HEADER TRANSFERASE 24-MAR-09 3A0T
TITLE CATALYTIC DOMAIN OF HISTIDINE KINASE THKA (TM1359) IN COMPLEX WITH ADP
TITLE 2 AND MG ION (TRIGONAL)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SENSOR PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: HISTIDINE KINASE THKA;
COMPND 6 EC: 2.7.13.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 GENE: TM_1359;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODONPLUS RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSETA
KEYWDS ATP-LID, KINASE, PHOSPHOPROTEIN, TRANSFERASE, TWO-COMPONENT
KEYWDS 2 REGULATORY SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.YAMADA,H.SUGIMOTO,M.KOBAYASHI,A.OHNO,H.NAKAMURA,Y.SHIRO
REVDAT 5 03-APR-24 3A0T 1 REMARK
REVDAT 4 13-MAR-24 3A0T 1 REMARK SEQADV LINK
REVDAT 3 10-JUL-13 3A0T 1 REMARK VERSN
REVDAT 2 17-NOV-09 3A0T 1 JRNL
REVDAT 1 20-OCT-09 3A0T 0
JRNL AUTH S.YAMADA,H.SUGIMOTO,M.KOBAYASHI,A.OHNO,H.NAKAMURA,Y.SHIRO
JRNL TITL STRUCTURE OF PAS-LINKED HISTIDINE KINASE AND THE RESPONSE
JRNL TITL 2 REGULATOR COMPLEX
JRNL REF STRUCTURE V. 17 1333 2009
JRNL REFN ISSN 0969-2126
JRNL PMID 19836334
JRNL DOI 10.1016/J.STR.2009.07.016
REMARK 2
REMARK 2 RESOLUTION. 1.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 22252
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1133
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) : 1.91
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.96
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1506
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2110
REMARK 3 BIN FREE R VALUE SET COUNT : 81
REMARK 3 BIN FREE R VALUE : 0.2360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1246
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 108
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.15000
REMARK 3 B22 (A**2) : 0.15000
REMARK 3 B33 (A**2) : -0.23000
REMARK 3 B12 (A**2) : 0.08000
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): 0.110
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.108
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.901
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1363 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1844 ; 1.930 ; 1.994
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 161 ; 6.769 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 69 ;34.697 ;24.348
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 269 ;17.443 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;15.472 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 203 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1011 ; 0.013 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 624 ; 0.328 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 932 ; 0.339 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 73 ; 0.115 ; 0.200
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): 53 ; 0.239 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.169 ; 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): 818 ; 3.306 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1296 ; 4.258 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 620 ; 6.164 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 544 ; 9.267 ; 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: NULL
REMARK 4
REMARK 4 3A0T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1000028668.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-SEP-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44B2
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 DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
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 : 22342
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.910
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 51.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.43200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: REFMAC 5.2.0019
REMARK 200 STARTING MODEL: NUCLEOTIDE FREE STRUCTURE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% ISOPROPANOL, 2.0M AMMONIUM
