HEADER GTP-BINDING 15-DEC-96 1JAI
TITLE H-RAS P21 PROTEIN MUTANT G12P, COMPLEXED WITH GUANOSINE-5'-[BETA,
TITLE 2 GAMMA-METHYLENE] TRIPHOSPHATE AND MANGANESE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: C-HA-RAS;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 1 - 166;
COMPND 5 SYNONYM: G-DOMAIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 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: H-RAS-1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: CK 600 K;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PTAC RAS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTAC
KEYWDS GTP HYDROLYSIS, SIGNAL TRANSDUCTION, CANCER, G-DOMAIN, GTP-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR T.SCHWEINS,K.SCHEFFZEK,R.ASSHEUER,A.WITTINGHOFER
REVDAT 5 03-APR-24 1JAI 1 REMARK
REVDAT 4 07-FEB-24 1JAI 1 REMARK
REVDAT 3 03-NOV-21 1JAI 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1JAI 1 VERSN
REVDAT 1 23-JUL-97 1JAI 0
JRNL AUTH T.SCHWEINS,K.SCHEFFZEK,R.ASSHEUER,A.WITTINGHOFER
JRNL TITL THE ROLE OF THE METAL ION IN THE P21RAS CATALYSED
JRNL TITL 2 GTP-HYDROLYSIS: MN2+ VERSUS MG2+.
JRNL REF J.MOL.BIOL. V. 266 847 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9102473
JRNL DOI 10.1006/JMBI.1996.0814
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.F.PAI,U.KRENGEL,G.A.PETSKO,R.S.GOODY,W.KABSCH,
REMARK 1 AUTH 2 A.WITTINGHOFER
REMARK 1 TITL REFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE CONFORMATION
REMARK 1 TITL 2 OF H-RAS P21 AT 1.35 A RESOLUTION: IMPLICATIONS FOR THE
REMARK 1 TITL 3 MECHANISM OF GTP HYDROLYSIS
REMARK 1 REF EMBO J. V. 9 2351 1990
REMARK 1 REFN ISSN 0261-4189
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.H.SEEBURG,W.W.COLBY,D.J.CAPON,D.V.GOEDDEL,A.D.LEVINSON
REMARK 1 TITL BIOLOGICAL PROPERTIES OF HUMAN C-HA-RAS1 GENES MUTATED AT
REMARK 1 TITL 2 CODON 12
REMARK 1 REF NATURE V. 312 71 1984
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 12733
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1326
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 41
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.00
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.25
REMARK 3 LOW RESOLUTION CUTOFF (A) : 8.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JAI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174299.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-NOV-92
REMARK 200 TEMPERATURE (KELVIN) : 277
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 : ELLIOTT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : FRANKS DOUBLE MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS (W.KABSCH)
REMARK 200 DATA SCALING SOFTWARE : XSCALE (KABSCH)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13392
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.14000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: C-H-RAS:GPPNP:MG
REMARK 200
REMARK 200 REMARK: CRYSTALS ARE ISOMORPHOUS TO C-H-RAS:GPPNP:MG2+, NO
REMARK 200 ROTATION/TRANSLATION CALCULATIONS REQUIRED.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 30.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-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 106.93333
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 53.46667
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 53.46667
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 106.93333
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: DIMERIC
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 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
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 30 64.17 -110.09
REMARK 500 ASP A 33 81.74 -159.56
REMARK 500 ILE A 36 -60.28 -102.16
REMARK 500 GLU A 37 111.35 -166.43
REMARK 500 GLN A 61 150.27 137.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 161 0.07 SIDE CHAIN
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 MN A 168 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 17 OG
REMARK 620 2 THR A 35 OG1 75.8
REMARK 620 3 GCP A 167 O2G 169.8 96.1
REMARK 620 4 GCP A 167 O2B 97.8 173.6 90.3
REMARK 620 5 HOH A 170 O 86.1 86.8 87.2 93.5
REMARK 620 6 HOH A 177 O 86.7 88.2 99.4 90.8 172.1
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 MN A 168
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GCP A 167
DBREF 1JAI A 1 166 UNP P01112 RASH_HUMAN 1 166
SEQADV 1JAI PRO A 12 UNP P01112 GLY 12 ENGINEERED MUTATION
SEQRES 1 A 166 MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA PRO 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 MN A 168 1
HET GCP A 167 32
HETNAM MN MANGANESE (II) ION
HETNAM GCP PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER
FORMUL 2 MN MN 2+
FORMUL 3 GCP C11 H18 N5 O13 P3
FORMUL 4 HOH *41(H2 O)
HELIX 1 1 LYS A 16 GLN A 25 1 10
HELIX 2 2 GLU A 62 THR A 74 5 13
HELIX 3 3 THR A 87 LYS A 104 1 18
HELIX 4 4 SER A 127 TYR A 137 1 11
HELIX 5 5 VAL A 152 ARG A 164 1 13
SHEET 1 A 6 PRO A 140 GLU A 143 0
SHEET 2 A 6 PRO A 110 ASN A 116 1 N LEU A 113 O PRO A 140
SHEET 3 A 6 GLY A 77 ALA A 83 1 N PHE A 78 O PRO A 110
SHEET 4 A 6 THR A 2 GLY A 10 1 N VAL A 7 O GLY A 77
SHEET 5 A 6 GLU A 49 THR A 58 1 N LEU A 52 O THR A 2
SHEET 6 A 6 GLU A 37 ILE A 46 -1 N ILE A 46 O GLU A 49
LINK OG SER A 17 MN MN A 168 1555 1555 2.31
LINK OG1 THR A 35 MN MN A 168 1555 1555 2.26
LINK O2G GCP A 167 MN MN A 168 1555 1555 2.23
LINK O2B GCP A 167 MN MN A 168 1555 1555 2.23
LINK MN MN A 168 O HOH A 170 1555 1555 2.38
LINK MN MN A 168 O HOH A 177 1555 1555 2.44
SITE 1 AC1 5 SER A 17 THR A 35 GCP A 167 HOH A 170
SITE 2 AC1 5 HOH A 177
SITE 1 AC2 24 PRO A 12 GLY A 13 VAL A 14 GLY A 15
SITE 2 AC2 24 LYS A 16 SER A 17 ALA A 18 PHE A 28
SITE 3 AC2 24 VAL A 29 ASP A 30 TYR A 32 PRO A 34
SITE 4 AC2 24 THR A 35 ASN A 116 LYS A 117 ASP A 119
SITE 5 AC2 24 LEU A 120 SER A 145 ALA A 146 LYS A 147
SITE 6 AC2 24 MN A 168 HOH A 169 HOH A 175 HOH A 177
CRYST1 40.000 40.000 160.400 90.00 90.00 120.00 P 32 2 1 6
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 0.025000 0.014434 0.000000 0.00000
SCALE2 0.000000 0.028868 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006234 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
