HEADER TRANSLATION 18-SEP-14 4RD1
TITLE STRUCTURE OF AIF2-GAMMA H97A VARIANT FROM SULFOLOBUS SOLFATARICUS
TITLE 2 BOUND TO GTP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSLATION INITIATION FACTOR 2 SUBUNIT GAMMA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: AIF2-GAMMA SUBUNIT;
COMPND 5 SYNONYM: AIF2-GAMMA, EIF-2-GAMMA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE 3 ORGANISM_TAXID: 273057;
SOURCE 4 STRAIN: ATCC 35092 / DSM 1617 / JCM 11322 / P2;
SOURCE 5 GENE: EIF2G, SSO0412, SULFOLOBUS SOLFATARICUS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS ROSSMANN-FOLD, TRANSLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR E.DUBIEZ,A.ALEKSANDROV,C.LAZENNEC-SCHURDEVIN,Y.MECHULAM,E.SCHMITT
REVDAT 4 20-SEP-23 4RD1 1 REMARK SEQADV LINK
REVDAT 3 22-NOV-17 4RD1 1 REMARK
REVDAT 2 29-JUL-15 4RD1 1 TITLE
REVDAT 1 27-MAY-15 4RD1 0
JRNL AUTH E.DUBIEZ,A.ALEKSANDROV,C.LAZENNEC-SCHURDEVIN,Y.MECHULAM,
JRNL AUTH 2 E.SCHMITT
JRNL TITL IDENTIFICATION OF A SECOND GTP-BOUND MAGNESIUM ION IN
JRNL TITL 2 ARCHAEAL INITIATION FACTOR 2.
JRNL REF NUCLEIC ACIDS RES. V. 43 2946 2015
JRNL REFN ISSN 0305-1048
JRNL PMID 25690901
JRNL DOI 10.1093/NAR/GKV053
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 65988
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 3348
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 44.1311 - 4.3241 1.00 2813 178 0.1598 0.1914
REMARK 3 2 4.3241 - 3.4325 1.00 2708 147 0.1442 0.1569
REMARK 3 3 3.4325 - 2.9988 1.00 2669 147 0.1559 0.1664
REMARK 3 4 2.9988 - 2.7246 1.00 2635 126 0.1674 0.1811
REMARK 3 5 2.7246 - 2.5294 1.00 2638 149 0.1678 0.2093
REMARK 3 6 2.5294 - 2.3802 1.00 2638 155 0.1666 0.2014
REMARK 3 7 2.3802 - 2.2610 1.00 2618 136 0.1598 0.1934
REMARK 3 8 2.2610 - 2.1626 1.00 2627 133 0.1563 0.1708
REMARK 3 9 2.1626 - 2.0794 1.00 2634 130 0.1507 0.1780
REMARK 3 10 2.0794 - 2.0076 1.00 2573 140 0.1587 0.1770
REMARK 3 11 2.0076 - 1.9448 1.00 2604 139 0.1551 0.1973
REMARK 3 12 1.9448 - 1.8892 1.00 2620 142 0.1492 0.2079
REMARK 3 13 1.8892 - 1.8395 1.00 2593 125 0.1537 0.2185
REMARK 3 14 1.8395 - 1.7946 1.00 2589 159 0.1590 0.2062
REMARK 3 15 1.7946 - 1.7538 1.00 2607 134 0.1564 0.2076
REMARK 3 16 1.7538 - 1.7165 1.00 2603 108 0.1527 0.2015
REMARK 3 17 1.7165 - 1.6822 1.00 2604 122 0.1616 0.1845
REMARK 3 18 1.6822 - 1.6504 1.00 2535 166 0.1763 0.2269
REMARK 3 19 1.6504 - 1.6209 1.00 2641 128 0.1944 0.2810
REMARK 3 20 1.6209 - 1.5935 1.00 2548 134 0.2004 0.2602
REMARK 3 21 1.5935 - 1.5678 1.00 2609 146 0.1845 0.2466
REMARK 3 22 1.5678 - 1.5436 1.00 2552 138 0.1919 0.2631
REMARK 3 23 1.5436 - 1.5209 1.00 2599 133 0.1943 0.2538
REMARK 3 24 1.5209 - 1.4995 0.94 2383 133 0.1988 0.2387
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.750
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 : 0.006 3479
REMARK 3 ANGLE : 1.124 4749
REMARK 3 CHIRALITY : 0.071 547
REMARK 3 PLANARITY : 0.005 587
REMARK 3 DIHEDRAL : 17.711 1334
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 4RD1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000087193.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979180
