HEADER TRANSCRIPTION 10-NOV-14 4WWC
TITLE CRYSTAL STRUCTURE OF FULL LENGTH YVOA IN COMPLEX WITH PALINDROMIC
TITLE 2 OPERATOR DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HTH-TYPE TRANSCRIPTIONAL REPRESSOR YVOA;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: FULL LENGTH YVOA;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (5'-
COMPND 8 D(P*CP*AP*GP*TP*GP*GP*TP*CP*TP*AP*GP*AP*CP*CP*AP*CP*TP*GP*G)-3');
COMPND 9 CHAIN: E, F;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: 19 MER PALINDROMIC CONSTRUCT; DERIVED FROM THE
COMPND 12 CONSENSUS SEQUENCE OF THE TWO NATIVE NON-PALINDROMIC DRE-SITE
COMPND 13 SEQUENCES UPSTREAM OF NAGAB-YVOA AND NAGP
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 STRAIN: 168;
SOURCE 5 GENE: YVOA, BSU35030;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168;
SOURCE 11 ORGANISM_TAXID: 224308
KEYWDS TRANSCRIPTION, REPRESSOR, BACTERIAL TRANSCRIPTION REGULATION,
KEYWDS 2 TRANSCRIPTION FACTOR, GNTR/HUTC FAMILY, WINGED HELIX-TURN-HELIX
KEYWDS 3 MOTIF, N-ACETYLGLUCOSAMINE UTILIZATION, DNA-BINDING, OPERATOR-
KEYWDS 4 BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR F.C.GRAU,S.B.FILLENBERG,Y.A.MULLER
REVDAT 4 10-JAN-24 4WWC 1 REMARK
REVDAT 3 04-FEB-15 4WWC 1 JRNL
REVDAT 2 21-JAN-15 4WWC 1 JRNL
REVDAT 1 14-JAN-15 4WWC 0
JRNL AUTH S.B.FILLENBERG,F.C.GRAU,G.SEIDEL,Y.A.MULLER
JRNL TITL STRUCTURAL INSIGHT INTO OPERATOR DRE-SITES RECOGNITION AND
JRNL TITL 2 EFFECTOR BINDING IN THE GNTR/HUTC TRANSCRIPTION REGULATOR
JRNL TITL 3 NAGR.
JRNL REF NUCLEIC ACIDS RES. V. 43 1283 2015
JRNL REFN ESSN 1362-4962
JRNL PMID 25564531
JRNL DOI 10.1093/NAR/GKU1374
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 18031
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1442
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 34.2794 - 6.2440 1.00 1815 157 0.2047 0.2237
REMARK 3 2 6.2440 - 4.9609 1.00 1692 147 0.2187 0.2660
REMARK 3 3 4.9609 - 4.3352 1.00 1679 147 0.1975 0.2477
REMARK 3 4 4.3352 - 3.9394 1.00 1666 144 0.2305 0.2791
REMARK 3 5 3.9394 - 3.6574 1.00 1624 142 0.2379 0.3479
REMARK 3 6 3.6574 - 3.4420 1.00 1635 142 0.2513 0.3261
REMARK 3 7 3.4420 - 3.2698 1.00 1627 142 0.2628 0.2874
REMARK 3 8 3.2698 - 3.1275 1.00 1614 140 0.2993 0.3949
REMARK 3 9 3.1275 - 3.0072 1.00 1623 141 0.3199 0.4042
REMARK 3 10 3.0072 - 2.9035 1.00 1614 140 0.3415 0.4127
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) : 0.550
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.090
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 90.49
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 : 0.011 4497
REMARK 3 ANGLE : 1.466 6206
REMARK 3 CHIRALITY : 0.063 690
REMARK 3 PLANARITY : 0.007 664
REMARK 3 DIHEDRAL : 19.558 1772
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 4WWC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-NOV-14.
