HEADER TRANSCRIPTION 01-OCT-04 1XMA
TITLE STRUCTURE OF A TRANSCRIPTIONAL REGULATOR FROM CLOSTRIDIUM THERMOCELLUM
TITLE 2 CTH-833
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PREDICTED TRANSCRIPTIONAL REGULATOR;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;
SOURCE 3 ORGANISM_TAXID: 1515;
SOURCE 4 ATCC: 27405;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CLOSTRIDIUM THERMOCELLUM, TRANSCRIPTIONAL REGULATOR, SOUTHEAST
KEYWDS 2 COLLABORATORY FOR STRUCTURAL GENOMICS, SECSG, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE, PSI, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR H.YANG,L.CHEN,D.LEE,J.HABEL,J.NGUYEN,S.-H.CHANG,I.KATAEVA,H.XU,
AUTHOR 2 J.CHANG,M.ZHAO,P.HORANYI,Q.FLORENCE,W.ZHOU,W.TEMPEL,D.LIN,
AUTHOR 3 J.PRAISSMAN,H.ZHANG,W.B.ARENDALL III,J.S.RICHARDSON,D.C.RICHARDSON,
AUTHOR 4 L.LJUNGDAHL,Z.-J.LIU,J.P.ROSE,B.-C.WANG,SOUTHEAST COLLABORATORY FOR
AUTHOR 5 STRUCTURAL GENOMICS (SECSG)
REVDAT 7 14-FEB-24 1XMA 1 REMARK LINK
REVDAT 6 18-MAR-20 1XMA 1 REMARK SEQADV
REVDAT 5 11-OCT-17 1XMA 1 REMARK
REVDAT 4 13-JUL-11 1XMA 1 VERSN
REVDAT 3 24-FEB-09 1XMA 1 VERSN
REVDAT 2 01-FEB-05 1XMA 1 REMARK
REVDAT 1 14-DEC-04 1XMA 0
JRNL AUTH H.YANG,L.CHEN,D.LEE,J.HABEL,J.NGUYEN,S.-H.CHANG,I.KATAEVA,
JRNL AUTH 2 H.XU,J.CHANG,M.ZHAO,P.HORANYI,Q.FLORENCE,W.ZHOU,W.TEMPEL,
JRNL AUTH 3 D.LIN,J.PRAISSMAN,H.ZHANG,W.B.ARENDALL III,J.S.RICHARDSON,
JRNL AUTH 4 D.C.RICHARDSON,L.LJUNGDAHL,Z.-J.LIU,J.P.ROSE,B.-C.WANG,
JRNL AUTH 5 SOUTHEAST COLLABORATORY FOR STRUCTURAL GENOMICS
JRNL TITL STRUCTURE OF A TRANSCRIPTIONAL REGULATOR FROM CLOSTRIDIUM
JRNL TITL 2 THERMOCELLUM CTH-833
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.2.0005
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.24
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 9669
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) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 518
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 472
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : 37
REMARK 3 BIN FREE R VALUE : 0.3320
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1698
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 40
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.07200
REMARK 3 B22 (A**2) : 0.03300
REMARK 3 B33 (A**2) : 0.04100
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.02400
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.400
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.268
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1748 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1608 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2348 ; 1.200 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3745 ; 3.793 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 200 ; 6.271 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 81 ;37.440 ;23.333
