HEADER SIGNALING PROTEIN 06-NOV-09 3KKN
TITLE CRYSTAL STRUCTURE OF H-RAS T35S IN COMPLEX WITH GPPNHP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTPASE HRAS;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: G DOMAIN, 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;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: AG-1;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1
KEYWDS GTP-BINDING, GTPASE, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MURAOKA,F.SHIMA,J.LIAO,Y.IJIRI,K.MATSUMOTO,M.YE,T.INOUE,T.KATAOKA
REVDAT 3 01-NOV-23 3KKN 1 REMARK SEQADV LINK
REVDAT 2 12-FEB-14 3KKN 1 JRNL VERSN
REVDAT 1 16-JUN-10 3KKN 0
JRNL AUTH F.SHIMA,Y.IJIRI,S.MURAOKA,J.LIAO,M.YE,M.ARAKI,K.MATSUMOTO,
JRNL AUTH 2 N.YAMAMOTO,T.SUGIMOTO,Y.YOSHIKAWA,T.KUMASAKA,M.YAMAMOTO,
JRNL AUTH 3 A.TAMURA,T.KATAOKA
JRNL TITL STRUCTURAL BASIS FOR CONFORMATIONAL DYNAMICS OF GTP-BOUND
JRNL TITL 2 RAS PROTEIN
JRNL REF J.BIOL.CHEM. V. 285 22696 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20479006
JRNL DOI 10.1074/JBC.M110.125161
REMARK 2
REMARK 2 RESOLUTION. 2.09 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 10128
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 508
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) : 2.09
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 716
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.45
REMARK 3 BIN R VALUE (WORKING SET) : 0.1750
REMARK 3 BIN FREE R VALUE SET COUNT : 46
REMARK 3 BIN FREE R VALUE : 0.2400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1322
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 66
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
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): 0.242
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.197
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.126
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.534
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1430 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1942 ; 1.171 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 174 ; 5.007 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 74 ;35.544 ;24.054
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 254 ;14.723 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;15.874 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 211 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1092 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 851 ; 0.654 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1380 ; 1.276 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 579 ; 1.876 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 562 ; 3.240 ; 4.500
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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
REMARK 4
REMARK 4 3KKN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-NOV-09.
REMARK 100 THE DEPOSITION ID IS D_1000056110.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAY-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10645
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.090
REMARK 200 RESOLUTION RANGE LOW (A) : 26.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 14.30
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : 0.08800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 45.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.60
REMARK 200 R MERGE FOR SHELL (I) : 0.28200
REMARK 200 R SYM FOR SHELL (I) : 0.28200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 14.70
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 5P21
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, AMMONIUM SULFATE, PEG-MME-5000,
REMARK 280 PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 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 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 17.29150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 60.99900
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 17.29150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 60.99900