REMARK 100 THE DEPOSITION ID IS D_1000204624.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : SI-111 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18046
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.903
REMARK 200 RESOLUTION RANGE LOW (A) : 34.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.09891
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.7700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 1.97900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.990
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: DNA-BINDING AND EFFECTOR-BINDING DOMAINS OF YVOA
REMARK 200 (2WV0)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.5, 25 % (W/V) PEG
REMARK 280 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 119.98150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.98950
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.98950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 179.97225
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.98950
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.98950
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 59.99075
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.98950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.98950
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 179.97225
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.98950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.98950
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 59.99075
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
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 119.98150
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F
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 GLU A 80
REMARK 465 GLN A 81
REMARK 465 ALA A 82
REMARK 465 LEU A 83
REMARK 465 PRO A 125
REMARK 465 LEU A 153
REMARK 465 ALA A 154
REMARK 465 GLY A 155
REMARK 465 GLU A 156
REMARK 465 LEU A 157
REMARK 465 ASN A 158
REMARK 465 GLU A 159
REMARK 465 SER A 160
REMARK 465 HIS A 161
REMARK 465 PHE A 162
REMARK 465 GLN A 163
REMARK 465 SER A 164
REMARK 465 SER A 165
REMARK 465 ILE A 166
REMARK 465 TYR A 167
REMARK 465 ASP A 168
REMARK 465 HIS A 169
REMARK 465 ILE A 170
REMARK 465 GLU A 171
REMARK 465 ARG A 172
REMARK 465 TYR A 173
REMARK 465 ASN A 174
REMARK 465 SER A 175
REMARK 465 ILE A 176
REMARK 465 PRO A 177
REMARK 465 SER A 243
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 ALA B 82
REMARK 465 LEU B 83
REMARK 465 GLN B 84
REMARK 465 THR B 113
REMARK 465 HIS B 124
REMARK 465 HIS B 161
REMARK 465 PHE B 162
REMARK 465 GLN B 163
REMARK 465 SER B 164
REMARK 465 SER B 165
REMARK 465 ARG B 241
REMARK 465 LEU B 242
REMARK 465 SER B 243
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 GLN B 81 CG CD OE1 NE2
REMARK 470 DT E 17 C7
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 O2 DC E 1 N2 DG F 18 2.09
REMARK 500 OG SER B 112 O GLU B 114 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 DA E 2 O3' DA E 2 C3' -0.047
REMARK 500 DT E 7 O3' DT E 7 C3' -0.041
REMARK 500 DT E 17 O3' DT E 17 C3' -0.040
REMARK 500 DT F 4 O3' DT F 4 C3' -0.038
REMARK 500 DG F 6 O3' DG F 6 C3' -0.037
REMARK 500 DT F 7 O3' DT F 7 C3' -0.043
REMARK 500 DT F 17 O3' DT F 17 C3' -0.040
REMARK 500 DT F 17 C5 DT F 17 C7 -0.042
REMARK 500
REMARK 500 REMARK: NULL