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 345 ;15.421 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;19.221 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 259 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1858 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 372 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 330 ; 0.193 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1274 ; 0.237 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 836 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 810 ; 0.109 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 51 ; 0.158 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.257 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 7 ; 0.126 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 73 ; 0.260 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.090 ; 0.200
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): 1007 ; 2.057 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 422 ; 0.000 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1640 ; 3.216 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 741 ; 2.323 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 708 ; 3.324 ; 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 BULK SOLVENT
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 ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1XMA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1000030508.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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 RU200
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 92
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10985
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
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) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 43.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.15100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE 2.06, RESOLVE 2.06, ISAS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 31.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8.5% V/V ISOPROPANOL, 10% W/V PEG
REMARK 280 4000, 15% V/V GLYCEROL, 0.085M TRIS, MODIFIED MICROBATCH,
REMARK 280 TEMPERATURE 291K, PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 26.08000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE:
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). THE BIOLOGICAL UNIT IS
REMARK 300 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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -113.0 KCAL/MOL
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 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -47.67528
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 51.02893
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 -30
REMARK 465 GLY A -29
REMARK 465 SER A -28
REMARK 465 SER A -27
REMARK 465 HIS A -26
REMARK 465 HIS A -25
REMARK 465 HIS A -24
REMARK 465 HIS A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 SER A -20
REMARK 465 SER A -19
REMARK 465 GLY A -18
REMARK 465 LEU A -17
REMARK 465 VAL A -16
REMARK 465 PRO A -15
REMARK 465 ARG A -14
REMARK 465 GLY A -13
REMARK 465 SER A -12
REMARK 465 GLN A -11
REMARK 465 SER A -10
REMARK 465 THR A -9
REMARK 465 SER A -8
REMARK 465 LEU A -7
