HEADER TRANSCRIPTION/TRANSFERASE/DNA 03-SEP-10 3OQO
TITLE CCPA-HPR-SER46P-SYN CRE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATABOLITE CONTROL PROTEIN A;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: GLUCOSE-RESISTANCE AMYLASE REGULATOR;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PHOSPHOCARRIER PROTEIN HPR;
COMPND 8 CHAIN: S, D;
COMPND 9 SYNONYM: HISTIDINE-CONTAINING PROTEIN;
COMPND 10 EC: 2.7.11.-;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: 5'-D(*CP*TP*GP*TP*TP*AP*GP*CP*GP*CP*TP*TP*TP*CP*AP*G)-3';
COMPND 14 CHAIN: E;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: 5'-D(*CP*TP*GP*AP*AP*AP*GP*CP*GP*CP*TP*AP*AP*CP*AP*G)-3';
COMPND 18 CHAIN: B;
COMPND 19 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: ALSA, AMYR, BSU29740, CCPA, GRAR;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 9 ORGANISM_TAXID: 1423;
SOURCE 10 GENE: BSU13900, HPR, PTSH;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES;
SOURCE 15 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 16 ORGANISM_TAXID: 1423;
SOURCE 17 MOL_ID: 4;
SOURCE 18 SYNTHETIC: YES;
SOURCE 19 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 20 ORGANISM_TAXID: 1423
KEYWDS PBP FOLD FOR CCPA, TRANSCRIPTION, HPR-SER46P, CRE DNA, NUCLEOID,
KEYWDS 2 TRANSCRIPTION-TRANSFERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.SCHUMACHER,M.SPREHE,M.BARTHOLOMAE,W.HILLEN,R.G.BRENNAN
REVDAT 2 09-APR-14 3OQO 1 JRNL
REVDAT 1 26-OCT-11 3OQO 0
JRNL AUTH M.A.SCHUMACHER,M.SPREHE,M.BARTHOLOMAE,W.HILLEN,R.G.BRENNAN
JRNL TITL STRUCTURES OF CARBON CATABOLITE PROTEIN A-(HPR-SER46-P)
JRNL TITL 2 BOUND TO DIVERSE CATABOLITE RESPONSE ELEMENT SITES REVEAL
JRNL TITL 3 THE BASIS FOR HIGH-AFFINITY BINDING TO DEGENERATE DNA
JRNL TITL 4 OPERATORS.
JRNL REF NUCLEIC ACIDS RES. V. 39 2931 2011
JRNL REFN ISSN 0305-1048
JRNL PMID 21106498
JRNL DOI 10.1093/NAR/GKQ1177
REMARK 2
REMARK 2 RESOLUTION. 2.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1865585.120
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 28497
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 SET) : 0.212
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1959
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.97
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.15
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3978
REMARK 3 BIN R VALUE (WORKING SET) : 0.3440
REMARK 3 BIN FREE R VALUE : 0.3910
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 302
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.023
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6437
REMARK 3 NUCLEIC ACID ATOMS : 650
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 48
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 250.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 86.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.84000
REMARK 3 B22 (A**2) : -2.00000
REMARK 3 B33 (A**2) : 11.85000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.39
REMARK 3 ESD FROM SIGMAA (A) : 0.56
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.49
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.62
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.800
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.940
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.600 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.710 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.760 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.260 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 55.40
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP-NEWSEP.PARAM.TXT
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN-NEWSEP.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3OQO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-10.
