HEADER TRANSCRIPTION 24-JUL-12 4G9Y
TITLE CRYSTAL STRUCTURE OF THE PCAV TRANSCRIPTIONAL REGULATOR FROM
TITLE 2 STREPTOMYCES COELICOLOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PCAV TRANSCRIPTIONAL REGULATOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR;
SOURCE 3 ORGANISM_TAXID: 100226;
SOURCE 4 STRAIN: ATCC BAA-471 / A3(2) / M145;
SOURCE 5 GENE: SCO6704;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) GOLD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS MARR FAMILY, WINGED HELIX-TURN-HELIX, TRANSCRIPTION FACTOR,
KEYWDS 2 TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR B.L.BROWN,J.R.DAVIS,J.K.SELLO,R.PAGE
REVDAT 2 13-SEP-23 4G9Y 1 REMARK SEQADV
REVDAT 1 05-JUN-13 4G9Y 0
JRNL AUTH J.R.DAVIS,B.L.BROWN,R.PAGE,J.K.SELLO
JRNL TITL STUDY OF PCAV FROM STREPTOMYCES COELICOLOR YIELDS NEW
JRNL TITL 2 INSIGHTS INTO LIGAND-RESPONSIVE MARR FAMILY TRANSCRIPTION
JRNL TITL 3 FACTORS.
JRNL REF NUCLEIC ACIDS RES. V. 41 3888 2013
JRNL REFN ISSN 0305-1048
JRNL PMID 23396446
JRNL DOI 10.1093/NAR/GKT009
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 17131
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1724
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 41.2854 - 4.6936 1.00 1395 148 0.1742 0.1574
REMARK 3 2 4.6936 - 3.7262 1.00 1319 151 0.1431 0.1572
REMARK 3 3 3.7262 - 3.2554 1.00 1291 138 0.1616 0.2067
REMARK 3 4 3.2554 - 2.9579 1.00 1282 146 0.1725 0.1989
REMARK 3 5 2.9579 - 2.7459 1.00 1289 137 0.1800 0.1983
REMARK 3 6 2.7459 - 2.5841 1.00 1277 141 0.1749 0.2095
REMARK 3 7 2.5841 - 2.4547 1.00 1269 142 0.1823 0.2470
REMARK 3 8 2.4547 - 2.3478 1.00 1276 143 0.1943 0.2430
REMARK 3 9 2.3478 - 2.2574 1.00 1253 146 0.1954 0.2223
REMARK 3 10 2.2574 - 2.1795 1.00 1260 138 0.2170 0.2433
REMARK 3 11 2.1795 - 2.1114 1.00 1255 148 0.2352 0.2678
REMARK 3 12 2.1114 - 2.0511 1.00 1241 146 0.2733 0.2807
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.540
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.008 1101
REMARK 3 ANGLE : 1.115 1489
REMARK 3 CHIRALITY : 0.070 170
REMARK 3 PLANARITY : 0.005 198
REMARK 3 DIHEDRAL : 11.852 423
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 8:34)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.0012 -18.8193 -41.0216
REMARK 3 T TENSOR
REMARK 3 T11: 0.1975 T22: 0.2272
REMARK 3 T33: 0.1676 T12: -0.0557
REMARK 3 T13: -0.0264 T23: -0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 0.2232 L22: 0.2012
REMARK 3 L33: 0.1353 L12: 0.0211
REMARK 3 L13: 0.0036 L23: -0.0081
REMARK 3 S TENSOR
REMARK 3 S11: -0.1058 S12: 0.3485 S13: -0.0452
REMARK 3 S21: -0.4074 S22: 0.2675 S23: -0.1994
REMARK 3 S31: 0.0366 S32: 0.3651 S33: 0.0121
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 35:97)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7256 -12.3401 -20.3855
REMARK 3 T TENSOR
REMARK 3 T11: 0.1785 T22: 0.2558
REMARK 3 T33: 0.3003 T12: -0.1239
REMARK 3 T13: 0.0198 T23: 0.0927
REMARK 3 L TENSOR
REMARK 3 L11: 0.3958 L22: 0.6429
REMARK 3 L33: 0.6249 L12: 0.1821
REMARK 3 L13: -0.3398 L23: -0.0935
REMARK 3 S TENSOR
REMARK 3 S11: -0.1178 S12: -0.3053 S13: -0.4328
REMARK 3 S21: 0.2066 S22: -0.1980 S23: -0.3750
REMARK 3 S31: 0.0414 S32: 0.2919 S33: -0.3440
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 98:143)
REMARK 3 ORIGIN FOR THE GROUP (A): -23.7944 -15.5954 -32.5710
REMARK 3 T TENSOR
REMARK 3 T11: 0.1276 T22: 0.1521
REMARK 3 T33: 0.1220 T12: 0.0116
REMARK 3 T13: -0.0075 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.7763 L22: 0.4191
REMARK 3 L33: 0.5499 L12: 0.5415
REMARK 3 L13: -0.0281 L23: 0.2169
REMARK 3 S TENSOR
REMARK 3 S11: -0.1482 S12: -0.0684 S13: 0.4333
REMARK 3 S21: -0.0987 S22: 0.0214 S23: 0.1574
REMARK 3 S31: -0.2103 S32: 0.0004 S33: -0.0313
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 4G9Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000073923.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : DOUBLE SILICON(111) CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17150
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
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 : 24.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 52.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 23.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4FHT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM CHLORIDE, 20% W/V PEG
REMARK 280 3350 , PH 6.3, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 51.38550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 51.38550
