HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 22-FEB-11 3QTB
TITLE STRUCTURE OF THE UNIVERSAL STRESS PROTEIN FROM ARCHAEOGLOBUS FULGIDUS
TITLE 2 IN COMPLEX WITH DAMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 3 ORGANISM_TAXID: 2234;
SOURCE 4 GENE: AF_0826;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIPL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P15TV LIC
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS, MCSG, A/B CLASS, RFM LIKE, PUTATIVE UNIVERSAL STRESS
KEYWDS 3 PROTEIN, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.TKACZUK,I.A.SHUMILIN,M.CHRUSZCZ,M.CYMBOROWSKI,X.XU,R.DI LEO,
AUTHOR 2 A.SAVCHENKO,A.JOACHIMIAK,W.MINOR,MIDWEST CENTER FOR STRUCTURAL
AUTHOR 3 GENOMICS (MCSG)
REVDAT 7 06-DEC-23 3QTB 1 REMARK
REVDAT 6 13-SEP-23 3QTB 1 REMARK
REVDAT 5 13-APR-22 3QTB 1 AUTHOR JRNL REMARK SEQADV
REVDAT 5 2 1 LINK
REVDAT 4 08-NOV-17 3QTB 1 REMARK
REVDAT 3 26-JUN-13 3QTB 1 JRNL
REVDAT 2 17-APR-13 3QTB 1 JRNL VERSN
REVDAT 1 30-MAR-11 3QTB 0
JRNL AUTH K.L.TKACZUK,I.A.SHUMILIN,M.CHRUSZCZ,E.EVDOKIMOVA,
JRNL AUTH 2 A.SAVCHENKO,W.MINOR
JRNL TITL STRUCTURAL AND FUNCTIONAL INSIGHT INTO THE UNIVERSAL STRESS
JRNL TITL 2 PROTEIN FAMILY.
JRNL REF EVOL APPL V. 6 434 2013
JRNL REFN ESSN 1752-4571
JRNL PMID 23745136
JRNL DOI 10.1111/EVA.12057
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0070
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 14059
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 738
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1027
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.45
REMARK 3 BIN R VALUE (WORKING SET) : 0.1960
REMARK 3 BIN FREE R VALUE SET COUNT : 54
REMARK 3 BIN FREE R VALUE : 0.2180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1970
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 50
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.10000
REMARK 3 B22 (A**2) : 0.63000
REMARK 3 B33 (A**2) : -1.75000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.35000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.254
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.195
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.153
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.228
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2031 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1394 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2750 ; 1.425 ; 2.003
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3402 ; 0.840 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 255 ; 5.673 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 81 ;34.469 ;23.333
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 355 ;15.158 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;15.662 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 323 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2228 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 388 ; 0.001 ; 0.020
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 104
REMARK 3 RESIDUE RANGE : B 1 B 102
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7546 29.7929 -13.3028
REMARK 3 T TENSOR
REMARK 3 T11: 0.0740 T22: 0.0374
REMARK 3 T33: 0.0524 T12: 0.0267
REMARK 3 T13: -0.0219 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 2.8696 L22: 1.2427
REMARK 3 L33: 1.3092 L12: 0.7256
REMARK 3 L13: -0.8763 L23: -0.3633
REMARK 3 S TENSOR
REMARK 3 S11: -0.0394 S12: -0.0858 S13: -0.0144
REMARK 3 S21: 0.0149 S22: 0.0671 S23: 0.0196
REMARK 3 S31: -0.0344 S32: 0.1352 S33: -0.0276
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 103 B 116
REMARK 3 ORIGIN FOR THE GROUP (A): 29.2668 23.4723 -29.6174
REMARK 3 T TENSOR
REMARK 3 T11: 0.0766 T22: 0.1751
REMARK 3 T33: 0.1278 T12: 0.0188
REMARK 3 T13: -0.0007 T23: -0.0343
REMARK 3 L TENSOR
REMARK 3 L11: 6.8741 L22: 10.1758
REMARK 3 L33: 13.7842 L12: -6.5710
REMARK 3 L13: -1.8980 L23: 6.4603
REMARK 3 S TENSOR
REMARK 3 S11: 0.3150 S12: 0.4575 S13: -0.0253
REMARK 3 S21: -0.3762 S22: -0.1049 S23: -0.2151
REMARK 3 S31: -0.0372 S32: 0.1960 S33: -0.2102
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 116 A 134
REMARK 3 RESIDUE RANGE : B 117 B 134
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1643 23.0176 -15.2641
REMARK 3 T TENSOR
REMARK 3 T11: 0.1685 T22: 0.1739
REMARK 3 T33: 0.1960 T12: 0.0141
REMARK 3 T13: -0.0310 T23: -0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 3.2047 L22: 1.7717
REMARK 3 L33: 1.0569 L12: 0.9418
REMARK 3 L13: -1.6701 L23: -0.1296
REMARK 3 S TENSOR
REMARK 3 S11: -0.0900 S12: -0.1662 S13: -0.2530
REMARK 3 S21: 0.0793 S22: 0.0851 S23: -0.0850
REMARK 3 S31: 0.1208 S32: 0.1892 S33: 0.0048
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: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3QTB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000064076.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-AUG-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9786
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14965
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.5000
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) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.40500
REMARK 200 R SYM FOR SHELL (I) : 0.40500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: HKL-3000, MOLREP
REMARK 200 STARTING MODEL: 3DLO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.1M BIS-TRIS
REMARK 280 PH 5.5, 25%W/V POLYETHYLENE GLYCOL, 3350, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
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 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 54.80350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.32750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 54.80350
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 21.32750
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 153 LIES ON A SPECIAL POSITION.