REMARK 100 THE RCSB ID CODE IS RCSB061452.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
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 : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28585
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.970
REMARK 200 RESOLUTION RANGE LOW (A) : 105.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 2.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.04
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 37.07500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 86.86500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.60500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 86.86500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.07500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.60500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -138.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, S, E, 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 HIS A 335
REMARK 465 HIS A 336
REMARK 465 HIS A 337
REMARK 465 HIS A 338
REMARK 465 HIS A 339
REMARK 465 HIS A 340
REMARK 465 ALA C 334
REMARK 465 HIS C 335
REMARK 465 HIS C 336
REMARK 465 HIS C 337
REMARK 465 HIS C 338
REMARK 465 HIS C 339
REMARK 465 HIS C 340
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 ILE A 4 89.90 32.50
REMARK 500 ASN A 29 73.04 -56.51
REMARK 500 VAL A 30 111.42 -166.15
REMARK 500 GLN A 101 9.67 57.24
REMARK 500 GLU A 106 -74.69 -58.40
REMARK 500 ARG A 138 48.94 -100.19
REMARK 500 GLU A 153 60.41 35.19
REMARK 500 ALA A 159 -168.95 -177.95
REMARK 500 ASP A 175 18.23 -61.73
REMARK 500 LYS A 196 -74.53 -107.06
REMARK 500 ASP A 221 39.48 -140.09
REMARK 500 TYR A 222 -10.62 65.46
REMARK 500 ILE A 256 -72.00 -45.08
REMARK 500 GLN A 262 31.90 -80.59
REMARK 500 ASP A 276 -49.17 118.14
REMARK 500 ASN A 277 42.80 72.98
REMARK 500 GLU A 317 109.01 66.32
REMARK 500 ARG A 329 -139.77 -121.83
REMARK 500 GLN S 3 159.34 176.57
REMARK 500 LYS S 4 139.81 168.21
REMARK 500 ALA S 16 -154.72 53.93
REMARK 500 ASN S 38 78.43 -6.76
REMARK 500 ALA S 68 -79.15 -59.54
REMARK 500 ASP S 69 9.71 -64.96
REMARK 500 ALA S 73 -70.36 -68.80
REMARK 500 MET S 81 -33.62 -39.80
REMARK 500 LEU S 86 -66.50 -95.89
REMARK 500 ASN C 3 179.58 -54.78
REMARK 500 GLU C 12 19.76 -63.32
REMARK 500 ALA C 13 1.53 -158.44
REMARK 500 ASN C 29 62.99 -65.15
REMARK 500 ASP C 70 97.22 -161.00
REMARK 500 ILE C 71 -6.87 -56.38
REMARK 500 LYS C 116 5.08 -69.39
REMARK 500 GLU C 154 -43.19 -130.84
REMARK 500 VAL C 158 86.21 -155.05
REMARK 500 ALA C 159 -144.78 -133.88
REMARK 500 ASP C 175 -1.55 -59.39
REMARK 500 ILE C 192 -33.38 -38.33
REMARK 500 ARG C 194 -71.74 -63.31
REMARK 500 SER C 195 24.84 -75.86
REMARK 500 LYS C 196 -59.45 -153.85
