HEADER COMPLEX (GTP-BINDING/ATP-BINDING) 18-JUN-96 1GUA
TITLE HUMAN RAP1A, RESIDUES 1-167, DOUBLE MUTANT (E30D,K31E) COMPLEXED WITH
TITLE 2 GPPNHP AND THE RAS-BINDING-DOMAIN OF HUMAN C-RAF1, RESIDUES 51-131
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAP1A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-167;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: COMPLEXED TO 5'-GUANOSYL-IMIDO-TRIPHOSPHATE;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: C-RAF1;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: RESIDUES 51-131;
COMPND 12 EC: 2.7.1.-;
COMPND 13 ENGINEERED: YES;
COMPND 14 OTHER_DETAILS: HUMAN RAP1A AND C-RAF1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HUMAN C-RAF1 GENE RESIDUES 51;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: CK600K;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTAC;
SOURCE 10 EXPRESSION_SYSTEM_GENE: HUMAN RAP1A GENE;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: HUMAN C-RAF1 GENE RESIDUES 51;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PGEX-RAFRBD;
SOURCE 20 EXPRESSION_SYSTEM_GENE: HUMAN C-RAF1 GENE, RESIDUES 51-131;
SOURCE 21 OTHER_DETAILS: PURIFIED AS A GST-FUSION PROTEIN WITH THROMBIN
SOURCE 22 CLEAVAGE SITE
KEYWDS ONCOGENE PROTEIN/KINASE/EFFECTOR PROTEIN GTP-BINDING-PROTEIN, COMPLEX
KEYWDS 2 (GTP-BINDING-ATP-BINDING), COMPLEX (GTP-BINDING-ATP-BINDING) COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.NASSAR,A.WITTINGHOFER
REVDAT 4 07-FEB-24 1GUA 1 REMARK
REVDAT 3 03-NOV-21 1GUA 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1GUA 1 VERSN
REVDAT 1 11-JAN-97 1GUA 0
JRNL AUTH N.NASSAR,G.HORN,C.HERRMANN,C.BLOCK,R.JANKNECHT,
JRNL AUTH 2 A.WITTINGHOFER
JRNL TITL RAS/RAP EFFECTOR SPECIFICITY DETERMINED BY CHARGE REVERSAL.
JRNL REF NAT.STRUCT.BIOL. V. 3 723 1996
JRNL REFN ISSN 1072-8368
JRNL PMID 8756332
JRNL DOI 10.1038/NSB0896-723
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.BLOCK,R.JANKNECHT,C.HERRMANN,N.NASSAR,A.WITTINGHOFER
REMARK 1 TITL QUANTITATIVE STRUCTURE-ACTIVITY ANALYSIS CORRELATING RAS/RAF
REMARK 1 TITL 2 INTERACTION IN VITRO TO RAF ACTIVATION IN VIVO
REMARK 1 REF NAT.STRUCT.BIOL. V. 3 244 1996
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.HERRMANN,G.A.MARTIN,A.WITTINGHOFER
REMARK 1 TITL QUANTITATIVE ANALYSIS OF THE COMPLEX BETWEEN P21RAS AND THE
REMARK 1 TITL 2 RAS-BINDING DOMAIN OF THE HUMAN RAF-1 PROTEIN KINASE
REMARK 1 REF J.BIOL.CHEM. V. 270 2901 1995
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
REMARK 1 AUTH N.NASSAR,G.HORN,C.HERRMANN,A.SCHERER,F.MCCORMICK,
REMARK 1 AUTH 2 A.WITTINGHOFER
REMARK 1 TITL THE 2.2 A CRYSTAL STRUCTURE OF THE RAS-BINDING DOMAIN OF THE
REMARK 1 TITL 2 SERINE/THREONINE KINASE C-RAF1 IN COMPLEX WITH RAP1A AND A
REMARK 1 TITL 3 GTP ANALOGUE
REMARK 1 REF NATURE V. 375 554 1995
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
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 : 21693
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) : 0.220
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
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 : 1939
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 89
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.90
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) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.21
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
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) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.940
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:
REMARK 3 THE ELECTRON DENSITY FOR THE SIDE CHAINS OF RESIDUES 104 -
REMARK 3 107 FROM RBD (CHAIN B) IS WEAK.
