HEADER ONCOPROTEIN 08-JAN-10 3LBI
TITLE RAS SOAKED IN MAGNESIUM ACETATE AND BACK SOAKED IN CALCIUM ACETATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTPASE HRAS;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-166;
COMPND 5 SYNONYM: TRANSFORMING PROTEIN P21, P21RAS, H-RAS-1, C-H-RAS, HA-RAS,
COMPND 6 GTPASE HRAS, N-TERMINALLY PROCESSED;
COMPND 7 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: HRAS, HRAS1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS ONCOPROTEIN, PROTEIN-NUCLEOTIDE COMPLEX, GTP-BINDING, ACETYLATION,
KEYWDS 2 CELL MEMBRANE, DISEASE MUTATION, GOLGI APPARATUS, LIPOPROTEIN,
KEYWDS 3 MEMBRANE, METHYLATION, NUCLEOTIDE-BINDING, PALMITATE, PRENYLATION,
KEYWDS 4 PROTO-ONCOGENE, S-NITROSYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR G.HOLZAPFEL,G.BUHRMAN,C.MATTOS
REVDAT 3 06-SEP-23 3LBI 1 REMARK LINK
REVDAT 2 12-MAY-10 3LBI 1 JRNL
REVDAT 1 02-MAR-10 3LBI 0
JRNL AUTH G.BUHRMAN,G.HOLZAPFEL,S.FETICS,C.MATTOS
JRNL TITL ALLOSTERIC MODULATION OF RAS POSITIONS Q61 FOR A DIRECT ROLE
JRNL TITL 2 IN CATALYSIS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 4931 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20194776
JRNL DOI 10.1073/PNAS.0912226107
REMARK 2
REMARK 2 RESOLUTION. 2.09 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.4_6)
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.040
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 3 NUMBER OF REFLECTIONS : 11685
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1170
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 25.4046 - 4.1678 0.99 1447 160 0.1703 0.1850
REMARK 3 2 4.1678 - 3.3105 0.99 1392 152 0.1434 0.1709
REMARK 3 3 3.3105 - 2.8927 0.98 1371 151 0.1578 0.2116
REMARK 3 4 2.8927 - 2.6285 0.96 1324 147 0.1640 0.2034
REMARK 3 5 2.6285 - 2.4402 0.95 1303 141 0.1735 0.2473
REMARK 3 6 2.4402 - 2.2965 0.93 1281 140 0.1875 0.2539
REMARK 3 7 2.2965 - 2.1815 0.89 1209 146 0.2312 0.2797
REMARK 3 8 2.1815 - 2.0870 0.86 1188 133 0.2851 0.3726
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 : 0.40
REMARK 3 B_SOL : 60.83
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 1.670
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.84
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 : 0.008 1379
REMARK 3 ANGLE : 1.062 1869
REMARK 3 CHIRALITY : 0.066 207
REMARK 3 PLANARITY : 0.003 241
REMARK 3 DIHEDRAL : 19.526 509
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 3LBI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000057072.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.5
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 RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : OSMIC CONFOCAL MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11685
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.087
REMARK 200 RESOLUTION RANGE LOW (A) : 28.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.13500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.95800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 3K8Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM CALCIUM ACETATE, 20 % PEG 3350,
REMARK 280 0.05% N-OCTYLGLUCOPYRANOSIDE, PH 7.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+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 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 44.35800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 25.61010
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 44.86100
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 44.35800
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 25.61010
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 44.86100
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 44.35800
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 25.61010