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 MSE A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 ARG A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY A 0
REMARK 465 LYS A 106
REMARK 465 ARG A 107
REMARK 465 SER A 108
REMARK 465 PRO A 109
REMARK 465 THR A 110
REMARK 465 GLY A 111
REMARK 465 LYS A 112
REMARK 465 LEU A 113
REMARK 465 ILE A 114
REMARK 465 MSE B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 ARG B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 GLY B 0
REMARK 465 MSE B 1
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 MSE A 1 CG SE CE
REMARK 470 LYS A 12 CG CD CE NZ
REMARK 470 LYS A 48 CG CD CE NZ
REMARK 470 ARG A 105 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 46 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 82 CG CD CE NZ
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D5M A 135
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 135
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 136
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 137
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DLO RELATED DB: PDB
REMARK 900 RELATED ID: APC7551 RELATED DB: TARGETDB
DBREF 3QTB A 1 134 UNP O29432 O29432_ARCFU 1 134
DBREF 3QTB B 1 134 UNP O29432 O29432_ARCFU 1 134
SEQADV 3QTB MSE A -20 UNP O29432 EXPRESSION TAG
SEQADV 3QTB GLY A -19 UNP O29432 EXPRESSION TAG
SEQADV 3QTB SER A -18 UNP O29432 EXPRESSION TAG
SEQADV 3QTB SER A -17 UNP O29432 EXPRESSION TAG
SEQADV 3QTB HIS A -16 UNP O29432 EXPRESSION TAG
SEQADV 3QTB HIS A -15 UNP O29432 EXPRESSION TAG
SEQADV 3QTB HIS A -14 UNP O29432 EXPRESSION TAG
SEQADV 3QTB HIS A -13 UNP O29432 EXPRESSION TAG
SEQADV 3QTB HIS A -12 UNP O29432 EXPRESSION TAG
SEQADV 3QTB HIS A -11 UNP O29432 EXPRESSION TAG
SEQADV 3QTB SER A -10 UNP O29432 EXPRESSION TAG
SEQADV 3QTB SER A -9 UNP O29432 EXPRESSION TAG
SEQADV 3QTB GLY A -8 UNP O29432 EXPRESSION TAG
SEQADV 3QTB ARG A -7 UNP O29432 EXPRESSION TAG
SEQADV 3QTB GLU A -6 UNP O29432 EXPRESSION TAG
SEQADV 3QTB ASN A -5 UNP O29432 EXPRESSION TAG
SEQADV 3QTB LEU A -4 UNP O29432 EXPRESSION TAG
SEQADV 3QTB TYR A -3 UNP O29432 EXPRESSION TAG
SEQADV 3QTB PHE A -2 UNP O29432 EXPRESSION TAG
SEQADV 3QTB GLN A -1 UNP O29432 EXPRESSION TAG
SEQADV 3QTB GLY A 0 UNP O29432 EXPRESSION TAG
SEQADV 3QTB MSE B -20 UNP O29432 EXPRESSION TAG
SEQADV 3QTB GLY B -19 UNP O29432 EXPRESSION TAG
SEQADV 3QTB SER B -18 UNP O29432 EXPRESSION TAG
SEQADV 3QTB SER B -17 UNP O29432 EXPRESSION TAG
SEQADV 3QTB HIS B -16 UNP O29432 EXPRESSION TAG