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 DG E 19 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DT F 17 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DT F 17 C6 - C5 - C7 ANGL. DEV. = -4.3 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 LYS A 68 128.78 -39.78
REMARK 500 PRO A 77 169.72 -49.43
REMARK 500 LEU A 86 97.56 54.03
REMARK 500 LEU A 120 -160.94 53.02
REMARK 500 CYS A 122 133.83 35.13
REMARK 500 PHE A 151 -2.41 72.47
REMARK 500 SER A 179 -139.06 62.34
REMARK 500 ARG A 241 163.06 170.06
REMARK 500 LYS B 68 125.01 -38.81
REMARK 500 LYS B 76 97.48 -3.59
REMARK 500 ALA B 154 -14.40 -159.70
REMARK 500 PRO B 177 -159.95 -82.51
REMARK 500 SER B 179 -121.40 60.54
REMARK 500 HIS B 237 -56.38 -139.99
REMARK 500 TYR B 238 110.71 56.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER B 75 LYS B 76 137.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO E 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO E 102
DBREF 4WWC A 1 243 UNP O34817 YVOA_BACSU 1 243
DBREF 4WWC B 1 243 UNP O34817 YVOA_BACSU 1 243
DBREF 4WWC E 1 19 PDB 4WWC 4WWC 1 19
DBREF 4WWC F 1 19 PDB 4WWC 4WWC 1 19
SEQADV 4WWC GLY A -2 UNP O34817 EXPRESSION TAG
SEQADV 4WWC SER A -1 UNP O34817 EXPRESSION TAG
SEQADV 4WWC HIS A 0 UNP O34817 EXPRESSION TAG
SEQADV 4WWC GLY B -2 UNP O34817 EXPRESSION TAG
SEQADV 4WWC SER B -1 UNP O34817 EXPRESSION TAG
SEQADV 4WWC HIS B 0 UNP O34817 EXPRESSION TAG
SEQRES 1 A 246 GLY SER HIS MET ASN ILE ASN LYS GLN SER PRO ILE PRO
SEQRES 2 A 246 ILE TYR TYR GLN ILE MET GLU GLN LEU LYS THR GLN ILE
SEQRES 3 A 246 LYS ASN GLY GLU LEU GLN PRO ASP MET PRO LEU PRO SER
SEQRES 4 A 246 GLU ARG GLU TYR ALA GLU GLN PHE GLY ILE SER ARG MET
SEQRES 5 A 246 THR VAL ARG GLN ALA LEU SER ASN LEU VAL ASN GLU GLY
SEQRES 6 A 246 LEU LEU TYR ARG LEU LYS GLY ARG GLY THR PHE VAL SER
SEQRES 7 A 246 LYS PRO LYS MET GLU GLN ALA LEU GLN GLY LEU THR SER
SEQRES 8 A 246 PHE THR GLU ASP MET LYS SER ARG GLY MET THR PRO GLY
SEQRES 9 A 246 SER ARG LEU ILE ASP TYR GLN LEU ILE ASP SER THR GLU
SEQRES 10 A 246 GLU LEU ALA ALA ILE LEU GLY CYS GLY HIS PRO SER SER
SEQRES 11 A 246 ILE HIS LYS ILE THR ARG VAL ARG LEU ALA ASN ASP ILE
SEQRES 12 A 246 PRO MET ALA ILE GLU SER SER HIS ILE PRO PHE GLU LEU
SEQRES 13 A 246 ALA GLY GLU LEU ASN GLU SER HIS PHE GLN SER SER ILE
SEQRES 14 A 246 TYR ASP HIS ILE GLU ARG TYR ASN SER ILE PRO ILE SER
SEQRES 15 A 246 ARG ALA LYS GLN GLU LEU GLU PRO SER ALA ALA THR THR
SEQRES 16 A 246 GLU GLU ALA ASN ILE LEU GLY ILE GLN LYS GLY ALA PRO
SEQRES 17 A 246 VAL LEU LEU ILE LYS ARG THR THR TYR LEU GLN ASN GLY
SEQRES 18 A 246 THR ALA PHE GLU HIS ALA LYS SER VAL TYR ARG GLY ASP
SEQRES 19 A 246 ARG TYR THR PHE VAL HIS TYR MET ASP ARG LEU SER
SEQRES 1 B 246 GLY SER HIS MET ASN ILE ASN LYS GLN SER PRO ILE PRO
SEQRES 2 B 246 ILE TYR TYR GLN ILE MET GLU GLN LEU LYS THR GLN ILE
SEQRES 3 B 246 LYS ASN GLY GLU LEU GLN PRO ASP MET PRO LEU PRO SER
SEQRES 4 B 246 GLU ARG GLU TYR ALA GLU GLN PHE GLY ILE SER ARG MET
SEQRES 5 B 246 THR VAL ARG GLN ALA LEU SER ASN LEU VAL ASN GLU GLY
SEQRES 6 B 246 LEU LEU TYR ARG LEU LYS GLY ARG GLY THR PHE VAL SER
SEQRES 7 B 246 LYS PRO LYS MET GLU GLN ALA LEU GLN GLY LEU THR SER
SEQRES 8 B 246 PHE THR GLU ASP MET LYS SER ARG GLY MET THR PRO GLY
SEQRES 9 B 246 SER ARG LEU ILE ASP TYR GLN LEU ILE ASP SER THR GLU