REMARK 465 TYR A -6
REMARK 465 LYS A -5
REMARK 465 LYS A -4
REMARK 465 ALA A -3
REMARK 465 GLY A -2
REMARK 465 LEU A -1
REMARK 465 MET A 0
REMARK 465 VAL A 1
REMARK 465 ILE A 2
REMARK 465 SER A 3
REMARK 465 GLN A 70
REMARK 465 GLY A 71
REMARK 465 GLU A 107
REMARK 465 LEU A 108
REMARK 465 GLU A 109
REMARK 465 SER A 110
REMARK 465 ASN A 111
REMARK 465 GLY A 112
REMARK 465 ASP A 113
REMARK 465 ASN A 114
REMARK 465 MET B -30
REMARK 465 GLY B -29
REMARK 465 SER B -28
REMARK 465 SER B -27
REMARK 465 HIS B -26
REMARK 465 HIS B -25
REMARK 465 HIS B -24
REMARK 465 HIS B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 SER B -20
REMARK 465 SER B -19
REMARK 465 GLY B -18
REMARK 465 LEU B -17
REMARK 465 VAL B -16
REMARK 465 PRO B -15
REMARK 465 ARG B -14
REMARK 465 GLY B -13
REMARK 465 SER B -12
REMARK 465 GLN B -11
REMARK 465 SER B -10
REMARK 465 THR B -9
REMARK 465 SER B -8
REMARK 465 LEU B -7
REMARK 465 TYR B -6
REMARK 465 LYS B -5
REMARK 465 LYS B -4
REMARK 465 ALA B -3
REMARK 465 GLY B -2
REMARK 465 LEU B -1
REMARK 465 MET B 0
REMARK 465 GLN B 70
REMARK 465 GLY B 71
REMARK 465 LYS B 72
REMARK 465 GLU B 107
REMARK 465 LEU B 108
REMARK 465 GLU B 109
REMARK 465 SER B 110
REMARK 465 ASN B 111
REMARK 465 GLY B 112
REMARK 465 ASP B 113
REMARK 465 ASN B 114
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 ARG A 8 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 106 CE NZ
REMARK 470 ARG B 8 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 85 CG CD CE NZ
REMARK 470 LYS B 99 CE NZ
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 GLU A 39 -10.28 78.11
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 HG A 116 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 91 O
REMARK 620 2 GLU A 92 N 39.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG B 115 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 21 OE1
REMARK 620 2 LYS B 36 NZ 98.3
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 HG B 115
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 116
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 115
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 116
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 413
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CTH-833 RELATED DB: TARGETDB
DBREF 1XMA A 2 114 GB 48858444 ZP_00312398 2 114
DBREF 1XMA B 2 114 GB 48858444 ZP_00312398 2 114
SEQADV 1XMA MET A -30 GB 48858444 EXPRESSION TAG
SEQADV 1XMA GLY A -29 GB 48858444 EXPRESSION TAG
SEQADV 1XMA SER A -28 GB 48858444 EXPRESSION TAG
SEQADV 1XMA SER A -27 GB 48858444 EXPRESSION TAG
SEQADV 1XMA HIS A -26 GB 48858444 EXPRESSION TAG
SEQADV 1XMA HIS A -25 GB 48858444 EXPRESSION TAG
SEQADV 1XMA HIS A -24 GB 48858444 EXPRESSION TAG
SEQADV 1XMA HIS A -23 GB 48858444 EXPRESSION TAG
SEQADV 1XMA HIS A -22 GB 48858444 EXPRESSION TAG
SEQADV 1XMA HIS A -21 GB 48858444 EXPRESSION TAG
SEQADV 1XMA SER A -20 GB 48858444 EXPRESSION TAG
SEQADV 1XMA SER A -19 GB 48858444 EXPRESSION TAG
SEQADV 1XMA GLY A -18 GB 48858444 EXPRESSION TAG
SEQADV 1XMA LEU A -17 GB 48858444 EXPRESSION TAG