SEQADV 3QTB HIS B -15 UNP O29432 EXPRESSION TAG
SEQADV 3QTB HIS B -14 UNP O29432 EXPRESSION TAG
SEQADV 3QTB HIS B -13 UNP O29432 EXPRESSION TAG
SEQADV 3QTB HIS B -12 UNP O29432 EXPRESSION TAG
SEQADV 3QTB HIS B -11 UNP O29432 EXPRESSION TAG
SEQADV 3QTB SER B -10 UNP O29432 EXPRESSION TAG
SEQADV 3QTB SER B -9 UNP O29432 EXPRESSION TAG
SEQADV 3QTB GLY B -8 UNP O29432 EXPRESSION TAG
SEQADV 3QTB ARG B -7 UNP O29432 EXPRESSION TAG
SEQADV 3QTB GLU B -6 UNP O29432 EXPRESSION TAG
SEQADV 3QTB ASN B -5 UNP O29432 EXPRESSION TAG
SEQADV 3QTB LEU B -4 UNP O29432 EXPRESSION TAG
SEQADV 3QTB TYR B -3 UNP O29432 EXPRESSION TAG
SEQADV 3QTB PHE B -2 UNP O29432 EXPRESSION TAG
SEQADV 3QTB GLN B -1 UNP O29432 EXPRESSION TAG
SEQADV 3QTB GLY B 0 UNP O29432 EXPRESSION TAG
SEQRES 1 A 155 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 155 ARG GLU ASN LEU TYR PHE GLN GLY MSE ILE TYR MSE PRO
SEQRES 3 A 155 ILE VAL VAL ALA VAL ASP LYS LYS SER ASP ARG ALA GLU
SEQRES 4 A 155 ARG VAL LEU ARG PHE ALA ALA GLU GLU ALA ARG LEU ARG
SEQRES 5 A 155 GLY VAL PRO VAL TYR VAL VAL HIS SER LEU PRO GLY GLY
SEQRES 6 A 155 GLY ARG THR LYS ASP GLU ASP ILE ILE GLU ALA LYS GLU
SEQRES 7 A 155 THR LEU SER TRP ALA VAL SER ILE ILE ARG LYS GLU GLY
SEQRES 8 A 155 ALA GLU GLY GLU GLU HIS LEU LEU VAL ARG GLY LYS GLU
SEQRES 9 A 155 PRO PRO ASP ASP ILE VAL ASP PHE ALA ASP GLU VAL ASP
SEQRES 10 A 155 ALA ILE ALA ILE VAL ILE GLY ILE ARG LYS ARG SER PRO
SEQRES 11 A 155 THR GLY LYS LEU ILE PHE GLY SER VAL ALA ARG ASP VAL
SEQRES 12 A 155 ILE LEU LYS ALA ASN LYS PRO VAL ILE CYS ILE LYS
SEQRES 1 B 155 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 155 ARG GLU ASN LEU TYR PHE GLN GLY MSE ILE TYR MSE PRO
SEQRES 3 B 155 ILE VAL VAL ALA VAL ASP LYS LYS SER ASP ARG ALA GLU
SEQRES 4 B 155 ARG VAL LEU ARG PHE ALA ALA GLU GLU ALA ARG LEU ARG
SEQRES 5 B 155 GLY VAL PRO VAL TYR VAL VAL HIS SER LEU PRO GLY GLY
SEQRES 6 B 155 GLY ARG THR LYS ASP GLU ASP ILE ILE GLU ALA LYS GLU
SEQRES 7 B 155 THR LEU SER TRP ALA VAL SER ILE ILE ARG LYS GLU GLY
SEQRES 8 B 155 ALA GLU GLY GLU GLU HIS LEU LEU VAL ARG GLY LYS GLU
SEQRES 9 B 155 PRO PRO ASP ASP ILE VAL ASP PHE ALA ASP GLU VAL ASP
SEQRES 10 B 155 ALA ILE ALA ILE VAL ILE GLY ILE ARG LYS ARG SER PRO
SEQRES 11 B 155 THR GLY LYS LEU ILE PHE GLY SER VAL ALA ARG ASP VAL
SEQRES 12 B 155 ILE LEU LYS ALA ASN LYS PRO VAL ILE CYS ILE LYS
MODRES 3QTB MSE A 1 MET SELENOMETHIONINE
MODRES 3QTB MSE A 4 MET SELENOMETHIONINE
MODRES 3QTB MSE B 4 MET SELENOMETHIONINE
HET MSE A 1 5
HET MSE A 4 8
HET MSE B 4 8
