HEADER NUCLEOTIDE BINDING PROTEIN 02-AUG-07 2QTH
TITLE CRYSTAL STRUCTURE OF A GTP-BINDING PROTEIN FROM THE HYPERTHERMOPHILIC
TITLE 2 ARCHAEON SULFOLOBUS SOLFATARICUS IN COMPLEX WITH GDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTP-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROTEIN HFLX;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS P2;
SOURCE 3 ORGANISM_COMMON: ARCHAEA;
SOURCE 4 STRAIN: P2, DSM 1617, JCM 11322;
SOURCE 5 ATCC: 35092;
SOURCE 6 GENE: HFLX, SSO0269;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HB101;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24D
KEYWDS BETA-ALPHA-BARRELS, GTP-BINDING, NUCLEOTIDE-BINDING, NUCLEOTIDE
KEYWDS 2 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.WU,L.SUN,S.J.BROUNS,S.FU,Z.RAO,J.VAN DER OOST
REVDAT 4 21-FEB-24 2QTH 1 REMARK SEQADV LINK
REVDAT 3 25-OCT-17 2QTH 1 REMARK
REVDAT 2 24-FEB-09 2QTH 1 VERSN
REVDAT 1 19-AUG-08 2QTH 0
JRNL AUTH H.WU,L.SUN,S.J.BROUNS,S.FU,J.AKERBOOM,X.LI,C.ZHANG,Z.RAO,
JRNL AUTH 2 J.VAN DER OOST
JRNL TITL CRYSTAL STRUCTURE OF A GTP-BINDING PROTEIN FROM THE
JRNL TITL 2 HYPERTHERMOPHILIC ARCHAEON SULFOLOBUS SOLFATARICUS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0022
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 30737
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) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1548
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1868
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.99
REMARK 3 BIN R VALUE (WORKING SET) : 0.2760
REMARK 3 BIN FREE R VALUE SET COUNT : 96
REMARK 3 BIN FREE R VALUE : 0.3880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2504
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 137
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.44
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): 0.175
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.164
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.111
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.807
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2592 ; 0.029 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3479 ; 2.127 ; 2.024
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 308 ; 6.504 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 99 ;34.618 ;24.747
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 523 ;16.729 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;11.868 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 415 ; 0.152 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1806 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1266 ; 0.247 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1795 ; 0.321 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 171 ; 0.193 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.113 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 40 ; 0.333 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.156 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 2 ; 0.345 ; 0.200
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): 1664 ; 1.652 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2542 ; 2.385 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1119 ; 3.742 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 937 ; 5.381 ; 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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2QTH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000044034.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : 100
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30737
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.38800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP, DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M CADMIUM SULFATE, 0.1M HEPES,
REMARK 280 0.8M SODIUM ACETATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 290K
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 32.49550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.00800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.20150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.00800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.49550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.20150