REMARK 500 GLN C 215 3.86 -69.14
REMARK 500 ASP C 221 44.47 -157.57
REMARK 500 TYR C 222 7.98 55.82
REMARK 500 SER C 236 -80.50 -55.74
REMARK 500 LEU C 237 163.71 -48.22
REMARK 500 LYS C 239 90.44 -63.37
REMARK 500 LEU C 264 146.33 -39.90
REMARK 500 ASP C 276 -33.52 157.18
REMARK 500
REMARK 500 THIS ENTRY HAS 68 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 DC B 700 0.07 SIDE CHAIN
REMARK 500 DC B 713 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 342 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH A 347 DISTANCE = 5.57 ANGSTROMS
REMARK 525 HOH A 352 DISTANCE = 5.29 ANGSTROMS
REMARK 525 HOH A 361 DISTANCE = 5.57 ANGSTROMS
REMARK 525 HOH C 345 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH S 135 DISTANCE = 5.01 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 399
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 599
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 699
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 999
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OQM RELATED DB: PDB
REMARK 900 CCPA-HPRSER46P-ACKA2 CRE
REMARK 900 RELATED ID: 3OQN RELATED DB: PDB
REMARK 900 CCPA-HPRSER46P-GNTR-DOWN CRE
DBREF 3OQO A 2 334 UNP P25144 CCPA_BACSU 1 333
DBREF 3OQO S 2 88 UNP P08877 PTHP_BACSU 2 88
DBREF 3OQO C 2 334 UNP P25144 CCPA_BACSU 1 333
DBREF 3OQO D 2 88 UNP P08877 PTHP_BACSU 2 88
DBREF 3OQO E 700 715 PDB 3OQO 3OQO 700 715
DBREF 3OQO B 700 715 PDB 3OQO 3OQO 700 715
SEQADV 3OQO HIS A 335 UNP P25144 EXPRESSION TAG
SEQADV 3OQO HIS A 336 UNP P25144 EXPRESSION TAG
SEQADV 3OQO HIS A 337 UNP P25144 EXPRESSION TAG
SEQADV 3OQO HIS A 338 UNP P25144 EXPRESSION TAG
SEQADV 3OQO HIS A 339 UNP P25144 EXPRESSION TAG
SEQADV 3OQO HIS A 340 UNP P25144 EXPRESSION TAG
SEQADV 3OQO HIS C 335 UNP P25144 EXPRESSION TAG
SEQADV 3OQO HIS C 336 UNP P25144 EXPRESSION TAG
SEQADV 3OQO HIS C 337 UNP P25144 EXPRESSION TAG
SEQADV 3OQO HIS C 338 UNP P25144 EXPRESSION TAG
SEQADV 3OQO HIS C 339 UNP P25144 EXPRESSION TAG
SEQADV 3OQO HIS C 340 UNP P25144 EXPRESSION TAG
SEQRES 1 A 339 MET ASN ILE THR ILE TYR ASP VAL ALA ARG GLU ALA ASN
SEQRES 2 A 339 VAL SER MET ALA THR VAL SER ARG VAL VAL ASN GLY ASN
SEQRES 3 A 339 PRO ASN VAL LYS PRO THR THR ARG LYS LYS VAL LEU GLU
SEQRES 4 A 339 ALA ILE GLU ARG LEU GLY TYR ARG PRO ASN ALA VAL ALA
SEQRES 5 A 339 ARG GLY LEU ALA SER LYS LYS THR THR THR VAL GLY VAL
SEQRES 6 A 339 ILE ILE PRO ASP ILE SER SER ILE PHE TYR SER GLU LEU
SEQRES 7 A 339 ALA ARG GLY ILE GLU ASP ILE ALA THR MET TYR LYS TYR
SEQRES 8 A 339 ASN ILE ILE LEU SER ASN SER ASP GLN ASN MET GLU LYS
SEQRES 9 A 339 GLU LEU HIS LEU LEU ASN THR MET LEU GLY LYS GLN VAL
SEQRES 10 A 339 ASP GLY ILE VAL PHE MET GLY GLY ASN ILE THR ASP GLU