HET D5M A 135 22
HET ACT B 135 4
HET ACT B 136 4
HET ACT B 137 4
HETNAM MSE SELENOMETHIONINE
HETNAM D5M 2'-DEOXYADENOSINE-5'-MONOPHOSPHATE
HETNAM ACT ACETATE ION
FORMUL 1 MSE 3(C5 H11 N O2 SE)
FORMUL 3 D5M C10 H14 N5 O6 P
FORMUL 4 ACT 3(C2 H3 O2 1-)
FORMUL 7 HOH *50(H2 O)
HELIX 1 1 SER A 14 GLY A 32 1 19
HELIX 2 2 GLY A 43 THR A 47 5 5
HELIX 3 3 LYS A 48 GLU A 69 1 22
HELIX 4 4 GLU A 83 VAL A 95 1 13
HELIX 5 5 GLY A 116 ALA A 126 1 11
HELIX 6 6 SER B 14 GLY B 32 1 19
HELIX 7 7 GLY B 43 THR B 47 5 5
HELIX 8 8 LYS B 48 GLU B 69 1 22
HELIX 9 9 GLU B 83 ASP B 96 1 14
HELIX 10 10 GLY B 116 ALA B 126 1 11
SHEET 1 A10 GLY A 73 VAL A 79 0
SHEET 2 A10 VAL A 35 LEU A 41 1 N HIS A 39 O LEU A 78
SHEET 3 A10 ILE A 6 ALA A 9 1 N ILE A 6 O TYR A 36
SHEET 4 A10 ALA A 99 GLY A 103 1 O VAL A 101 N VAL A 7
SHEET 5 A10 VAL A 130 ILE A 133 1 O ILE A 131 N ILE A 100
SHEET 6 A10 VAL B 130 ILE B 133 -1 O CYS B 132 N VAL A 130
SHEET 7 A10 ALA B 99 GLY B 103 1 N ILE B 100 O ILE B 131
SHEET 8 A10 ILE B 6 ALA B 9 1 N VAL B 7 O VAL B 101
SHEET 9 A10 VAL B 35 LEU B 41 1 O TYR B 36 N ILE B 6
SHEET 10 A10 GLY B 73 VAL B 79 1 O LEU B 78 N HIS B 39
SHEET 1 B 2 ARG B 105 ARG B 107 0
SHEET 2 B 2 LEU B 113 PHE B 115 -1 O ILE B 114 N LYS B 106
LINK C MSE A 1 N ILE A 2 1555 1555 1.34
LINK C TYR A 3 N MSE A 4 1555 1555 1.33
LINK C MSE A 4 N PRO A 5 1555 1555 1.34
LINK C TYR B 3 N MSE B 4 1555 1555 1.32
LINK C MSE B 4 N PRO B 5 1555 1555 1.34
SITE 1 AC1 12 ALA A 9 VAL A 10 ASP A 11 HIS A 39
SITE 2 AC1 12 SER A 40 PRO A 84 GLY A 103 GLY A 116
SITE 3 AC1 12 SER A 117 VAL A 118 ALA A 119 HOH A 164
SITE 1 AC2 2 LYS A 13 ARG B 80
SITE 1 AC3 4 ASP B 11 LYS B 12 ARG B 16 ARG B 107
SITE 1 AC4 3 GLY B 44 THR B 110 LYS B 112
CRYST1 109.607 42.655 61.289 90.00 116.82 90.00 C 1 2 1 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 0.009124 0.000000 0.004612 0.00000
SCALE2 0.000000 0.023444 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018282 0.00000
HETATM 1 N MSE A 1 -3.150 36.057 -16.081 1.00 70.43 N
ANISOU 1 N MSE A 1 7778 8540 10443 736 -198 1456 N
HETATM 2 CA MSE A 1 -3.821 34.727 -16.086 1.00 71.04 C
ANISOU 2 CA MSE A 1 7816 8748 10427 651 -262 1421 C
HETATM 3 C MSE A 1 -2.885 33.664 -16.667 1.00 69.74 C
ANISOU 3 C MSE A 1 7771 8682 10046 524 -360 1313 C
HETATM 4 O MSE A 1 -2.685 32.598 -16.063 1.00 70.37 O
ANISOU 4 O MSE A 1 7929 8764 10043 471 -337 1174 O
HETATM 5 CB MSE A 1 -5.126 34.792 -16.887 1.00 73.14 C
ANISOU 5 CB MSE A 1 7880 9140 10771 649 -350 1620 C
(ATOM LINES ARE NOT SHOWN.)
END