REMARK 200 MONOCHROMATOR : CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65993
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 46.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.420
REMARK 200 R MERGE (I) : 0.13600
REMARK 200 R SYM (I) : 0.13600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 7.15
REMARK 200 R MERGE FOR SHELL (I) : 0.53300
REMARK 200 R SYM FOR SHELL (I) : 0.53300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.250
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: PHENIX 1.8.4_1496
REMARK 200 STARTING MODEL: 4RCZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 70% MPD, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277K
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 23.16000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.30000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.30500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.30000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.16000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.30500
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: MONOMERIC
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 MET A 1
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 250 0.45 81.07
REMARK 500 LYS A 354 -3.05 81.36
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 504 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 19 OD1
REMARK 620 2 GLY A 44 O 161.9
REMARK 620 3 HOH A 648 O 81.1 83.6
REMARK 620 4 HOH A 699 O 93.8 77.4 93.5
REMARK 620 5 HOH A 887 O 84.3 106.2 93.2 172.7
REMARK 620 6 HOH A 888 O 88.4 106.5 169.5 86.2 86.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 23 OG1
REMARK 620 2 THR A 46 OG1 88.5
REMARK 620 3 GTP A 501 O2G 171.9 97.0
REMARK 620 4 GTP A 501 O2B 88.2 172.9 87.0
REMARK 620 5 GDP A 502 O3B 95.2 172.8 80.0 7.0
REMARK 620 6 PO4 A 505 O3 178.0 91.5 6.8 92.0 85.0
REMARK 620 7 HOH A 606 O 89.2 91.6 84.6 94.6 94.6 88.8
REMARK 620 8 HOH A 611 O 88.6 86.8 97.7 86.9 87.1 93.4 177.3
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 GTP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 508
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4RCY RELATED DB: PDB
REMARK 900 RELATED ID: 4RCZ RELATED DB: PDB
REMARK 900 RELATED ID: 4RD0 RELATED DB: PDB
REMARK 900 RELATED ID: 4RD2 RELATED DB: PDB
REMARK 900 RELATED ID: 4RD3 RELATED DB: PDB
REMARK 900 RELATED ID: 4RD4 RELATED DB: PDB
REMARK 900 RELATED ID: 4RD6 RELATED DB: PDB
DBREF 4RD1 A 1 415 UNP Q980A5 IF2G_SULSO 1 415
SEQADV 4RD1 ALA A 97 UNP Q980A5 HIS 97 ENGINEERED MUTATION
SEQRES 1 A 415 MET ALA TRP PRO LYS VAL GLN PRO GLU VAL ASN ILE GLY
SEQRES 2 A 415 VAL VAL GLY HIS VAL ASP HIS GLY LYS THR THR LEU VAL
SEQRES 3 A 415 GLN ALA ILE THR GLY ILE TRP THR SER LYS HIS SER GLU
SEQRES 4 A 415 GLU LEU LYS ARG GLY MET THR ILE LYS LEU GLY TYR ALA
SEQRES 5 A 415 GLU THR ASN ILE GLY VAL CYS GLU SER CYS LYS LYS PRO
SEQRES 6 A 415 GLU ALA TYR VAL THR GLU PRO SER CYS LYS SER CYS GLY
SEQRES 7 A 415 SER ASP ASP GLU PRO LYS PHE LEU ARG ARG ILE SER PHE