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 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 TYR A 123
REMARK 465 THR A 124
REMARK 465 LYS A 125
REMARK 465 SER A 126
REMARK 465 LYS A 127
REMARK 465 ILE A 128
REMARK 465 GLY A 129
REMARK 465 GLU A 130
REMARK 465 GLN A 131
REMARK 465 GLN A 132
REMARK 465 GLY A 133
REMARK 465 PRO A 134
REMARK 465 LEU A 135
REMARK 465 GLY A 136
REMARK 465 ALA A 137
REMARK 465 GLY A 138
REMARK 465 THR A 139
REMARK 465 TYR A 140
REMARK 465 GLY A 141
REMARK 465 VAL A 142
REMARK 465 GLU A 143
REMARK 465 PHE A 166
REMARK 465 LYS A 167
REMARK 465 GLU A 168
REMARK 465 LYS A 169
REMARK 465 SER A 170
REMARK 465 ILE A 171
REMARK 465 GLU A 172
REMARK 465 SER A 173
REMARK 465 ASN A 174
REMARK 465 LYS A 175
REMARK 465 ARG A 176
REMARK 465 ASN A 177
REMARK 465 ASN A 178
REMARK 465 THR A 203
REMARK 465 GLN A 204
REMARK 465 LYS A 205
REMARK 465 VAL A 206
REMARK 465 ASP A 207
REMARK 465 THR A 208
REMARK 465 LYS A 209
REMARK 465 LEU A 210
REMARK 465 PHE A 211
REMARK 465 THR A 212
REMARK 465 THR A 213
REMARK 465 LEU A 357
REMARK 465 GLU A 358
REMARK 465 HIS A 359
REMARK 465 HIS A 360
REMARK 465 HIS A 361
REMARK 465 HIS A 362
REMARK 465 HIS A 363
REMARK 465 HIS A 364
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 356 O
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 OE2 GLU A 276 C ACT A 503 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 77 C LEU A 78 N -0.222
REMARK 500 GLU A 283 C ILE A 284 N -0.169
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 TYR A 42 -67.00 65.20
REMARK 500 ASN A 224 -126.05 55.84
REMARK 500 SER A 270 155.94 -46.77
REMARK 500 ASN A 306 77.58 38.07
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 CD A 401 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 92 OE1
REMARK 620 2 GLU A 92 OE2 57.6
REMARK 620 3 HOH A 528 O 74.2 127.5
REMARK 620 4 HOH A 624 O 88.0 82.9 75.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 402 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 97 NE2
REMARK 620 2 ASP A 232 OD2 104.0
REMARK 620 3 HOH A 505 O 83.8 127.9
REMARK 620 4 HOH A 543 O 84.2 152.3 78.9
REMARK 620 5 HOH A 560 O 170.9 84.5 88.3 89.7
REMARK 620 6 HOH A 584 O 95.3 84.5 147.0 68.3 88.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 193 OG1
REMARK 620 2 GDP A 500 O3B 84.6
REMARK 620 3 HOH A 608 O 155.4 101.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 403 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 283 OE1
REMARK 620 2 GLU A 283 OE2 54.8
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 CD A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QTF RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT GDP
DBREF 2QTH A 1 356 UNP Q980M3 Q980M3_SULSO 1 356
SEQADV 2QTH LEU A 357 UNP Q980M3 INSERTION
SEQADV 2QTH GLU A 358 UNP Q980M3 INSERTION
SEQADV 2QTH HIS A 359 UNP Q980M3 INSERTION
SEQADV 2QTH HIS A 360 UNP Q980M3 INSERTION
SEQADV 2QTH HIS A 361 UNP Q980M3 INSERTION
SEQADV 2QTH HIS A 362 UNP Q980M3 INSERTION
SEQADV 2QTH HIS A 363 UNP Q980M3 INSERTION
SEQADV 2QTH HIS A 364 UNP Q980M3 INSERTION
SEQRES 1 A 364 MET LYS THR ALA ALA LEU PHE VAL SER LYS GLU PHE GLU
SEQRES 2 A 364 GLU GLU ALA ILE ALA LEU VAL GLU GLY ALA ASN TYR LYS
SEQRES 3 A 364 VAL THR SER ILE TYR LYS LEU PRO LYS SER PRO ASN VAL
SEQRES 4 A 364 LYS PHE TYR ILE GLN TYR ASP LYS LEU GLN GLN ILE LYS
SEQRES 5 A 364 ASN ASP GLU GLU ILE SER THR LEU ILE ILE PHE GLU GLN
SEQRES 6 A 364 LEU LYS PRO ARG HIS PHE ILE ASN ILE ARG ARG GLU LEU
SEQRES 7 A 364 LYS GLY LYS GLU VAL LEU ASP LYS ILE LEU LEU LEU LEU
SEQRES 8 A 364 GLU ILE PHE ALA LEU HIS ALA GLY SER LYS GLU ALA LYS
SEQRES 9 A 364 MET GLN ILE GLU LEU ALA ARG LEU LYS TYR GLU LEU PRO
SEQRES 10 A 364 ILE ILE LYS GLU THR TYR THR LYS SER LYS ILE GLY GLU
SEQRES 11 A 364 GLN GLN GLY PRO LEU GLY ALA GLY THR TYR GLY VAL GLU
SEQRES 12 A 364 SER THR ILE LYS PHE TYR LYS ARG ARG ILE ASN LYS LEU
SEQRES 13 A 364 MET LYS GLU LEU GLU SER ILE LYS ILE PHE LYS GLU LYS