SEQRES 10 B 246 GLU LEU ALA ALA ILE LEU GLY CYS GLY HIS PRO SER SER
SEQRES 11 B 246 ILE HIS LYS ILE THR ARG VAL ARG LEU ALA ASN ASP ILE
SEQRES 12 B 246 PRO MET ALA ILE GLU SER SER HIS ILE PRO PHE GLU LEU
SEQRES 13 B 246 ALA GLY GLU LEU ASN GLU SER HIS PHE GLN SER SER ILE
SEQRES 14 B 246 TYR ASP HIS ILE GLU ARG TYR ASN SER ILE PRO ILE SER
SEQRES 15 B 246 ARG ALA LYS GLN GLU LEU GLU PRO SER ALA ALA THR THR
SEQRES 16 B 246 GLU GLU ALA ASN ILE LEU GLY ILE GLN LYS GLY ALA PRO
SEQRES 17 B 246 VAL LEU LEU ILE LYS ARG THR THR TYR LEU GLN ASN GLY
SEQRES 18 B 246 THR ALA PHE GLU HIS ALA LYS SER VAL TYR ARG GLY ASP
SEQRES 19 B 246 ARG TYR THR PHE VAL HIS TYR MET ASP ARG LEU SER
SEQRES 1 E 19 DC DA DG DT DG DG DT DC DT DA DG DA DC
SEQRES 2 E 19 DC DA DC DT DG DG
SEQRES 1 F 19 DC DA DG DT DG DG DT DC DT DA DG DA DC
SEQRES 2 F 19 DC DA DC DT DG DG
HET EDO A 301 4
HET EDO B 301 4
HET EDO B 302 4
HET EDO B 303 4
HET EDO B 304 4
HET EDO E 101 4
HET EDO E 102 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 EDO 7(C2 H6 O2)
FORMUL 12 HOH *2(H2 O)
HELIX 1 AA1 PRO A 10 ASN A 25 1 16
HELIX 2 AA2 SER A 36 GLY A 45 1 10
HELIX 3 AA3 SER A 47 ASN A 60 1 14
HELIX 4 AA4 SER A 88 SER A 95 1 8
HELIX 5 AA5 THR A 113 ILE A 119 1 7
HELIX 6 AA6 THR A 191 GLY A 199 1 9
HELIX 7 AA7 PRO B 10 ASN B 25 1 16
HELIX 8 AA8 SER B 36 GLY B 45 1 10
HELIX 9 AA9 SER B 47 GLU B 61 1 15
HELIX 10 AB1 SER B 88 SER B 95 1 8
HELIX 11 AB2 GLU B 115 ILE B 119 1 5
HELIX 12 AB3 ASP B 168 ASN B 174 1 7
HELIX 13 AB4 THR B 191 GLY B 199 1 9
SHEET 1 AA1 2 LEU A 64 LEU A 67 0
SHEET 2 AA1 2 GLY A 71 VAL A 74 -1 O PHE A 73 N TYR A 65
SHEET 1 AA2 3 PRO A 100 ASP A 106 0
SHEET 2 AA2 3 ILE A 128 ALA A 137 -1 O LEU A 136 N GLY A 101
SHEET 3 AA2 3 LEU A 109 ILE A 110 -1 N ILE A 110 O ILE A 128
SHEET 1 AA3 7 PRO A 100 ASP A 106 0
SHEET 2 AA3 7 ILE A 128 ALA A 137 -1 O LEU A 136 N GLY A 101
SHEET 3 AA3 7 ILE A 140 ILE A 149 -1 O ILE A 149 N HIS A 129
SHEET 4 AA3 7 ALA A 220 ARG A 229 -1 O LYS A 225 N SER A 146
SHEET 5 AA3 7 PRO A 205 TYR A 214 -1 N THR A 213 O PHE A 221
SHEET 6 AA3 7 ALA A 181 ALA A 189 -1 N LYS A 182 O THR A 212
SHEET 7 AA3 7 PHE B 235 VAL B 236 -1 O PHE B 235 N LEU A 185
SHEET 1 AA4 7 PHE A 235 MET A 239 0
SHEET 2 AA4 7 ALA B 181 ALA B 189 -1 O ALA B 181 N MET A 239
SHEET 3 AA4 7 PRO B 205 TYR B 214 -1 O LEU B 208 N GLU B 186
SHEET 4 AA4 7 ALA B 220 ARG B 229 -1 O ALA B 224 N ARG B 211
SHEET 5 AA4 7 ILE B 140 PRO B 150 -1 N ILE B 144 O VAL B 227
SHEET 6 AA4 7 ILE B 128 ALA B 137 -1 N HIS B 129 O ILE B 149
SHEET 7 AA4 7 PRO B 100 ILE B 110 -1 N ARG B 103 O VAL B 134
SHEET 1 AA5 2 LEU B 64 LEU B 67 0
SHEET 2 AA5 2 GLY B 71 VAL B 74 -1 O PHE B 73 N TYR B 65
SITE 1 AC1 2 MET A 49 MET B 49
SITE 1 AC2 7 THR B 87 SER B 88 ASP B 92 GLN B 183
SITE 2 AC2 7 ARG B 211 TYR B 228 TYR B 233
SITE 1 AC3 5 GLN A 53 MET B 49 ARG B 52 DT E 7
SITE 2 AC3 5 DC E 8
SITE 1 AC4 1 THR B 132
SITE 1 AC5 4 TYR B 167 THR B 213 PHE B 221 GLU B 222
SITE 1 AC6 2 DC E 13 DT F 7
SITE 1 AC7 4 DG E 5 DG E 6 DC F 14 DA F 15
CRYST1 79.979 79.979 239.963 90.00 90.00 90.00 P 43 21 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 0.012503 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012503 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004167 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