REMARK 4
REMARK 4 1GUA 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_1000173713.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS HI-STAR
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21975
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 -1.000000 0.000000 0.000000 22.25000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.15000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.90000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.15000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.25000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.90000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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, 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 PRO B 51
REMARK 465 SER B 52
REMARK 465 LYS B 53
REMARK 465 THR B 54
REMARK 465 SER B 55
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 CYS A 141 CA - CB - SG ANGL. DEV. = 8.4 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 ASP A 105 47.04 70.90
REMARK 500 LYS A 117 36.09 71.80
REMARK 500 LEU A 120 60.83 -102.02
REMARK 500 HIS B 105 61.19 -102.91
REMARK 500 LYS B 106 81.45 7.75
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 171 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 17 OG
REMARK 620 2 THR A 35 OG1 81.4
REMARK 620 3 GNP A 170 O3G 171.0 92.2
REMARK 620 4 GNP A 170 O2B 90.1 171.0 96.6
REMARK 620 5 HOH A 501 O 84.0 91.7 90.0 90.5
REMARK 620 6 HOH A 502 O 89.8 85.5 96.0 91.4 173.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 132 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 80 OD1
REMARK 620 2 ASP B 80 OD2 51.0
REMARK 620 3 GLY B 123 O 154.4 154.2
REMARK 620 4 GLU B 125 OE2 130.9 80.2 74.0
REMARK 620 5 GLU B 125 OE1 107.9 69.4 93.6 48.4
REMARK 620 6 HOH B 517 O 80.5 101.1 92.3 118.9 74.6
REMARK 620 7 HOH B 531 O 93.9 89.0 84.9 78.4 124.2 161.1
REMARK 620 8 HOH B 574 O 73.9 123.7 80.5 149.9 151.1 77.3 83.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 171
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 132
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 170
DBREF 1GUA A 1 167 UNP P62834 RAP1A_HUMAN 1 167
DBREF 1GUA B 51 131 UNP P04049 RAF1_HUMAN 51 131
SEQADV 1GUA ASP A 30 UNP P62834 GLU 30 ENGINEERED MUTATION
SEQADV 1GUA GLU A 31 UNP P62834 LYS 31 ENGINEERED MUTATION
SEQRES 1 A 167 MET ARG GLU TYR LYS LEU VAL VAL LEU GLY SER GLY GLY
SEQRES 2 A 167 VAL GLY LYS SER ALA LEU THR VAL GLN PHE VAL GLN GLY
SEQRES 3 A 167 ILE PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SER
SEQRES 4 A 167 TYR ARG LYS GLN VAL GLU VAL ASP CYS GLN GLN CYS MET
SEQRES 5 A 167 LEU GLU ILE LEU ASP THR ALA GLY THR GLU GLN PHE THR
SEQRES 6 A 167 ALA MET ARG ASP LEU TYR MET LYS ASN GLY GLN GLY PHE
SEQRES 7 A 167 ALA LEU VAL TYR SER ILE THR ALA GLN SER THR PHE ASN
SEQRES 8 A 167 ASP LEU GLN ASP LEU ARG GLU GLN ILE LEU ARG VAL LYS
SEQRES 9 A 167 ASP THR GLU ASP VAL PRO MET ILE LEU VAL GLY ASN LYS
SEQRES 10 A 167 CYS ASP LEU GLU ASP GLU ARG VAL VAL GLY LYS GLU GLN
SEQRES 11 A 167 GLY GLN ASN LEU ALA ARG GLN TRP CYS ASN CYS ALA PHE
