HEADER TRANSCRIPTION 26-MAY-16 5K7H
TITLE CRYSTAL STRUCTURE OF AIBR IN COMPLEX WITH THE EFFECTOR MOLECULE
TITLE 2 ISOVALERYL COENZYME A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REGULATOR, TETR FAMILY;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYXOCOCCUS XANTHUS DK 1622;
SOURCE 3 ORGANISM_TAXID: 246197;
SOURCE 4 GENE: MXAN_4263;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TETR LIKE REGULATOR, ISOVALERYL COENZYME A, REGULATION, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR T.BOCK,C.VOLZ,R.MUELLER,W.BLANKENFELDT
REVDAT 3 10-JAN-24 5K7H 1 LINK
REVDAT 2 03-MAY-17 5K7H 1 JRNL
REVDAT 1 21-DEC-16 5K7H 0
JRNL AUTH T.BOCK,C.VOLZ,V.HERING,A.SCRIMA,R.MULLER,W.BLANKENFELDT
JRNL TITL THE AIBR-ISOVALERYL COENZYME A REGULATOR AND ITS DNA BINDING
JRNL TITL 2 SITE - A MODEL FOR THE REGULATION OF ALTERNATIVE DE NOVO
JRNL TITL 3 ISOVALERYL COENZYME A BIOSYNTHESIS IN MYXOCOCCUS XANTHUS.
JRNL REF NUCLEIC ACIDS RES. V. 45 2166 2017
JRNL REFN ESSN 1362-4962
JRNL PMID 27940564
JRNL DOI 10.1093/NAR/GKW1238
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 25108
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1231
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 44.8982 - 4.8866 1.00 2704 135 0.1659 0.2398
REMARK 3 2 4.8866 - 3.8793 1.00 2659 130 0.1521 0.1822
REMARK 3 3 3.8793 - 3.3892 1.00 2663 139 0.1877 0.2268
REMARK 3 4 3.3892 - 3.0794 1.00 2620 167 0.2311 0.2567
REMARK 3 5 3.0794 - 2.8587 1.00 2637 140 0.2369 0.2869
REMARK 3 6 2.8587 - 2.6902 1.00 2668 122 0.2284 0.2317
REMARK 3 7 2.6902 - 2.5555 1.00 2647 134 0.2278 0.2496
REMARK 3 8 2.5555 - 2.4442 1.00 2662 123 0.2357 0.2495
REMARK 3 9 2.4442 - 2.3501 1.00 2617 141 0.2702 0.3068
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.210
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.61
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.03
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 : 0.002 3056
REMARK 3 ANGLE : 0.512 4152
REMARK 3 CHIRALITY : 0.035 455
REMARK 3 PLANARITY : 0.002 518
REMARK 3 DIHEDRAL : 14.665 1780
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 5K7H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000220499.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-APR-15
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 : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.7
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25158
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 44.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.200
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 8.20
REMARK 200 R MERGE FOR SHELL (I) : 0.76500
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 5K7F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE PH 4.6, 2 M
REMARK 280 SODIUM CHLORIDE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 44.03933
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 88.07867
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 66.05900
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 110.09833