SEQRES 11 A 339 HIS VAL ALA GLU PHE LYS ARG SER PRO VAL PRO ILE VAL
SEQRES 12 A 339 LEU ALA ALA SER VAL GLU GLU GLN GLU GLU THR PRO SER
SEQRES 13 A 339 VAL ALA ILE ASP TYR GLU GLN ALA ILE TYR ASP ALA VAL
SEQRES 14 A 339 LYS LEU LEU VAL ASP LYS GLY HIS THR ASP ILE ALA PHE
SEQRES 15 A 339 VAL SER GLY PRO MET ALA GLU PRO ILE ASN ARG SER LYS
SEQRES 16 A 339 LYS LEU GLN GLY TYR LYS ARG ALA LEU GLU GLU ALA ASN
SEQRES 17 A 339 LEU PRO PHE ASN GLU GLN PHE VAL ALA GLU GLY ASP TYR
SEQRES 18 A 339 THR TYR ASP SER GLY LEU GLU ALA LEU GLN HIS LEU MET
SEQRES 19 A 339 SER LEU ASP LYS LYS PRO THR ALA ILE LEU SER ALA THR
SEQRES 20 A 339 ASP GLU MET ALA LEU GLY ILE ILE HIS ALA ALA GLN ASP
SEQRES 21 A 339 GLN GLY LEU SER ILE PRO GLU ASP LEU ASP ILE ILE GLY
SEQRES 22 A 339 PHE ASP ASN THR ARG LEU SER LEU MET VAL ARG PRO GLN
SEQRES 23 A 339 LEU SER THR VAL VAL GLN PRO THR TYR ASP ILE GLY ALA
SEQRES 24 A 339 VAL ALA MET ARG LEU LEU THR LYS LEU MET ASN LYS GLU
SEQRES 25 A 339 PRO VAL GLU GLU HIS ILE VAL GLU LEU PRO HIS ARG ILE
SEQRES 26 A 339 GLU LEU ARG LYS SER THR LYS ALA HIS HIS HIS HIS HIS
SEQRES 27 A 339 HIS
SEQRES 1 S 87 ALA GLN LYS THR PHE LYS VAL THR ALA ASP SER GLY ILE
SEQRES 2 S 87 HIS ALA ARG PRO ALA THR VAL LEU VAL GLN THR ALA SER
SEQRES 3 S 87 LYS TYR ASP ALA ASP VAL ASN LEU GLU TYR ASN GLY LYS
SEQRES 4 S 87 THR VAL ASN LEU LYS SEP ILE MET GLY VAL MET SER LEU
SEQRES 5 S 87 GLY ILE ALA LYS GLY ALA GLU ILE THR ILE SER ALA SER
SEQRES 6 S 87 GLY ALA ASP GLU ASN ASP ALA LEU ASN ALA LEU GLU GLU
SEQRES 7 S 87 THR MET LYS SER GLU GLY LEU GLY GLU
SEQRES 1 C 339 MET ASN ILE THR ILE TYR ASP VAL ALA ARG GLU ALA ASN
SEQRES 2 C 339 VAL SER MET ALA THR VAL SER ARG VAL VAL ASN GLY ASN
SEQRES 3 C 339 PRO ASN VAL LYS PRO THR THR ARG LYS LYS VAL LEU GLU
SEQRES 4 C 339 ALA ILE GLU ARG LEU GLY TYR ARG PRO ASN ALA VAL ALA
SEQRES 5 C 339 ARG GLY LEU ALA SER LYS LYS THR THR THR VAL GLY VAL
SEQRES 6 C 339 ILE ILE PRO ASP ILE SER SER ILE PHE TYR SER GLU LEU
SEQRES 7 C 339 ALA ARG GLY ILE GLU ASP ILE ALA THR MET TYR LYS TYR
SEQRES 8 C 339 ASN ILE ILE LEU SER ASN SER ASP GLN ASN MET GLU LYS
SEQRES 9 C 339 GLU LEU HIS LEU LEU ASN THR MET LEU GLY LYS GLN VAL
SEQRES 10 C 339 ASP GLY ILE VAL PHE MET GLY GLY ASN ILE THR ASP GLU
SEQRES 11 C 339 HIS VAL ALA GLU PHE LYS ARG SER PRO VAL PRO ILE VAL
SEQRES 12 C 339 LEU ALA ALA SER VAL GLU GLU GLN GLU GLU THR PRO SER
SEQRES 13 C 339 VAL ALA ILE ASP TYR GLU GLN ALA ILE TYR ASP ALA VAL
SEQRES 14 C 339 LYS LEU LEU VAL ASP LYS GLY HIS THR ASP ILE ALA PHE
SEQRES 15 C 339 VAL SER GLY PRO MET ALA GLU PRO ILE ASN ARG SER LYS
SEQRES 16 C 339 LYS LEU GLN GLY TYR LYS ARG ALA LEU GLU GLU ALA ASN
SEQRES 17 C 339 LEU PRO PHE ASN GLU GLN PHE VAL ALA GLU GLY ASP TYR