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 44.86100
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 44.35800
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 25.61010
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 44.86100
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 44.35800
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 25.61010
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 44.86100
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 44.35800
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 25.61010
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 44.86100
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 51.22021
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 89.72200
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 51.22021
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 89.72200
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 51.22021
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 89.72200
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 51.22021
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 89.72200
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 51.22021
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 89.72200
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 51.22021
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 89.72200
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -122.0 KCAL/MOL
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 BIOMT1 2 -0.500000 -0.866025 0.000000 44.35800
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 76.83031
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -44.35800
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 76.83031
REMARK 350 BIOMT3 3 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 MG MG A 170 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 200 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 273 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 278 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 281 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 303 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 OH TYR A 32 O HOH A 287 2.14
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 ASP A 105 52.13 37.58
REMARK 500 ALA A 122 48.69 -78.57
REMARK 500 ARG A 149 -5.20 75.09
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 168 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 17 OG
REMARK 620 2 THR A 35 OG1 77.4
REMARK 620 3 HOH A 202 O 94.5 85.2
REMARK 620 4 HOH A 203 O 89.2 87.9 171.3
REMARK 620 5 GNP A 528 O2G 165.1 87.8 85.3 89.1
REMARK 620 6 GNP A 528 O2B 96.6 168.3 85.2 102.2 98.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 167 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 28 O
REMARK 620 2 ASP A 30 OD1 83.1
REMARK 620 3 HOH A 244 O 89.3 89.8
REMARK 620 4 HOH A 274 O 163.9 80.9 92.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 169 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 107 O
REMARK 620 2 TYR A 137 O 146.2
REMARK 620 3 HOH A 262 O 106.6 86.2
REMARK 620 4 HOH A 293 O 75.0 73.4 91.4
REMARK 620 5 ACT A 719 O 76.3 137.3 71.7 140.7
REMARK 620 6 ACT A 719 OXT 100.2 107.5 102.5 166.1 46.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 170 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 242 O
REMARK 620 2 HOH A 253 O 70.6
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 528
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 167
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 168
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 169
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 719
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3K8Y RELATED DB: PDB
REMARK 900 WT HIGH RESOLUTION
REMARK 900 RELATED ID: 3K9N RELATED DB: PDB
