP SER GLU ASP VAL PRO
SEQRES 11 B 189 MET VAL LEU VAL GLY ASN LYS CYS ASP LEU PRO SER ARG
SEQRES 12 B 189 THR VAL ASP THR LYS GLN ALA GLN ASP LEU ALA ARG SER
SEQRES 13 B 189 TYR GLY ILE PRO PHE ILE GLU THR SER ALA LYS THR ARG
SEQRES 14 B 189 GLN GLY VAL ASP ASP ALA PHE TYR THR LEU VAL ARG GLU
SEQRES 15 B 189 ILE ARG LYS HIS LYS GLU LYS
HET GDP A 201 28
HET MG A 202 1
HET GOL A 203 6
HET GDP B 201 28
HET MG B 202 1
HET GOL B 203 6
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GDP 2(C10 H15 N5 O11 P2)
FORMUL 4 MG 2(MG 2+)
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 9 HOH *239(H2 O)
HELIX 1 AA1 GLY A 15 ASN A 26 1 12
HELIX 2 AA2 ALA A 66 GLY A 75 1 10
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 ARG B 68 GLY B 75 1 8
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 CYS A 51 N VAL A 44
SHEET 3 AA1 6 THR A 2 VAL A 9 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 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 LEU B 53 N LYS B 42
SHEET 3 AA2 6 THR B 2 VAL B 9 1 N VAL B 8 O LEU B 56
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 O2B GDP A 201 MG MG A 202 1555 1555 2.14
LINK MG MG A 202 O HOH A 310 1555 1555 2.18
LINK MG MG A 202 O HOH A 312 1555 1555 2.17
LINK MG MG A 202 O HOH A 327 1555 1555 2.16
LINK MG MG A 202 O HOH A 338 1555 1555 2.15
LINK OG SER B 17 MG MG B 202 1555 1555 2.12
LINK O2B GDP B 201 MG MG B 202 1555 1555 2.10
LINK MG MG B 202 O HOH B 314 1555 1555 2.24
LINK MG MG B 202 O HOH B 324 1555 1555 2.18
LINK MG MG B 202 O HOH B 333 1555 1555 2.14
LINK MG MG B 202 O HOH B 344 1555 1555 2.19
SITE 1 AC1 22 GLY A 13 VAL A 14 GLY A 15 LYS A 16
SITE 2 AC1 22 SER A 17 ALA A 18 PHE A 28 ASP A 30
SITE 3 AC1 22 ASN A 116 LYS A 117 ASP A 119 LEU A 120
SITE 4 AC1 22 SER A 145 ALA A 146 LYS A 147 MG A 202
SITE 5 AC1 22 HOH A 310 HOH A 312 HOH A 324 HOH A 344
SITE 6 AC1 22 HOH A 379 HOH A 403
SITE 1 AC2 6 SER A 17 GDP A 201 HOH A 310 HOH A 312
SITE 2 AC2 6 HOH A 327 HOH A 338
SITE 1 AC3 7 ASN A 85 GLU A 91 LEU A 120 PRO A 121
SITE 2 AC3 7 SER A 122 LEU A 133 HOH A 340
SITE 1 AC4 22 GLY B 13 VAL B 14 GLY B 15 LYS B 16
SITE 2 AC4 22 SER B 17 ALA B 18 PHE B 28 ASP B 30
SITE 3 AC4 22 ASN B 116 LYS B 117 ASP B 119 LEU B 120
SITE 4 AC4 22 SER B 145 ALA B 146 LYS B 147 MG B 202
SITE 5 AC4 22 HOH B 314 HOH B 322 HOH B 343 HOH B 344
SITE 6 AC4 22 HOH B 372 HOH B 394
SITE 1 AC5 6 SER B 17 GDP B 201 HOH B 314 HOH B 324
SITE 2 AC5 6 HOH B 333 HOH B 344
SITE 1 AC6 6 ASN B 85 GLU B 91 PRO B 121 SER B 122
SITE 2 AC6 6 LEU B 133 HOH B 328
CRYST1 93.822 93.822 121.352 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 0.010658 0.006154 0.000000 0.00000
SCALE2 0.000000 0.012307 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008240 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