SEQRES 18 C 339 THR TYR ASP SER GLY LEU GLU ALA LEU GLN HIS LEU MET
SEQRES 19 C 339 SER LEU ASP LYS LYS PRO THR ALA ILE LEU SER ALA THR
SEQRES 20 C 339 ASP GLU MET ALA LEU GLY ILE ILE HIS ALA ALA GLN ASP
SEQRES 21 C 339 GLN GLY LEU SER ILE PRO GLU ASP LEU ASP ILE ILE GLY
SEQRES 22 C 339 PHE ASP ASN THR ARG LEU SER LEU MET VAL ARG PRO GLN
SEQRES 23 C 339 LEU SER THR VAL VAL GLN PRO THR TYR ASP ILE GLY ALA
SEQRES 24 C 339 VAL ALA MET ARG LEU LEU THR LYS LEU MET ASN LYS GLU
SEQRES 25 C 339 PRO VAL GLU GLU HIS ILE VAL GLU LEU PRO HIS ARG ILE
SEQRES 26 C 339 GLU LEU ARG LYS SER THR LYS ALA HIS HIS HIS HIS HIS
SEQRES 27 C 339 HIS
SEQRES 1 D 87 ALA GLN LYS THR PHE LYS VAL THR ALA ASP SER GLY ILE
SEQRES 2 D 87 HIS ALA ARG PRO ALA THR VAL LEU VAL GLN THR ALA SER
SEQRES 3 D 87 LYS TYR ASP ALA ASP VAL ASN LEU GLU TYR ASN GLY LYS
SEQRES 4 D 87 THR VAL ASN LEU LYS SEP ILE MET GLY VAL MET SER LEU
SEQRES 5 D 87 GLY ILE ALA LYS GLY ALA GLU ILE THR ILE SER ALA SER
SEQRES 6 D 87 GLY ALA ASP GLU ASN ASP ALA LEU ASN ALA LEU GLU GLU
SEQRES 7 D 87 THR MET LYS SER GLU GLY LEU GLY GLU
SEQRES 1 E 16 DC DT DG DT DT DA DG DC DG DC DT DT DT
SEQRES 2 E 16 DC DA DG
SEQRES 1 B 16 DC DT DG DA DA DA DG DC DG DC DT DA DA
SEQRES 2 B 16 DC DA DG
MODRES 3OQO SEP S 46 SER PHOSPHOSERINE
MODRES 3OQO SEP D 46 SER PHOSPHOSERINE
HET SEP S 46 10
HET SEP D 46 10
HET SO4 A 499 5
HET SO4 A 399 5
HET SO4 C 599 5
HET SO4 C 699 5
HET SO4 C 999 5
HETNAM SEP PHOSPHOSERINE
HETNAM SO4 SULFATE ION
HETSYN SEP PHOSPHONOSERINE
FORMUL 2 SEP 2(C3 H8 N O6 P)
FORMUL 7 SO4 5(O4 S 2-)
FORMUL 12 HOH *48(H2 O)
HELIX 1 1 THR A 5 ALA A 13 1 9
HELIX 2 2 SER A 16 ASN A 25 1 10
HELIX 3 3 LYS A 31 GLY A 46 1 16
HELIX 4 4 ASN A 50 LYS A 59 1 10
HELIX 5 5 SER A 73 TYR A 90 1 18
HELIX 6 6 ASN A 102 LYS A 116 1 15
HELIX 7 7 THR A 129 ARG A 138 1 10
HELIX 8 8 ASP A 161 ASP A 175 1 15
HELIX 9 9 GLU A 190 SER A 195 1 6
HELIX 10 10 LYS A 196 ALA A 208 1 13
HELIX 11 11 ASN A 213 GLN A 215 5 3
HELIX 12 12 THR A 223 MET A 235 1 13
HELIX 13 13 THR A 248 GLN A 262 1 15
HELIX 14 14 THR A 278 VAL A 284 5 7
HELIX 15 15 PRO A 294 ASN A 311 1 18
HELIX 16 16 HIS S 15 LYS S 28 1 14
HELIX 17 17 SEP S 46 SER S 52 1 7
HELIX 18 18 ASP S 69 GLU S 84 1 16
HELIX 19 19 THR C 5 GLU C 12 1 8
HELIX 20 20 SER C 16 ASN C 25 1 10
HELIX 21 21 LYS C 31 GLY C 46 1 16
HELIX 22 22 ASN C 50 LYS C 59 1 10
HELIX 23 23 SER C 73 TYR C 90 1 18
HELIX 24 24 ASN C 102 LYS C 116 1 15
HELIX 25 25 THR C 129 LYS C 137 1 9
HELIX 26 26 ASP C 161 ASP C 175 1 15
HELIX 27 27 GLU C 190 SER C 195 1 6
HELIX 28 28 LYS C 196 GLU C 207 1 12
HELIX 29 29 ASN C 213 GLN C 215 5 3
HELIX 30 30 THR C 223 LEU C 237 1 15
HELIX 31 31 THR C 248 ASP C 261 1 14
