HEADER TRANSCRIPTION 27-FEB-06 2CG4
TITLE STRUCTURE OF E.COLI ASNC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REGULATORY PROTEIN ASNC;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: B834(DE3);
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834(DE3)
KEYWDS ASNC, DNA BINDING, FFRP, LRP FAMILY, TRANSCRIPTION, DNA-BINDING,
KEYWDS 2 TRANSCRIPTION REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR P.THAW,S.E.SEDELNIKOVA,T.MURANOVA,S.WIESE,S.AYORA,J.C.ALONSO,
AUTHOR 2 A.B.BRINKMAN,J.AKERBOOM,J.VAN DER OOST,J.B.RAFFERTY
REVDAT 3 28-APR-21 2CG4 1 REMARK LINK
REVDAT 2 24-FEB-09 2CG4 1 VERSN
REVDAT 1 04-APR-06 2CG4 0
JRNL AUTH P.THAW,S.E.SEDELNIKOVA,T.MURANOVA,S.WIESE,S.AYORA,
JRNL AUTH 2 J.C.ALONSO,A.B.BRINKMAN,J.AKERBOOM,J.VAN DER OOST,
JRNL AUTH 3 J.B.RAFFERTY
JRNL TITL STRUCTURAL INSIGHT INTO GENE TRANSCRIPTIONAL REGULATION AND
JRNL TITL 2 EFFECTOR BINDING BY THE LRP/ASNC FAMILY.
JRNL REF NUCLEIC ACIDS RES. V. 34 1439 2006
JRNL REFN ISSN 0305-1048
JRNL PMID 16528101
JRNL DOI 10.1093/NAR/GKL009
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 20542
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) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1103
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1531
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3120
REMARK 3 BIN FREE R VALUE SET COUNT : 77
REMARK 3 BIN FREE R VALUE : 0.4290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2300
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 135
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.75000
REMARK 3 B22 (A**2) : -1.75000
REMARK 3 B33 (A**2) : 3.49000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.269
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.249
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.197
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.448
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.879
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2350 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3180 ; 0.971 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 296 ; 8.617 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 94 ;41.200 ;24.681
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 428 ;21.493 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;17.901 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 382 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1706 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1108 ; 0.264 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1599 ; 0.320 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 154 ; 0.181 ; 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): 69 ; 0.338 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.247 ; 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): 1513 ; 1.030 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2410 ; 1.869 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 908 ; 2.829 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 770 ; 4.555 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 70 A 150 4
REMARK 3 1 B 70 B 150 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 642 ; 0.12 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 642 ; 0.72 ; 2.00
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2CG4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1290027977.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.70
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.488
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21843
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.69000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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: LOW RES ASNC FROM SELENO MET EXPERIMENT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2M MAGNESIUM CHLORIDE, O.1M BICINE