SEQRES 8 A 415 ILE ASP ALA PRO GLY ALA GLU VAL LEU MET ALA THR MET
SEQRES 9 A 415 LEU SER GLY ALA ALA LEU MET ASP GLY ALA ILE LEU VAL
SEQRES 10 A 415 VAL ALA ALA ASN GLU PRO PHE PRO GLN PRO GLN THR ARG
SEQRES 11 A 415 GLU HIS PHE VAL ALA LEU GLY ILE ILE GLY VAL LYS ASN
SEQRES 12 A 415 LEU ILE ILE VAL GLN ASN LYS VAL ASP VAL VAL SER LYS
SEQRES 13 A 415 GLU GLU ALA LEU SER GLN TYR ARG GLN ILE LYS GLN PHE
SEQRES 14 A 415 THR LYS GLY THR TRP ALA GLU ASN VAL PRO ILE ILE PRO
SEQRES 15 A 415 VAL SER ALA LEU HIS LYS ILE ASN ILE ASP SER LEU ILE
SEQRES 16 A 415 GLU GLY ILE GLU GLU TYR ILE LYS THR PRO TYR ARG ASP
SEQRES 17 A 415 LEU SER GLN LYS PRO VAL MET LEU VAL ILE ARG SER PHE
SEQRES 18 A 415 ASP VAL ASN LYS PRO GLY THR GLN PHE ASN GLU LEU LYS
SEQRES 19 A 415 GLY GLY VAL ILE GLY GLY SER ILE ILE GLN GLY LEU PHE
SEQRES 20 A 415 LYS VAL ASP GLN GLU ILE LYS VAL LEU PRO GLY LEU ARG
SEQRES 21 A 415 VAL GLU LYS GLN GLY LYS VAL SER TYR GLU PRO ILE PHE
SEQRES 22 A 415 THR LYS ILE SER SER ILE ARG PHE GLY ASP GLU GLU PHE
SEQRES 23 A 415 LYS GLU ALA LYS PRO GLY GLY LEU VAL ALA ILE GLY THR
SEQRES 24 A 415 TYR LEU ASP PRO SER LEU THR LYS ALA ASP ASN LEU LEU
SEQRES 25 A 415 GLY SER ILE ILE THR LEU ALA ASP ALA GLU VAL PRO VAL
SEQRES 26 A 415 LEU TRP ASN ILE ARG ILE LYS TYR ASN LEU LEU GLU ARG
SEQRES 27 A 415 VAL VAL GLY ALA LYS GLU MET LEU LYS VAL ASP PRO ILE
SEQRES 28 A 415 ARG ALA LYS GLU THR LEU MET LEU SER VAL GLY SER SER
SEQRES 29 A 415 THR THR LEU GLY ILE VAL THR SER VAL LYS LYS ASP GLU
SEQRES 30 A 415 ILE GLU VAL GLU LEU ARG ARG PRO VAL ALA VAL TRP SER
SEQRES 31 A 415 ASN ASN ILE ARG THR VAL ILE SER ARG GLN ILE ALA GLY
SEQRES 32 A 415 ARG TRP ARG MET ILE GLY TRP GLY LEU VAL GLU ILE
HET GTP A 501 32
HET GDP A 502 28
HET MG A 503 1
HET MG A 504 1
HET PO4 A 505 5
HET GDP A 506 28
HET MPD A 507 8
HET MPD A 508 8
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM PO4 PHOSPHATE ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 2 GTP C10 H16 N5 O14 P3
FORMUL 3 GDP 2(C10 H15 N5 O11 P2)
FORMUL 4 MG 2(MG 2+)
FORMUL 6 PO4 O4 P 3-
FORMUL 8 MPD 2(C6 H14 O2)
FORMUL 10 HOH *317(H2 O)
HELIX 1 1 GLY A 21 GLY A 31 1 11
HELIX 2 2 HIS A 37 GLY A 44 1 8
HELIX 3 3 CYS A 74 GLY A 78 5 5
HELIX 4 4 ALA A 97 VAL A 99 5 3
HELIX 5 5 LEU A 100 ALA A 109 1 10
HELIX 6 6 GLN A 126 GLY A 140 1 15
HELIX 7 7 LYS A 150 VAL A 154 5 5
HELIX 8 8 SER A 155 LYS A 171 1 17
HELIX 9 9 ASN A 190 ILE A 202 1 13
HELIX 10 10 GLN A 229 LEU A 233 5 5
HELIX 11 11 THR A 306 ASN A 310 5 5
SHEET 1 A 7 TYR A 68 VAL A 69 0
SHEET 2 A 7 GLY A 50 VAL A 58 -1 N GLY A 57 O VAL A 69
SHEET 3 A 7 LYS A 84 ASP A 93 -1 O ILE A 89 N THR A 54
SHEET 4 A 7 ASN A 11 VAL A 15 1 N ILE A 12 O SER A 90
SHEET 5 A 7 GLY A 113 ALA A 119 1 O GLY A 113 N GLY A 13
SHEET 6 A 7 LEU A 144 ASN A 149 1 O VAL A 147 N VAL A 118
SHEET 7 A 7 ILE A 180 PRO A 182 1 O ILE A 181 N ILE A 146
SHEET 1 B 8 LYS A 266 LYS A 275 0
SHEET 2 B 8 GLU A 252 LYS A 263 -1 N VAL A 261 O SER A 268
SHEET 3 B 8 ILE A 315 LEU A 318 -1 O ILE A 315 N LEU A 256
SHEET 4 B 8 VAL A 214 PHE A 221 -1 N MET A 215 O ILE A 316