SEQADV 1XMA VAL A -16 GB 48858444 EXPRESSION TAG
SEQADV 1XMA PRO A -15 GB 48858444 EXPRESSION TAG
SEQADV 1XMA ARG A -14 GB 48858444 EXPRESSION TAG
SEQADV 1XMA GLY A -13 GB 48858444 EXPRESSION TAG
SEQADV 1XMA SER A -12 GB 48858444 EXPRESSION TAG
SEQADV 1XMA GLN A -11 GB 48858444 EXPRESSION TAG
SEQADV 1XMA SER A -10 GB 48858444 EXPRESSION TAG
SEQADV 1XMA THR A -9 GB 48858444 EXPRESSION TAG
SEQADV 1XMA SER A -8 GB 48858444 EXPRESSION TAG
SEQADV 1XMA LEU A -7 GB 48858444 EXPRESSION TAG
SEQADV 1XMA TYR A -6 GB 48858444 EXPRESSION TAG
SEQADV 1XMA LYS A -5 GB 48858444 EXPRESSION TAG
SEQADV 1XMA LYS A -4 GB 48858444 EXPRESSION TAG
SEQADV 1XMA ALA A -3 GB 48858444 EXPRESSION TAG
SEQADV 1XMA GLY A -2 GB 48858444 EXPRESSION TAG
SEQADV 1XMA LEU A -1 GB 48858444 EXPRESSION TAG
SEQADV 1XMA MET A 0 GB 48858444 EXPRESSION TAG
SEQADV 1XMA VAL A 1 GB 48858444 EXPRESSION TAG
SEQADV 1XMA MET B -30 GB 48858444 EXPRESSION TAG
SEQADV 1XMA GLY B -29 GB 48858444 EXPRESSION TAG
SEQADV 1XMA SER B -28 GB 48858444 EXPRESSION TAG
SEQADV 1XMA SER B -27 GB 48858444 EXPRESSION TAG
SEQADV 1XMA HIS B -26 GB 48858444 EXPRESSION TAG
SEQADV 1XMA HIS B -25 GB 48858444 EXPRESSION TAG
SEQADV 1XMA HIS B -24 GB 48858444 EXPRESSION TAG
SEQADV 1XMA HIS B -23 GB 48858444 EXPRESSION TAG
SEQADV 1XMA HIS B -22 GB 48858444 EXPRESSION TAG
SEQADV 1XMA HIS B -21 GB 48858444 EXPRESSION TAG
SEQADV 1XMA SER B -20 GB 48858444 EXPRESSION TAG
SEQADV 1XMA SER B -19 GB 48858444 EXPRESSION TAG
SEQADV 1XMA GLY B -18 GB 48858444 EXPRESSION TAG
SEQADV 1XMA LEU B -17 GB 48858444 EXPRESSION TAG
SEQADV 1XMA VAL B -16 GB 48858444 EXPRESSION TAG
SEQADV 1XMA PRO B -15 GB 48858444 EXPRESSION TAG
SEQADV 1XMA ARG B -14 GB 48858444 EXPRESSION TAG
SEQADV 1XMA GLY B -13 GB 48858444 EXPRESSION TAG
SEQADV 1XMA SER B -12 GB 48858444 EXPRESSION TAG
SEQADV 1XMA GLN B -11 GB 48858444 EXPRESSION TAG
SEQADV 1XMA SER B -10 GB 48858444 EXPRESSION TAG
SEQADV 1XMA THR B -9 GB 48858444 EXPRESSION TAG
SEQADV 1XMA SER B -8 GB 48858444 EXPRESSION TAG
SEQADV 1XMA LEU B -7 GB 48858444 EXPRESSION TAG
SEQADV 1XMA TYR B -6 GB 48858444 EXPRESSION TAG
SEQADV 1XMA LYS B -5 GB 48858444 EXPRESSION TAG
SEQADV 1XMA LYS B -4 GB 48858444 EXPRESSION TAG
SEQADV 1XMA ALA B -3 GB 48858444 EXPRESSION TAG
SEQADV 1XMA GLY B -2 GB 48858444 EXPRESSION TAG
SEQADV 1XMA LEU B -1 GB 48858444 EXPRESSION TAG
SEQADV 1XMA MET B 0 GB 48858444 EXPRESSION TAG
SEQADV 1XMA VAL B 1 GB 48858444 EXPRESSION TAG
SEQRES 1 A 145 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 145 LEU VAL PRO ARG GLY SER GLN SER THR SER LEU TYR LYS
SEQRES 3 A 145 LYS ALA GLY LEU MET VAL ILE SER SER ASP VAL ILE ARG
SEQRES 4 A 145 GLY TYR VAL ASP THR ILE ILE LEU SER LEU LEU ILE GLU
SEQRES 5 A 145 GLY ASP SER TYR GLY TYR GLU ILE SER LYS ASN ILE ARG
SEQRES 6 A 145 ILE LYS THR ASP GLU LEU TYR VAL ILE LYS GLU THR THR
SEQRES 7 A 145 LEU TYR SER ALA PHE ALA ARG LEU GLU LYS ASN GLY TYR
SEQRES 8 A 145 ILE LYS SER TYR TYR GLY GLU GLU THR GLN GLY LYS ARG
SEQRES 9 A 145 ARG THR TYR TYR ARG ILE THR PRO GLU GLY ILE LYS TYR
SEQRES 10 A 145 TYR LYS GLN LYS CYS GLU GLU TRP GLU LEU THR LYS LYS