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.15300
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 51.38550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 25.07650
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 51.38550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 75.22950
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 51.38550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 75.22950
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.38550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 25.07650
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 51.38550
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 51.38550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 50.15300
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 51.38550
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 51.38550
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 50.15300
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 51.38550
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 75.22950
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 51.38550
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 25.07650
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 51.38550
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 25.07650
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 51.38550
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 75.22950
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 51.38550
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 51.38550
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 50.15300
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: 3740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -51.38550
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -75.22950
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 325 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 388 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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 VAL A 4
REMARK 465 ASP A 5
REMARK 465 LEU A 6
REMARK 465 ALA A 7
REMARK 465 ARG A 144
REMARK 465 ASN A 145
REMARK 465 PRO A 146
REMARK 465 ALA A 147
REMARK 465 GLU A 148
REMARK 465 PRO A 149
REMARK 465 ALA A 150
REMARK 465 VAL A 151
REMARK 465 ALA A 152
REMARK 465 PRO A 153
REMARK 465 GLY A 154
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 HIS A 9 71.66 71.60
REMARK 500 GLN A 86 -79.48 -71.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FHT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PCAV TRANSCRIPTIONAL REGULATOR FROM
REMARK 900 STREPTOMYCES COELICOLOR IN COMPLEX WITH ITS NATURAL LIGAND
DBREF 4G9Y A 1 154 UNP Q9XAM6 Q9XAM6_STRCO 1 154
SEQADV 4G9Y GLY A -2 UNP Q9XAM6 EXPRESSION TAG
SEQADV 4G9Y SER A -1 UNP Q9XAM6 EXPRESSION TAG
SEQADV 4G9Y HIS A 0 UNP Q9XAM6 EXPRESSION TAG
SEQRES 1 A 157 GLY SER HIS MET ALA ALA VAL ASP LEU ALA THR HIS PRO
SEQRES 2 A 157 GLY HIS LEU ALA ARG ARG LEU GLN GLN ALA HIS TYR LEU
SEQRES 3 A 157 LEU TRP ASN THR MET VAL SER GLU GLU THR THR SER PRO
SEQRES 4 A 157 GLN TYR ALA VAL LEU ASN ALA LEU VAL ALA GLU PRO GLY
SEQRES 5 A 157 LEU ASP GLN ARG THR VAL GLY GLU ARG VAL GLY LEU ASP
SEQRES 6 A 157 ARG SER THR ILE ALA GLU VAL VAL SER ARG LEU GLY ARG
SEQRES 7 A 157 ARG GLY LEU LEU ASP LYS VAL ARG ASP PRO GLN ASP GLY
SEQRES 8 A 157 ARG ARG SER LEU LEU ARG LEU THR ASP GLU GLY LEU ARG
SEQRES 9 A 157 VAL HIS ARG ARG LEU GLY VAL ARG ILE ALA ARG MET ASN
SEQRES 10 A 157 GLN VAL PHE LEU ALA PRO LEU ALA ALA ASP GLU GLN ALA
SEQRES 11 A 157 VAL PHE PHE ASP LEU ILE ARG ARG VAL ALA ASP ALA ALA
SEQRES 12 A 157 GLU GLY LEU ARG ASN PRO ALA GLU PRO ALA VAL ALA PRO
SEQRES 13 A 157 GLY
HET GOL A 201 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 HOH *132(H2 O)
HELIX 1 1 HIS A 9 VAL A 29 1 21
HELIX 2 2 THR A 34 GLU A 47 1 14
HELIX 3 3 GLN A 52 GLY A 60 1 9
HELIX 4 4 ASP A 62 ARG A 76 1 15
HELIX 5 5 THR A 96 ALA A 119 1 24
HELIX 6 6 ALA A 122 GLY A 142 1 21
SHEET 1 A 3 LEU A 50 ASP A 51 0
SHEET 2 A 3 SER A 91 LEU A 95 -1 O LEU A 93 N LEU A 50
SHEET 3 A 3 LEU A 79 ARG A 83 -1 N ASP A 80 O ARG A 94
SITE 1 AC1 3 LEU A 23 GLU A 141 LEU A 143
CRYST1 102.771 102.771 100.306 90.00 90.00 90.00 I 41 2 2 16
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 0.009730 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009730 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009969 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