SHEET 5 B 8 VAL A 237 GLN A 244 -1 O SER A 241 N LEU A 216
SHEET 6 B 8 VAL A 295 GLY A 298 -1 O ILE A 297 N ILE A 238
SHEET 7 B 8 SER A 278 PHE A 281 -1 N ARG A 280 O ALA A 296
SHEET 8 B 8 GLU A 284 PHE A 286 -1 O PHE A 286 N ILE A 279
SHEET 1 C 2 PHE A 247 LYS A 248 0
SHEET 2 C 2 GLU A 288 ALA A 289 -1 O ALA A 289 N PHE A 247
SHEET 1 D 7 VAL A 325 LEU A 335 0
SHEET 2 D 7 GLU A 377 ALA A 387 -1 O LEU A 382 N TRP A 327
SHEET 3 D 7 SER A 364 VAL A 373 -1 N ILE A 369 O GLU A 381
SHEET 4 D 7 THR A 356 VAL A 361 -1 N LEU A 359 O THR A 366
SHEET 5 D 7 ILE A 393 ILE A 401 -1 O SER A 398 N MET A 358
SHEET 6 D 7 ARG A 404 GLU A 414 -1 O ILE A 408 N ILE A 397
SHEET 7 D 7 VAL A 325 LEU A 335 -1 N ARG A 330 O GLU A 414
SSBOND 1 CYS A 59 CYS A 74 1555 1555 2.04
SSBOND 2 CYS A 62 CYS A 77 1555 1555 2.04
LINK OD1 ASP A 19 MG MG A 504 1555 1555 2.12
LINK OG1 THR A 23 MG MG A 503 1555 1555 2.10
LINK O GLY A 44 MG MG A 504 1555 1555 2.09
LINK OG1 THR A 46 MG MG A 503 1555 1555 2.08
LINK O2GAGTP A 501 MG MG A 503 1555 1555 1.86
LINK O2BAGTP A 501 MG MG A 503 1555 1555 2.20
LINK O3BBGDP A 502 MG MG A 503 1555 1555 2.09
LINK MG MG A 503 O3 BPO4 A 505 1555 1555 2.33
LINK MG MG A 503 O HOH A 606 1555 1555 2.03
LINK MG MG A 503 O HOH A 611 1555 1555 2.11
LINK MG MG A 504 O HOH A 648 1555 1555 1.98
LINK MG MG A 504 O HOH A 699 1555 1555 2.37
LINK MG MG A 504 O HOH A 887 1555 1555 2.26
LINK MG MG A 504 O HOH A 888 1555 1555 2.09
CISPEP 1 LYS A 64 PRO A 65 0 6.64
CISPEP 2 PHE A 124 PRO A 125 0 -4.30
CISPEP 3 LEU A 256 PRO A 257 0 0.56
SITE 1 AC1 29 VAL A 18 ASP A 19 HIS A 20 GLY A 21
SITE 2 AC1 29 LYS A 22 THR A 23 THR A 24 MET A 45
SITE 3 AC1 29 THR A 46 GLY A 96 ASN A 149 LYS A 150
SITE 4 AC1 29 ASP A 152 VAL A 153 SER A 184 ALA A 185
SITE 5 AC1 29 LEU A 186 MG A 503 HOH A 601 HOH A 606
SITE 6 AC1 29 HOH A 611 HOH A 648 HOH A 649 HOH A 655
SITE 7 AC1 29 HOH A 679 HOH A 798 HOH A 816 HOH A 874
SITE 8 AC1 29 HOH A 887
SITE 1 AC2 22 ASP A 19 HIS A 20 GLY A 21 LYS A 22
SITE 2 AC2 22 THR A 23 THR A 24 ASN A 149 LYS A 150
SITE 3 AC2 22 ASP A 152 VAL A 153 SER A 184 ALA A 185
SITE 4 AC2 22 LEU A 186 MG A 503 HOH A 606 HOH A 611
SITE 5 AC2 22 HOH A 648 HOH A 649 HOH A 679 HOH A 798
SITE 6 AC2 22 HOH A 816 HOH A 874
SITE 1 AC3 7 THR A 23 THR A 46 GTP A 501 GDP A 502
SITE 2 AC3 7 PO4 A 505 HOH A 606 HOH A 611
SITE 1 AC4 6 ASP A 19 GLY A 44 HOH A 648 HOH A 699
SITE 2 AC4 6 HOH A 887 HOH A 888
SITE 1 AC5 12 VAL A 18 LYS A 22 MET A 45 THR A 46
SITE 2 AC5 12 PRO A 95 GLY A 96 GDP A 502 MG A 503
SITE 3 AC5 12 HOH A 601 HOH A 606 HOH A 648 HOH A 887
SITE 1 AC6 12 VAL A 223 LYS A 225 LYS A 234 SER A 278
SITE 2 AC6 12 ARG A 280 GLY A 282 ALA A 296 GLY A 298
SITE 3 AC6 12 HOH A 702 HOH A 757 HOH A 869 HOH A 915
SITE 1 AC7 5 GLU A 39 LYS A 42 ARG A 43 LYS A 287
SITE 2 AC7 5 HOH A 631
SITE 1 AC8 2 ALA A 2 TYR A 300
CRYST1 46.320 60.610 144.600 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 0.021589 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016499 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006916 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