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 17.29150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 41.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 60.99900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 17.29150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 41.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 60.99900
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 300 REMARK: AUTHOR DETERMINED BIOLOGICAL UNIT: UNKNOWN
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 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 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 GLY A -5
REMARK 465 PRO A -4
REMARK 465 LEU A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 ASP A 0
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 ARG A 149 -5.17 81.90
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 GNP A 167 O2G 177.1
REMARK 620 3 GNP A 167 O2B 85.4 92.0
REMARK 620 4 HOH A1001 O 87.3 94.2 96.1
REMARK 620 5 HOH A1002 O 85.7 92.9 84.1 172.9
REMARK 620 6 HOH A1003 O 88.1 94.5 172.9 86.3 92.7
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 GNP A 167
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 168
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1X1S RELATED DB: PDB
REMARK 900 RELATED ID: 1X1R RELATED DB: PDB
REMARK 900 RELATED ID: 3KKM RELATED DB: PDB
REMARK 900 RELATED ID: 3KKO RELATED DB: PDB
REMARK 900 RELATED ID: 3KKP RELATED DB: PDB
REMARK 900 RELATED ID: 3KKQ RELATED DB: PDB
DBREF 3KKN A 1 166 UNP P01112 RASH_HUMAN 1 166
SEQADV 3KKN GLY A -5 UNP P01112 EXPRESSION TAG
SEQADV 3KKN PRO A -4 UNP P01112 EXPRESSION TAG
SEQADV 3KKN LEU A -3 UNP P01112 EXPRESSION TAG
SEQADV 3KKN GLY A -2 UNP P01112 EXPRESSION TAG
SEQADV 3KKN SER A -1 UNP P01112 EXPRESSION TAG
SEQADV 3KKN ASP A 0 UNP P01112 EXPRESSION TAG
SEQADV 3KKN SER A 35 UNP P01112 THR 35 ENGINEERED MUTATION
SEQRES 1 A 172 GLY PRO LEU GLY SER ASP MET THR GLU TYR LYS LEU VAL
SEQRES 2 A 172 VAL VAL GLY ALA GLY GLY VAL GLY LYS SER ALA LEU THR
SEQRES 3 A 172 ILE GLN LEU ILE GLN ASN HIS PHE VAL ASP GLU TYR ASP
SEQRES 4 A 172 PRO SER ILE GLU ASP SER TYR ARG LYS GLN VAL VAL ILE
SEQRES 5 A 172 ASP GLY GLU THR CYS LEU LEU ASP ILE LEU ASP THR ALA
SEQRES 6 A 172 GLY GLN GLU GLU TYR SER ALA MET ARG ASP GLN TYR MET
SEQRES 7 A 172 ARG THR GLY GLU GLY PHE LEU CYS VAL PHE ALA ILE ASN
SEQRES 8 A 172 ASN THR LYS SER PHE GLU ASP ILE HIS GLN TYR ARG GLU
SEQRES 9 A 172 GLN ILE LYS ARG VAL LYS ASP SER ASP ASP VAL PRO MET
SEQRES 10 A 172 VAL LEU VAL GLY ASN LYS CYS ASP LEU ALA ALA ARG THR
SEQRES 11 A 172 VAL GLU SER ARG GLN ALA GLN ASP LEU ALA ARG SER TYR
SEQRES 12 A 172 GLY ILE PRO TYR ILE GLU THR SER ALA LYS THR ARG GLN
SEQRES 13 A 172 GLY VAL GLU ASP ALA PHE TYR THR LEU VAL ARG GLU ILE
SEQRES 14 A 172 ARG GLN HIS
HET GNP A 167 32
HET MG A 168 1
HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
HETNAM MG MAGNESIUM ION
FORMUL 2 GNP C10 H17 N6 O13 P3
FORMUL 3 MG MG 2+
FORMUL 4 HOH *66(H2 O)
HELIX 1 1 GLY A 15 GLN A 25 1 11
HELIX 2 2 MET A 67 GLY A 75 1 9
HELIX 3 3 ASN A 86 ASP A 92 1 7
HELIX 4 4 ASP A 92 ASP A 105 1 14
HELIX 5 5 GLU A 126 GLY A 138 1 13
HELIX 6 6 GLY A 151 GLN A 165 1 15
SHEET 1 A 6 ASP A 38 ILE A 46 0
SHEET 2 A 6 GLU A 49 ASP A 57 -1 O CYS A 51 N VAL A 44
SHEET 3 A 6 THR A 2 VAL A 9 1 N TYR A 4 O ASP A 54
SHEET 4 A 6 GLY A 77 ALA A 83 1 O LEU A 79 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 2.15
LINK O2G GNP A 167 MG MG A 168 1555 1555 1.84
LINK O2B GNP A 167 MG MG A 168 1555 1555 2.14
LINK MG MG A 168 O HOH A1001 1555 1555 2.04
LINK MG MG A 168 O HOH A1002 1555 1555 2.23
LINK MG MG A 168 O HOH A1003 1555 1555 2.11
SITE 1 AC1 20 GLY A 12 GLY A 13 VAL A 14 GLY A 15
SITE 2 AC1 20 LYS A 16 SER A 17 ALA A 18 ASN A 116
SITE 3 AC1 20 LYS A 117 ASP A 119 LEU A 120 SER A 145
SITE 4 AC1 20 ALA A 146 LYS A 147 MG A 168 HOH A1001
SITE 5 AC1 20 HOH A1002 HOH A1003 HOH A1017 HOH A1036
SITE 1 AC2 5 SER A 17 GNP A 167 HOH A1001 HOH A1002
SITE 2 AC2 5 HOH A1003
CRYST1 34.583 82.000 121.998 90.00 90.00 90.00 I 2 2 2 8
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 0.028916 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012195 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008197 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