REMARK 280 SULPHATE, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.83867
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 30.41933
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 30.41933
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 60.83867
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 ARG A 755 CA - C - O ANGL. DEV. = 15.4 DEGREES
REMARK 500 ARG A 755 CA - C - O ANGL. DEV. = 25.7 DEGREES
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 ASN A 639 110.57 -162.29
REMARK 500 TYR A 680 -68.32 84.51
REMARK 500 PHE A 706 -6.10 81.19
REMARK 500 GLU A 739 -134.21 56.89
REMARK 500 ASN A 740 43.14 -101.00
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 800 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 2 O
REMARK 620 2 HOH A 3 O 92.3
REMARK 620 3 HOH A 4 O 91.1 89.6
REMARK 620 4 ASN A 661 OD1 84.9 86.3 174.2
REMARK 620 5 ADP A 801 O2A 90.2 177.2 89.0 95.2
REMARK 620 6 ADP A 801 O1B 177.0 90.1 90.8 93.4 87.4
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 MG A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3A0R RELATED DB: PDB
REMARK 900 STRUCTURE OF HISTIDINE KINASE THKA (TM1359) IN COMPLEX WITH
REMARK 900 RESPONSE REGULATOR PROTEIN TRRA (TM1360)
REMARK 900 RELATED ID: 3A0S RELATED DB: PDB
REMARK 900 PAS DOMAIN OF HISTIDINE KINASE THKA (TM1359)
DBREF 3A0T A 605 755 UNP Q9X180 Q9X180_THEMA 605 755
SEQADV 3A0T MET A 604 UNP Q9X180 EXPRESSION TAG
SEQRES 1 A 152 MET GLU PHE THR GLU PHE ASN LEU ASN GLU LEU ILE ARG
SEQRES 2 A 152 GLU VAL TYR VAL LEU PHE GLU GLU LYS ILE ARG LYS MET
SEQRES 3 A 152 ASN ILE ASP PHE CYS PHE GLU THR ASP ASN GLU ASP LEU
SEQRES 4 A 152 ARG VAL GLU ALA ASP ARG THR ARG ILE LYS GLN VAL LEU
SEQRES 5 A 152 ILE ASN LEU VAL GLN ASN ALA ILE GLU ALA THR GLY GLU
SEQRES 6 A 152 ASN GLY LYS ILE LYS ILE THR SER GLU ASP MET TYR THR
SEQRES 7 A 152 LYS VAL ARG VAL SER VAL TRP ASN SER GLY PRO PRO ILE
SEQRES 8 A 152 PRO GLU GLU LEU LYS GLU LYS ILE PHE SER PRO PHE PHE
SEQRES 9 A 152 THR THR LYS THR GLN GLY THR GLY LEU GLY LEU SER ILE
SEQRES 10 A 152 CYS ARG LYS ILE ILE GLU ASP GLU HIS GLY GLY LYS ILE
SEQRES 11 A 152 TRP THR GLU ASN ARG GLU ASN GLY VAL VAL PHE ILE PHE
SEQRES 12 A 152 GLU ILE PRO LYS THR PRO GLU LYS ARG
HET MG A 800 1
HET ADP A 801 27
HETNAM MG MAGNESIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 2 MG MG 2+
FORMUL 3 ADP C10 H15 N5 O10 P2
FORMUL 4 HOH *108(H2 O)
HELIX 1 1 LEU A 611 MET A 629 1 19
HELIX 2 2 ASP A 647 GLY A 667 1 21
HELIX 3 3 PRO A 695 LYS A 699 5 5
HELIX 4 4 GLU A 700 SER A 704 5 5
HELIX 5 5 LEU A 716 ASP A 727 1 12
SHEET 1 A 2 THR A 607 ASN A 610 0
SHEET 2 A 2 ARG A 643 ALA A 646 -1 O ALA A 646 N THR A 607
SHEET 1 B 5 ASP A 632 THR A 637 0
SHEET 2 B 5 LYS A 671 ASP A 678 1 O ILE A 672 N ASP A 632
SHEET 3 B 5 LYS A 682 SER A 690 -1 O TRP A 688 N LYS A 673
SHEET 4 B 5 GLY A 741 PRO A 749 -1 O PHE A 744 N VAL A 687
SHEET 5 B 5 LYS A 732 ARG A 738 -1 N GLU A 736 O VAL A 743
LINK O HOH A 2 MG MG A 800 1555 1555 2.09
LINK O HOH A 3 MG MG A 800 1555 1555 2.14
LINK O HOH A 4 MG MG A 800 1555 1555 2.25
LINK OD1 ASN A 661 MG MG A 800 1555 1555 2.09
LINK MG MG A 800 O2A ADP A 801 1555 1555 2.02
LINK MG MG A 800 O1B ADP A 801 1555 1555 2.04
SITE 1 AC1 5 HOH A 2 HOH A 3 HOH A 4 ASN A 661
SITE 2 AC1 5 ADP A 801
SITE 1 AC2 24 HOH A 1 HOH A 2 HOH A 3 HOH A 4
SITE 2 AC2 24 HOH A 7 HOH A 16 HOH A 21 HOH A 44
SITE 3 AC2 24 ASN A 661 ALA A 665 ASN A 689 ILE A 694
SITE 4 AC2 24 ILE A 702 PHE A 707 THR A 708 THR A 709
SITE 5 AC2 24 LYS A 710 GLY A 713 THR A 714 GLY A 715
SITE 6 AC2 24 GLY A 717 LEU A 718 PHE A 744 MG A 800
CRYST1 72.943 72.943 91.258 90.00 90.00 120.00 P 32 2 1 6
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 0.013709 0.007915 0.000000 0.00000
SCALE2 0.000000 0.015830 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010958 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