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 22.01967
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: 4580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 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 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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 ASN A 3
REMARK 465 THR A 4
REMARK 465 GLY A 5
REMARK 465 GLY A 6
REMARK 465 ARG A 7
REMARK 465 LYS A 8
REMARK 465 PRO A 9
REMARK 465 ASP A 10
REMARK 465 GLU A 11
REMARK 465 GLY A 12
REMARK 465 GLU A 13
REMARK 465 ALA A 198
REMARK 465 ALA A 199
REMARK 465 ALA A 200
REMARK 465 GLY A 201
REMARK 465 ASP A 202
REMARK 465 THR A 203
REMARK 465 ALA A 204
REMARK 465 GLY A 205
REMARK 465 GLN A 206
REMARK 465 ALA A 207
REMARK 465 GLY A 208
REMARK 465 PRO A 209
REMARK 465 SER A 210
REMARK 465 PRO A 211
REMARK 465 LEU A 212
REMARK 465 ARG A 213
REMARK 465 MET A 214
REMARK 465 VAL A 215
REMARK 465 PRO A 216
REMARK 465 SER A 217
REMARK 465 VAL A 218
REMARK 465 SER A 219
REMARK 465 ALA A 220
REMARK 465 THR A 221
REMARK 465 GLY A 222
REMARK 465 THR A 223
REMARK 465 ASP A 224
REMARK 465 SER A 225
REMARK 465 GLU A 226
REMARK 465 ASP A 227
REMARK 465 ALA A 228
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ASN B 3
REMARK 465 THR B 4
REMARK 465 GLY B 5
REMARK 465 GLY B 6
REMARK 465 ARG B 7
REMARK 465 LYS B 8
REMARK 465 PRO B 9
REMARK 465 ASP B 10
REMARK 465 GLU B 11
REMARK 465 GLY B 12
REMARK 465 GLU B 13
REMARK 465 ALA B 198
REMARK 465 ALA B 199
REMARK 465 ALA B 200
REMARK 465 GLY B 201
REMARK 465 ASP B 202
REMARK 465 THR B 203
REMARK 465 ALA B 204
REMARK 465 GLY B 205
REMARK 465 GLN B 206
REMARK 465 ALA B 207
REMARK 465 GLY B 208
REMARK 465 PRO B 209
REMARK 465 SER B 210
REMARK 465 PRO B 211
REMARK 465 LEU B 212
REMARK 465 ARG B 213
REMARK 465 MET B 214
REMARK 465 VAL B 215
REMARK 465 PRO B 216
REMARK 465 SER B 217
REMARK 465 VAL B 218
REMARK 465 SER B 219
REMARK 465 ALA B 220
REMARK 465 THR B 221
REMARK 465 GLY B 222
REMARK 465 THR B 223
REMARK 465 ASP B 224
REMARK 465 SER B 225
REMARK 465 GLU B 226
REMARK 465 ASP B 227
REMARK 465 ALA B 228
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 14 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 32 CG CD OE1 OE2
REMARK 470 GLU A 38 CG CD OE1 OE2
REMARK 470 ARG A 44 CG CD NE CZ NH1 NH2
REMARK 470 MET A 45 CG SD CE
REMARK 470 THR A 46 OG1 CG2
REMARK 470 LYS A 47 CG CD CE NZ
REMARK 470 HIS A 52 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 58 CG CD OE1 OE2
REMARK 470 LYS A 107 CG CD CE NZ
REMARK 470 GLU A 122 CG CD OE1 OE2
REMARK 470 ASP A 177 CG OD1 OD2
REMARK 470 ARG B 14 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 32 CG CD OE1 OE2
REMARK 470 GLN B 37 CG CD OE1 NE2
REMARK 470 ARG B 44 CG CD NE CZ NH1 NH2
REMARK 470 THR B 46 OG1 CG2
REMARK 470 LYS B 47 CG CD CE NZ
REMARK 470 HIS B 52 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 74 CG CD OE1 OE2
REMARK 470 GLU B 88 CG CD OE1 OE2
REMARK 470 LYS B 107 CG CD CE NZ
REMARK 470 ASP B 177 CG OD1 OD2
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 O HIS B 116 NH1 ARG B 124 2.11