SEQRES 12 A 167 LEU GLU SER SER ALA LYS SER LYS ILE ASN VAL ASN GLU
SEQRES 13 A 167 ILE PHE TYR ASP LEU VAL ARG GLN ILE ASN ARG
SEQRES 1 B 81 PRO SER LYS THR SER ASN THR ILE ARG VAL PHE LEU PRO
SEQRES 2 B 81 ASN LYS GLN ARG THR VAL VAL ASN VAL ARG ASN GLY MET
SEQRES 3 B 81 SER LEU HIS ASP CYS LEU MET LYS ALA LEU LYS VAL ARG
SEQRES 4 B 81 GLY LEU GLN PRO GLU CYS CYS ALA VAL PHE ARG LEU LEU
SEQRES 5 B 81 HIS GLU HIS LYS GLY LYS LYS ALA ARG LEU ASP TRP ASN
SEQRES 6 B 81 THR ASP ALA ALA SER LEU ILE GLY GLU GLU LEU GLN VAL
SEQRES 7 B 81 ASP PHE LEU
HET MG A 171 1
HET GNP A 170 32
HET CA B 132 1
HETNAM MG MAGNESIUM ION
HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
HETNAM CA CALCIUM ION
FORMUL 3 MG MG 2+
FORMUL 4 GNP C10 H17 N6 O13 P3
FORMUL 5 CA CA 2+
FORMUL 6 HOH *89(H2 O)
HELIX 1 1 LYS A 16 GLN A 25 1 10
HELIX 2 2 ALA A 66 ASN A 74 5 9
HELIX 3 3 GLN A 87 LYS A 104 1 18
HELIX 4 4 GLU A 121 GLU A 123 5 3
HELIX 5 5 LYS A 128 GLN A 137 1 10
HELIX 6 6 VAL A 154 ILE A 165 1 12
HELIX 7 7 LEU B 78 ARG B 89 1 12
HELIX 8 8 PRO B 93 CYS B 95 5 3
HELIX 9 9 ALA B 118 LEU B 121 5 4
SHEET 1 A11 ALA A 142 GLU A 145 0
SHEET 2 A11 PRO A 110 ASN A 116 1 N LEU A 113 O ALA A 142
SHEET 3 A11 GLY A 77 SER A 83 1 N PHE A 78 O PRO A 110
SHEET 4 A11 GLU A 3 GLY A 10 1 N VAL A 7 O GLY A 77
SHEET 5 A11 GLN A 49 ASP A 57 1 N MET A 52 O TYR A 4
SHEET 6 A11 GLU A 37 VAL A 46 -1 N VAL A 46 O GLN A 49
SHEET 7 A11 GLN B 66 ASN B 71 -1 N VAL B 69 O GLU A 37
SHEET 8 A11 THR B 57 LEU B 62 -1 N LEU B 62 O GLN B 66
SHEET 9 A11 GLU B 125 PHE B 130 1 N LEU B 126 O ARG B 59
SHEET 10 A11 CYS B 96 LEU B 102 -1 N PHE B 99 O GLN B 127
SHEET 11 A11 LYS B 108 LEU B 112 -1 N LEU B 112 O VAL B 98
LINK OG SER A 17 MG MG A 171 1555 1555 2.33
LINK OG1 THR A 35 MG MG A 171 1555 1555 2.16
LINK O3G GNP A 170 MG MG A 171 1555 1555 2.10
LINK O2B GNP A 170 MG MG A 171 1555 1555 2.22
LINK MG MG A 171 O HOH A 501 1555 1555 2.21
LINK MG MG A 171 O HOH A 502 1555 1555 2.13
LINK OD1 ASP B 80 CA CA B 132 4556 1555 2.50
LINK OD2 ASP B 80 CA CA B 132 4556 1555 2.55
LINK O GLY B 123 CA CA B 132 1555 1555 2.36
LINK OE2 GLU B 125 CA CA B 132 1555 1555 2.71
LINK OE1 GLU B 125 CA CA B 132 1555 1555 2.55
LINK CA CA B 132 O HOH B 517 1555 1555 2.26
LINK CA CA B 132 O HOH B 531 1555 1555 2.36
LINK CA CA B 132 O HOH B 574 1555 1555 2.32
SITE 1 AC1 5 SER A 17 THR A 35 GNP A 170 HOH A 501
SITE 2 AC1 5 HOH A 502
SITE 1 AC2 6 ASP B 80 GLY B 123 GLU B 125 HOH B 517
SITE 2 AC2 6 HOH B 531 HOH B 574
SITE 1 AC3 25 GLY A 12 GLY A 13 VAL A 14 GLY A 15
SITE 2 AC3 25 LYS A 16 SER A 17 ALA A 18 PHE A 28
SITE 3 AC3 25 VAL A 29 ASP A 30 GLU A 31 PRO A 34
SITE 4 AC3 25 THR A 35 GLN A 50 GLY A 60 ASN A 116
SITE 5 AC3 25 LYS A 117 ASP A 119 SER A 147 ALA A 148
SITE 6 AC3 25 MG A 171 HOH A 501 HOH A 503 HOH A 526
SITE 7 AC3 25 HOH A 537
CRYST1 44.500 71.800 100.300 90.00 90.00 90.00 P 21 21 21 4
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 0.022472 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013928 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009970 0.00000
(ATOM LINES ARE NOT SHOWN.)
END