SEQRES 11 A 145 VAL ILE ASN LYS PHE VAL LYS GLU LEU GLU SER ASN GLY
SEQRES 12 A 145 ASP ASN
SEQRES 1 B 145 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 145 LEU VAL PRO ARG GLY SER GLN SER THR SER LEU TYR LYS
SEQRES 3 B 145 LYS ALA GLY LEU MET VAL ILE SER SER ASP VAL ILE ARG
SEQRES 4 B 145 GLY TYR VAL ASP THR ILE ILE LEU SER LEU LEU ILE GLU
SEQRES 5 B 145 GLY ASP SER TYR GLY TYR GLU ILE SER LYS ASN ILE ARG
SEQRES 6 B 145 ILE LYS THR ASP GLU LEU TYR VAL ILE LYS GLU THR THR
SEQRES 7 B 145 LEU TYR SER ALA PHE ALA ARG LEU GLU LYS ASN GLY TYR
SEQRES 8 B 145 ILE LYS SER TYR TYR GLY GLU GLU THR GLN GLY LYS ARG
SEQRES 9 B 145 ARG THR TYR TYR ARG ILE THR PRO GLU GLY ILE LYS TYR
SEQRES 10 B 145 TYR LYS GLN LYS CYS GLU GLU TRP GLU LEU THR LYS LYS
SEQRES 11 B 145 VAL ILE ASN LYS PHE VAL LYS GLU LEU GLU SER ASN GLY
SEQRES 12 B 145 ASP ASN
HET HG A 115 1
HET HG A 116 1
HET UNX A 403 1
HET UNX A 404 1
HET UNX A 409 1
HET UNX A 411 1
HET HG B 115 1
HET HG B 116 1
HET UNX B 401 1
HET UNX B 402 1
HET UNX B 405 1
HET UNX B 406 1
HET UNX B 407 1
HET UNX B 408 1
HET UNX B 410 1
HET UNX B 412 1
HET UNX B 413 1
HETNAM HG MERCURY (II) ION
HETNAM UNX UNKNOWN ATOM OR ION
FORMUL 3 HG 4(HG 2+)
FORMUL 5 UNX 13(X)
FORMUL 20 HOH *40(H2 O)
HELIX 1 1 VAL A 6 GLY A 9 5 4
HELIX 2 2 TYR A 10 GLY A 22 1 13
HELIX 3 3 GLY A 26 ASP A 38 1 13
HELIX 4 4 LYS A 44 ASN A 58 1 15
HELIX 5 5 THR A 80 LYS A 103 1 24
HELIX 6 6 SER B 3 GLY B 22 1 20
HELIX 7 7 GLY B 26 THR B 37 1 12
HELIX 8 8 LYS B 44 ASN B 58 1 15
HELIX 9 9 THR B 80 VAL B 105 1 26
SHEET 1 A 3 SER A 24 TYR A 25 0
SHEET 2 A 3 THR A 75 ILE A 79 -1 O TYR A 77 N SER A 24
SHEET 3 A 3 ILE A 61 TYR A 65 -1 N TYR A 64 O TYR A 76
SHEET 1 B 3 SER B 24 TYR B 25 0
SHEET 2 B 3 THR B 75 ILE B 79 -1 O TYR B 77 N SER B 24
SHEET 3 B 3 ILE B 61 TYR B 65 -1 N LYS B 62 O ARG B 78
LINK O CYS A 91 HG HG A 116 1555 1555 3.28
LINK N GLU A 92 HG HG A 116 1555 1555 3.39
LINK HG HG A 115 O LYS B 106 1555 1456 2.37
LINK N VAL B 1 HG HG B 116 1555 1555 2.80
LINK OE1 GLU B 21 HG HG B 115 1555 1555 2.97
LINK NZ LYS B 36 HG HG B 115 1555 1555 2.16
SITE 1 AC1 2 GLU B 21 LYS B 36
SITE 1 AC2 1 VAL B 1
SITE 1 AC3 3 TYR A 87 CYS A 91 LYS B 106
SITE 1 AC4 2 CYS A 91 GLU A 92
SITE 1 AC5 3 LEU B 40 UNX B 402 UNX B 412
SITE 1 AC6 3 LEU B 40 VAL B 42 UNX B 401
SITE 1 AC7 4 SER A 24 ILE A 29 ASN A 32 UNX A 404
SITE 1 AC8 5 LEU A 18 GLY A 22 UNX A 403 UNX A 409
SITE 2 AC8 5 UNX A 411
SITE 1 AC9 3 ILE B 35 ASP B 38 UNX B 406
SITE 1 BC1 2 GLU B 39 UNX B 405
SITE 1 BC2 4 TYR B 25 GLY B 26 THR B 75 UNX B 408
SITE 1 BC3 3 TYR B 49 TYR B 77 UNX B 407
SITE 1 BC4 3 ASP A 23 GLU A 28 UNX A 404
SITE 1 BC5 3 LEU B 18 GLY B 22 UNX B 413
SITE 1 BC6 2 GLU A 21 UNX A 404
SITE 1 BC7 3 VAL B 1 ILE B 2 UNX B 401
SITE 1 BC8 4 GLY B 22 ASP B 23 GLU B 28 UNX B 410
CRYST1 45.483 52.160 51.076 90.00 92.46 90.00 P 1 21 1 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 0.021986 0.000000 0.000945 0.00000
SCALE2 0.000000 0.019172 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019597 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