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 VAL A 76 -72.63 -120.56
REMARK 500 ARG A 103 -159.77 -139.53
REMARK 500 ARG B 44 84.28 -68.03
REMARK 500 VAL B 76 -74.20 -115.62
REMARK 500 ARG B 103 -156.64 -136.97
REMARK 500 TRP B 173 -31.86 -132.38
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 NI A 301 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 96 NE2
REMARK 620 2 CL A 302 CL 116.4
REMARK 620 3 CL A 303 CL 104.2 105.9
REMARK 620 4 HIS B 96 NE2 64.1 105.9 44.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NI A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IVC A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IVC B 302
DBREF 5K7H A 1 228 UNP Q1D4I5 Q1D4I5_MYXXD 1 228
DBREF 5K7H B 1 228 UNP Q1D4I5 Q1D4I5_MYXXD 1 228
SEQADV 5K7H GLY A -2 UNP Q1D4I5 EXPRESSION TAG
SEQADV 5K7H SER A -1 UNP Q1D4I5 EXPRESSION TAG
SEQADV 5K7H HIS A 0 UNP Q1D4I5 EXPRESSION TAG
SEQADV 5K7H GLY B -2 UNP Q1D4I5 EXPRESSION TAG
SEQADV 5K7H SER B -1 UNP Q1D4I5 EXPRESSION TAG
SEQADV 5K7H HIS B 0 UNP Q1D4I5 EXPRESSION TAG
SEQRES 1 A 231 GLY SER HIS MET THR ASN THR GLY GLY ARG LYS PRO ASP
SEQRES 2 A 231 GLU GLY GLU ARG TYR ARG ALA ILE LEU GLU THR ALA ALA
SEQRES 3 A 231 ARG LEU ILE CYS ASP ARG GLY TYR GLU GLY THR SER MET
SEQRES 4 A 231 GLN GLU ILE ALA ALA ALA CYS ARG MET THR LYS ALA GLY
SEQRES 5 A 231 LEU TYR HIS HIS ILE GLN ASN LYS GLU GLN LEU LEU PHE
SEQRES 6 A 231 ALA ILE MET ASN TYR GLY MET ASP LEU PHE GLU GLU GLN
SEQRES 7 A 231 VAL LEU SER ARG VAL GLN ASP ILE ALA ASN PRO VAL GLU
SEQRES 8 A 231 ARG LEU ARG ALA CYS MET ARG HIS ASN ILE LEU LEU VAL
SEQRES 9 A 231 THR ARG GLY TRP SER LYS GLU VAL ILE ILE ILE LEU HIS
SEQRES 10 A 231 GLU HIS ALA THR LEU THR GLY GLU THR ARG ALA PHE ILE
SEQRES 11 A 231 ASP ALA ARG LYS LYS LYS TYR VAL ASP PHE LEU GLU GLU
SEQRES 12 A 231 ALA PHE SER GLN ALA SER GLN GLN GLY LEU ILE ARG PRO
SEQRES 13 A 231 VAL ASP PRO THR VAL GLY ALA PHE SER PHE LEU GLY MET
SEQRES 14 A 231 VAL LEU TRP ILE TYR LYS TRP PHE LYS PRO ASP GLY ARG
SEQRES 15 A 231 LEU THR ASP GLU GLN ILE ALA ASP GLY MET VAL GLY MET
SEQRES 16 A 231 LEU PHE PRO PRO PHE ALA ALA ALA GLY ASP THR ALA GLY
SEQRES 17 A 231 GLN ALA GLY PRO SER PRO LEU ARG MET VAL PRO SER VAL
SEQRES 18 A 231 SER ALA THR GLY THR ASP SER GLU ASP ALA
SEQRES 1 B 231 GLY SER HIS MET THR ASN THR GLY GLY ARG LYS PRO ASP
SEQRES 2 B 231 GLU GLY GLU ARG TYR ARG ALA ILE LEU GLU THR ALA ALA
SEQRES 3 B 231 ARG LEU ILE CYS ASP ARG GLY TYR GLU GLY THR SER MET
SEQRES 4 B 231 GLN GLU ILE ALA ALA ALA CYS ARG MET THR LYS ALA GLY
SEQRES 5 B 231 LEU TYR HIS HIS ILE GLN ASN LYS GLU GLN LEU LEU PHE
SEQRES 6 B 231 ALA ILE MET ASN TYR GLY MET ASP LEU PHE GLU GLU GLN
SEQRES 7 B 231 VAL LEU SER ARG VAL GLN ASP ILE ALA ASN PRO VAL GLU
SEQRES 8 B 231 ARG LEU ARG ALA CYS MET ARG HIS ASN ILE LEU LEU VAL
SEQRES 9 B 231 THR ARG GLY TRP SER LYS GLU VAL ILE ILE ILE LEU HIS
SEQRES 10 B 231 GLU HIS ALA THR LEU THR GLY GLU THR ARG ALA PHE ILE
SEQRES 11 B 231 ASP ALA ARG LYS LYS LYS TYR VAL ASP PHE LEU GLU GLU