HELIX 32 32 THR C 278 MET C 283 5 6
HELIX 33 33 PRO C 294 ASN C 311 1 18
HELIX 34 34 HIS D 15 ALA D 26 1 12
HELIX 35 35 SEP D 46 GLY D 54 1 9
HELIX 36 36 ASP D 69 GLU D 84 1 16
SHEET 1 A12 ILE A 319 GLU A 321 0
SHEET 2 A12 SER A 157 ALA A 159 1 N SER A 157 O VAL A 320
SHEET 3 A12 ILE A 143 ALA A 146 1 N LEU A 145 O VAL A 158
SHEET 4 A12 GLY A 120 PHE A 123 1 N PHE A 123 O VAL A 144
SHEET 5 A12 THR A 63 ILE A 68 1 N GLY A 65 O GLY A 120
SHEET 6 A12 ASN A 93 ASN A 98 1 O ILE A 95 N VAL A 66
SHEET 7 A12 ASN C 93 ASN C 98 -1 O ILE C 94 N LEU A 96
SHEET 8 A12 THR C 63 ILE C 68 1 N VAL C 64 O ASN C 93
SHEET 9 A12 GLY C 120 PHE C 123 1 O GLY C 120 N GLY C 65
SHEET 10 A12 ILE C 143 ALA C 146 1 O VAL C 144 N PHE C 123
SHEET 11 A12 SER C 157 ALA C 159 1 O VAL C 158 N LEU C 145
SHEET 12 A12 VAL C 320 GLU C 321 1 O VAL C 320 N SER C 157
SHEET 1 B 6 VAL A 217 GLU A 219 0
SHEET 2 B 6 ILE A 181 SER A 185 1 N SER A 185 O ALA A 218
SHEET 3 B 6 ALA A 243 SER A 246 1 O LEU A 245 N ALA A 182
SHEET 4 B 6 ASP A 271 ASP A 276 1 O ASP A 271 N ILE A 244
SHEET 5 B 6 SER A 289 VAL A 292 1 O SER A 289 N GLY A 274
SHEET 6 B 6 ARG A 325 GLU A 327 -1 O ARG A 325 N VAL A 292
SHEET 1 C 4 THR S 5 LYS S 7 0
SHEET 2 C 4 GLU S 60 SER S 66 -1 O ILE S 61 N PHE S 6
SHEET 3 C 4 ASP S 32 TYR S 37 -1 N GLU S 36 O THR S 62
SHEET 4 C 4 THR S 41 VAL S 42 -1 O VAL S 42 N LEU S 35
SHEET 1 D 6 VAL C 217 GLU C 219 0
SHEET 2 D 6 ILE C 181 SER C 185 1 N PHE C 183 O ALA C 218
SHEET 3 D 6 ALA C 243 SER C 246 1 O LEU C 245 N VAL C 184
SHEET 4 D 6 ASP C 271 ASP C 276 1 O ASP C 271 N ILE C 244
SHEET 5 D 6 SER C 289 VAL C 292 1 O SER C 289 N GLY C 274
SHEET 6 D 6 ARG C 325 GLU C 327 -1 O ARG C 325 N VAL C 292
SHEET 1 E 4 THR D 5 LYS D 7 0
SHEET 2 E 4 GLU D 60 ILE D 63 -1 O ILE D 61 N PHE D 6
SHEET 3 E 4 ASN D 34 TYR D 37 -1 N GLU D 36 O THR D 62
SHEET 4 E 4 LYS D 40 ASN D 43 -1 O LYS D 40 N TYR D 37
LINK C LYS S 45 N SEP S 46 1555 1555 1.33
LINK C SEP S 46 N ILE S 47 1555 1555 1.33
LINK C LYS D 45 N SEP D 46 1555 1555 1.33
LINK C SEP D 46 N ILE D 47 1555 1555 1.33
CISPEP 1 ILE A 266 PRO A 267 0 -0.03
CISPEP 2 ARG A 285 PRO A 286 0 0.27
CISPEP 3 ILE C 266 PRO C 267 0 -0.42
CISPEP 4 ARG C 285 PRO C 286 0 -0.02
SITE 1 AC1 4 TYR A 90 ARG A 304 ASN A 311 GLU A 313
SITE 1 AC2 1 TYR A 90
SITE 1 AC3 5 TYR C 90 ARG C 304 THR C 307 ASN C 311
SITE 2 AC3 5 GLU C 313
SITE 1 AC4 1 MET C 89
SITE 1 AC5 2 ASP C 85 ARG D 17
CRYST1 74.150 105.210 173.730 90.00 90.00 90.00 P 21 21 21 8
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 0.013486 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009505 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005756 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