SEQRES 14 A 364 SER ILE GLU SER ASN LYS ARG ASN ASN ILE PRO SER ILE
SEQRES 15 A 364 GLY ILE VAL GLY TYR THR ASN SER GLY LYS THR SER LEU
SEQRES 16 A 364 PHE ASN SER LEU THR GLY LEU THR GLN LYS VAL ASP THR
SEQRES 17 A 364 LYS LEU PHE THR THR MET SER PRO LYS ARG TYR ALA ILE
SEQRES 18 A 364 PRO ILE ASN ASN ARG LYS ILE MET LEU VAL ASP THR VAL
SEQRES 19 A 364 GLY PHE ILE ARG GLY ILE PRO PRO GLN ILE VAL ASP ALA
SEQRES 20 A 364 PHE PHE VAL THR LEU SER GLU ALA LYS TYR SER ASP ALA
SEQRES 21 A 364 LEU ILE LEU VAL ILE ASP SER THR PHE SER GLU ASN LEU
SEQRES 22 A 364 LEU ILE GLU THR LEU GLN SER SER PHE GLU ILE LEU ARG
SEQRES 23 A 364 GLU ILE GLY VAL SER GLY LYS PRO ILE LEU VAL THR LEU
SEQRES 24 A 364 ASN LYS ILE ASP LYS ILE ASN GLY ASP LEU TYR LYS LYS
SEQRES 25 A 364 LEU ASP LEU VAL GLU LYS LEU SER LYS GLU LEU TYR SER
SEQRES 26 A 364 PRO ILE PHE ASP VAL ILE PRO ILE SER ALA LEU LYS ARG
SEQRES 27 A 364 THR ASN LEU GLU LEU LEU ARG ASP LYS ILE TYR GLN LEU
SEQRES 28 A 364 ALA THR GLN LEU SER LEU GLU HIS HIS HIS HIS HIS HIS
HET CD A 401 1
HET CD A 402 1
HET CD A 403 1
HET CD A 404 1
HET MG A 501 1
HET ACT A 502 4
HET GDP A 500 28
HET ACT A 503 4
HET ACT A 504 4
HETNAM CD CADMIUM ION
HETNAM MG MAGNESIUM ION
HETNAM ACT ACETATE ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 2 CD 4(CD 2+)
FORMUL 6 MG MG 2+
FORMUL 7 ACT 3(C2 H3 O2 1-)
FORMUL 8 GDP C10 H15 N5 O11 P2
FORMUL 11 HOH *137(H2 O)
HELIX 1 1 PHE A 12 ALA A 23 1 12
HELIX 2 2 GLN A 44 ASN A 53 1 10
HELIX 3 3 LYS A 67 GLU A 77 1 11
HELIX 4 4 ASP A 85 ALA A 98 1 14
HELIX 5 5 SER A 100 THR A 122 1 23
HELIX 6 6 SER A 144 ILE A 165 1 22
HELIX 7 7 GLY A 191 GLY A 201 1 11
HELIX 8 8 PRO A 241 GLN A 243 5 3
HELIX 9 9 ILE A 244 GLU A 254 1 11
HELIX 10 10 ALA A 255 SER A 258 5 4
HELIX 11 11 SER A 270 GLU A 283 1 14
HELIX 12 12 ILE A 284 GLY A 289 1 6
HELIX 13 13 LYS A 301 ILE A 305 5 5
HELIX 14 14 ASP A 308 TYR A 324 1 17
HELIX 15 15 ASN A 340 SER A 356 1 17
SHEET 1 A 4 LYS A 26 TYR A 31 0
SHEET 2 A 4 THR A 3 PHE A 7 1 N LEU A 6 O SER A 29
SHEET 3 A 4 THR A 59 ILE A 62 1 O ILE A 61 N ALA A 5
SHEET 4 A 4 GLU A 82 LEU A 84 1 O GLU A 82 N LEU A 60
SHEET 1 B 6 ARG A 218 ILE A 223 0
SHEET 2 B 6 ARG A 226 ASP A 232 -1 O ILE A 228 N ILE A 221
SHEET 3 B 6 SER A 181 GLY A 186 1 N ILE A 182 O MET A 229
SHEET 4 B 6 ALA A 260 ASP A 266 1 O ILE A 262 N GLY A 183
SHEET 5 B 6 ILE A 295 ASN A 300 1 O ASN A 300 N ILE A 265
SHEET 6 B 6 ILE A 327 PRO A 332 1 O ILE A 331 N LEU A 299
LINK OE1 GLU A 92 CD CD A 401 1555 1555 2.36
LINK OE2 GLU A 92 CD CD A 401 1555 1555 2.19
LINK NE2 HIS A 97 CD CD A 402 1555 1555 2.25
LINK OE1 GLU A 108 CD CD A 404 1555 1555 2.33
LINK OG1 THR A 193 MG MG A 501 1555 1555 2.12
LINK OD2 ASP A 232 CD CD A 402 1555 1555 2.21
LINK OE1 GLU A 283 CD CD A 403 1555 1555 2.51
LINK OE2 GLU A 283 CD CD A 403 1555 1555 2.24
LINK CD CD A 401 O HOH A 528 1555 1555 2.40
LINK CD CD A 401 O HOH A 624 1555 1555 2.58
LINK CD CD A 402 O HOH A 505 1555 1555 2.54
LINK CD CD A 402 O HOH A 543 1555 1555 2.47
LINK CD CD A 402 O HOH A 560 1555 1555 2.25
LINK CD CD A 402 O HOH A 584 1555 1555 2.41
LINK O3B GDP A 500 MG MG A 501 1555 1555 2.34
LINK MG MG A 501 O HOH A 608 1555 1555 2.23
CISPEP 1 SER A 215 PRO A 216 0 -6.73
CISPEP 2 SER A 325 PRO A 326 0 0.62
SITE 1 AC1 5 GLU A 92 GLU A 342 ASP A 346 HOH A 528
SITE 2 AC1 5 HOH A 624
SITE 1 AC2 6 HIS A 97 ASP A 232 HOH A 505 HOH A 543
SITE 2 AC2 6 HOH A 560 HOH A 584
SITE 1 AC3 3 GLU A 77 GLU A 283 HOH A 595
SITE 1 AC4 3 GLU A 108 PRO A 222 HOH A 527
SITE 1 AC5 2 THR A 193 HOH A 608
SITE 1 AC6 3 LYS A 79 GLU A 276 HOH A 540
SITE 1 AC7 1 ASP A 329
SITE 1 AC8 15 TYR A 187 ASN A 189 SER A 190 GLY A 191
SITE 2 AC8 15 LYS A 192 THR A 193 SER A 194 ASN A 300
SITE 3 AC8 15 LYS A 301 ASP A 303 LYS A 304 SER A 334
SITE 4 AC8 15 ALA A 335 LEU A 336 HOH A 608
CRYST1 64.991 72.403 96.016 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 0.015387 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013812 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010415 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