SEQRES 12 B 231 ALA PHE SER GLN ALA SER GLN GLN GLY LEU ILE ARG PRO
SEQRES 13 B 231 VAL ASP PRO THR VAL GLY ALA PHE SER PHE LEU GLY MET
SEQRES 14 B 231 VAL LEU TRP ILE TYR LYS TRP PHE LYS PRO ASP GLY ARG
SEQRES 15 B 231 LEU THR ASP GLU GLN ILE ALA ASP GLY MET VAL GLY MET
SEQRES 16 B 231 LEU PHE PRO PRO PHE ALA ALA ALA GLY ASP THR ALA GLY
SEQRES 17 B 231 GLN ALA GLY PRO SER PRO LEU ARG MET VAL PRO SER VAL
SEQRES 18 B 231 SER ALA THR GLY THR ASP SER GLU ASP ALA
HET NI A 301 1
HET CL A 302 1
HET CL A 303 1
HET CL A 304 1
HET IVC A 305 94
HET CL B 301 1
HET IVC B 302 94
HETNAM NI NICKEL (II) ION
HETNAM CL CHLORIDE ION
HETNAM IVC ISOVALERYL-COENZYME A
HETSYN IVC S-[2-[3-[[(2R)-4-[[[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-
HETSYN 2 IVC YL)-4-OXIDANYL-3-PHOSPHONOOXY-OXOLAN-2-YL]METHOXY-
HETSYN 3 IVC OXIDANYL-PHOSPHORYL]OXY-OXIDANYL-PHOSPHORYL]OXY-3,3-
HETSYN 4 IVC DIMETHYL-2-OXIDANYL-
HETSYN 5 IVC BUTANOYL]AMINO]PROPANOYLAMINO]ETHYL] 3-
HETSYN 6 IVC METHYLBUTANETHIOATE
FORMUL 3 NI NI 2+
FORMUL 4 CL 4(CL 1-)
FORMUL 7 IVC 2(C26 H44 N7 O17 P3 S)
FORMUL 10 HOH *28(H2 O)
HELIX 1 AA1 ARG A 14 ARG A 29 1 16
HELIX 2 AA2 SER A 35 CYS A 43 1 9
HELIX 3 AA3 THR A 46 ILE A 54 1 9
HELIX 4 AA4 ASN A 56 VAL A 76 1 21
HELIX 5 AA5 VAL A 76 GLN A 81 1 6
HELIX 6 AA6 ASN A 85 THR A 102 1 18
HELIX 7 AA7 TRP A 105 GLU A 115 1 11
HELIX 8 AA8 HIS A 116 LEU A 119 5 4
HELIX 9 AA9 THR A 120 GLN A 148 1 29
HELIX 10 AB1 ASP A 155 TRP A 169 1 15
HELIX 11 AB2 ILE A 170 TRP A 173 5 4
HELIX 12 AB3 THR A 181 PHE A 194 1 14
HELIX 13 AB4 TYR B 15 ARG B 29 1 15
HELIX 14 AB5 SER B 35 CYS B 43 1 9
HELIX 15 AB6 THR B 46 HIS B 52 1 7
HELIX 16 AB7 ASN B 56 VAL B 76 1 21
HELIX 17 AB8 VAL B 76 GLN B 81 1 6
HELIX 18 AB9 ASN B 85 THR B 102 1 18
HELIX 19 AC1 TRP B 105 GLU B 115 1 11
HELIX 20 AC2 THR B 120 GLN B 148 1 29
HELIX 21 AC3 ASP B 155 TRP B 169 1 15
HELIX 22 AC4 ILE B 170 TRP B 173 5 4
HELIX 23 AC5 THR B 181 PHE B 194 1 14
LINK NE2 HIS A 96 NI NI A 301 1555 1555 1.91
LINK NI NI A 301 CL CL A 302 1555 1555 2.24
LINK NI NI A 301 CL CL A 303 1555 1555 2.20
LINK NI NI A 301 NE2 HIS B 96 5554 1555 1.91
SITE 1 AC1 4 HIS A 96 CL A 302 CL A 303 HIS B 96
SITE 1 AC2 4 HIS A 96 NI A 301 CL A 303 HIS B 96
SITE 1 AC3 4 HIS A 96 NI A 301 CL A 302 HIS B 96
SITE 1 AC4 2 LYS A 131 IVC B 302
SITE 1 AC5 15 TRP A 169 LYS A 172 TRP A 173 PHE A 174
SITE 2 AC5 15 LYS A 175 GLY A 178 ARG A 179 LEU A 180
SITE 3 AC5 15 PHE B 72 LYS B 131 LYS B 132 ASP B 136
SITE 4 AC5 15 GLU B 139 PHE B 161 CL B 301
SITE 1 AC6 2 IVC A 305 LYS B 131
SITE 1 AC7 17 PHE A 72 LYS A 131 LYS A 132 TYR A 134
SITE 2 AC7 17 VAL A 135 PHE A 161 CL A 304 GLU B 122
SITE 3 AC7 17 TRP B 169 LYS B 172 TRP B 173 PHE B 174
SITE 4 AC7 17 LYS B 175 GLY B 178 ARG B 179 LEU B 180
SITE 5 AC7 17 HOH B 405
CRYST1 89.780 89.780 132.118 90.00 90.00 120.00 P 61 12
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 0.011138 0.006431 0.000000 0.00000
SCALE2 0.000000 0.012861 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007569 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