REMARK 900 Y32F MUTANT
REMARK 900 RELATED ID: 3LBH RELATED DB: PDB
REMARK 900 CALCIUM ACETATE CONTROL SOAK
REMARK 900 RELATED ID: 3LBN RELATED DB: PDB
DBREF 3LBI A 1 166 UNP P01112 RASH_HUMAN 1 166
SEQRES 1 A 166 MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY GLY
SEQRES 2 A 166 VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN ASN
SEQRES 3 A 166 HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SER
SEQRES 4 A 166 TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS LEU
SEQRES 5 A 166 LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR SER
SEQRES 6 A 166 ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY PHE
SEQRES 7 A 166 LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE GLU
SEQRES 8 A 166 ASP ILE HIS GLN TYR ARG GLU GLN ILE LYS ARG VAL LYS
SEQRES 9 A 166 ASP SER ASP ASP VAL PRO MET VAL LEU VAL GLY ASN LYS
SEQRES 10 A 166 CYS ASP LEU ALA ALA ARG THR VAL GLU SER ARG GLN ALA
SEQRES 11 A 166 GLN ASP LEU ALA ARG SER TYR GLY ILE PRO TYR ILE GLU
SEQRES 12 A 166 THR SER ALA LYS THR ARG GLN GLY VAL GLU ASP ALA PHE
SEQRES 13 A 166 TYR THR LEU VAL ARG GLU ILE ARG GLN HIS
HET GNP A 528 32
HET CA A 167 1
HET MG A 168 1
HET CA A 169 1
HET MG A 170 1
HET ACT A 719 4
HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
HETNAM CA CALCIUM ION
HETNAM MG MAGNESIUM ION
HETNAM ACT ACETATE ION
FORMUL 2 GNP C10 H17 N6 O13 P3
FORMUL 3 CA 2(CA 2+)
FORMUL 4 MG 2(MG 2+)
FORMUL 7 ACT C2 H3 O2 1-
FORMUL 8 HOH *119(H2 O)
HELIX 1 1 GLY A 15 ASN A 26 1 12
HELIX 2 2 GLN A 61 ALA A 66 5 6
HELIX 3 3 MET A 67 GLY A 75 1 9
HELIX 4 4 ASN A 86 LYS A 104 1 19
HELIX 5 5 GLU A 126 GLY A 138 1 13
HELIX 6 6 GLY A 151 ARG A 164 1 14
SHEET 1 A 6 GLU A 37 ILE A 46 0
SHEET 2 A 6 GLU A 49 THR A 58 -1 O ILE A 55 N TYR A 40
SHEET 3 A 6 THR A 2 VAL A 9 1 N VAL A 8 O LEU A 56
SHEET 4 A 6 GLY A 77 ALA A 83 1 O VAL A 81 N VAL A 9
SHEET 5 A 6 MET A 111 ASN A 116 1 O ASN A 116 N PHE A 82
SHEET 6 A 6 TYR A 141 GLU A 143 1 O ILE A 142 N LEU A 113
LINK OG SER A 17 MG MG A 168 1555 1555 2.17
LINK O PHE A 28 CA CA A 167 1555 1555 2.40
LINK OD1 ASP A 30 CA CA A 167 1555 1555 2.50
LINK OG1 THR A 35 MG MG A 168 1555 1555 2.27
LINK O ASP A 107 CA CA A 169 1555 1555 2.57
LINK O TYR A 137 CA CA A 169 1555 1555 2.62
LINK CA CA A 167 O HOH A 244 1555 1555 2.54
LINK CA CA A 167 O HOH A 274 1555 1555 2.56
LINK MG MG A 168 O HOH A 202 1555 1555 2.32
LINK MG MG A 168 O HOH A 203 1555 1555 2.23
LINK MG MG A 168 O2G GNP A 528 1555 1555 2.15
LINK MG MG A 168 O2B GNP A 528 1555 1555 2.18
LINK CA CA A 169 O HOH A 262 1555 1555 2.61
LINK CA CA A 169 O HOH A 293 1555 1555 2.71
LINK CA CA A 169 O ACT A 719 1555 1555 2.68
LINK CA CA A 169 OXT ACT A 719 1555 1555 2.70
LINK MG MG A 170 O HOH A 242 1555 1555 2.16
LINK MG MG A 170 O HOH A 253 1555 1555 2.40
SITE 1 AC1 29 GLY A 12 GLY A 13 VAL A 14 GLY A 15
SITE 2 AC1 29 LYS A 16 SER A 17 ALA A 18 PHE A 28
SITE 3 AC1 29 VAL A 29 ASP A 30 GLU A 31 TYR A 32
SITE 4 AC1 29 PRO A 34 THR A 35 GLY A 60 ASN A 116
SITE 5 AC1 29 LYS A 117 ASP A 119 LEU A 120 SER A 145
SITE 6 AC1 29 ALA A 146 LYS A 147 MG A 168 HOH A 202
SITE 7 AC1 29 HOH A 203 HOH A 210 HOH A 224 HOH A 283
SITE 8 AC1 29 HOH A 287
SITE 1 AC2 6 PHE A 28 ASP A 30 GLU A 31 ASP A 33
SITE 2 AC2 6 HOH A 244 HOH A 274
SITE 1 AC3 5 SER A 17 THR A 35 HOH A 202 HOH A 203
SITE 2 AC3 5 GNP A 528
SITE 1 AC4 5 ASP A 107 TYR A 137 HOH A 262 HOH A 293
SITE 2 AC4 5 ACT A 719
SITE 1 AC5 2 HOH A 242 HOH A 253
SITE 1 AC6 7 ARG A 97 LYS A 101 ASP A 107 ASP A 108
SITE 2 AC6 7 VAL A 109 MET A 111 CA A 169
CRYST1 88.716 88.716 134.583 90.00 90.00 120.00 H 3 2 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 0.011272 0.006508 0.000000 0.00000
SCALE2 0.000000 0.013016 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007430 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