REMARK 280 PH 8.7, 5MM L-ASPARAGINE, PH 8.70
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PQS
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 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLY 37 TO GLU
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLY 37 TO GLU
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 MET A 1
REMARK 465 GLU A 2
REMARK 465 ASN A 3
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ASN B 3
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 LEU A 5 CG CD1 CD2
REMARK 470 VAL A 34 CG1 CG2
REMARK 470 GLN A 48 CG CD OE1 NE2
REMARK 470 LYS A 151 CG CD CE NZ
REMARK 470 LEU B 5 CG CD1 CD2
REMARK 470 VAL B 34 CG1 CG2
REMARK 470 GLN B 48 CG CD OE1 NE2
REMARK 470 LYS B 151 CG CD CE NZ
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 THR A 101 C THR A 102 N 0.189
REMARK 500 THR A 102 C GLY A 103 N -0.376
REMARK 500 THR B 101 C THR B 102 N 0.149
REMARK 500 THR B 102 C GLY B 103 N -0.276
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 THR A 101 O - C - N ANGL. DEV. = -11.6 DEGREES
REMARK 500 THR B 101 O - C - N ANGL. DEV. = -10.1 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 PRO A 36 -19.16 -46.28
REMARK 500 ARG A 148 -151.11 -153.13
REMARK 500 PRO B 36 -19.97 -39.44
REMARK 500 ARG B 148 -161.42 -160.85
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 A1154 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 58 OD2
REMARK 620 2 ASP B 58 OD2 171.9
REMARK 620 N 1
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASN A1153
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASN B1153
DBREF 2CG4 A 1 152 UNP P0ACI6 ASNC_ECOLI 1 152
DBREF 2CG4 B 1 152 UNP P0ACI6 ASNC_ECOLI 1 152
SEQADV 2CG4 GLU A 37 UNP P0ACI6 GLY 37 ENGINEERED MUTATION
SEQADV 2CG4 GLU B 37 UNP P0ACI6 GLY 37 ENGINEERED MUTATION
SEQRES 1 A 152 MET GLU ASN TYR LEU ILE ASP ASN LEU ASP ARG GLY ILE
SEQRES 2 A 152 LEU GLU ALA LEU MET GLY ASN ALA ARG THR ALA TYR ALA
SEQRES 3 A 152 GLU LEU ALA LYS GLN PHE GLY VAL SER PRO GLU THR ILE
SEQRES 4 A 152 HIS VAL ARG VAL GLU LYS MET LYS GLN ALA GLY ILE ILE
SEQRES 5 A 152 THR GLY ALA ARG ILE ASP VAL SER PRO LYS GLN LEU GLY
SEQRES 6 A 152 TYR ASP VAL GLY CYS PHE ILE GLY ILE ILE LEU LYS SER
SEQRES 7 A 152 ALA LYS ASP TYR PRO SER ALA LEU ALA LYS LEU GLU SER
SEQRES 8 A 152 LEU ASP GLU VAL THR GLU ALA TYR TYR THR THR GLY HIS
SEQRES 9 A 152 TYR SER ILE PHE ILE LYS VAL MET CYS ARG SER ILE ASP
SEQRES 10 A 152 ALA LEU GLN HIS VAL LEU ILE ASN LYS ILE GLN THR ILE
SEQRES 11 A 152 ASP GLU ILE GLN SER THR GLU THR LEU ILE VAL LEU GLN
SEQRES 12 A 152 ASN PRO ILE MET ARG THR ILE LYS PRO
SEQRES 1 B 152 MET GLU ASN TYR LEU ILE ASP ASN LEU ASP ARG GLY ILE
SEQRES 2 B 152 LEU GLU ALA LEU MET GLY ASN ALA ARG THR ALA TYR ALA
SEQRES 3 B 152 GLU LEU ALA LYS GLN PHE GLY VAL SER PRO GLU THR ILE
SEQRES 4 B 152 HIS VAL ARG VAL GLU LYS MET LYS GLN ALA GLY ILE ILE
SEQRES 5 B 152 THR GLY ALA ARG ILE ASP VAL SER PRO LYS GLN LEU GLY
SEQRES 6 B 152 TYR ASP VAL GLY CYS PHE ILE GLY ILE ILE LEU LYS SER
SEQRES 7 B 152 ALA LYS ASP TYR PRO SER ALA LEU ALA LYS LEU GLU SER
SEQRES 8 B 152 LEU ASP GLU VAL THR GLU ALA TYR TYR THR THR GLY HIS
SEQRES 9 B 152 TYR SER ILE PHE ILE LYS VAL MET CYS ARG SER ILE ASP
SEQRES 10 B 152 ALA LEU GLN HIS VAL LEU ILE ASN LYS ILE GLN THR ILE
SEQRES 11 B 152 ASP GLU ILE GLN SER THR GLU THR LEU ILE VAL LEU GLN
SEQRES 12 B 152 ASN PRO ILE MET ARG THR ILE LYS PRO
HET ASN A1153 9
HET MG A1154 1
HET ASN B1153 9
HETNAM ASN ASPARAGINE
HETNAM MG MAGNESIUM ION
FORMUL 3 ASN 2(C4 H8 N2 O3)
FORMUL 4 MG MG 2+
FORMUL 6 HOH *135(H2 O)
HELIX 1 1 ASP A 7 ASN A 20 1 14
HELIX 2 2 ALA A 24 GLY A 33 1 10
HELIX 3 3 SER A 35 ALA A 49 1 15
HELIX 4 4 SER A 78 LYS A 80 5 3
HELIX 5 5 ASP A 81 SER A 91 1 11
HELIX 6 6 SER A 115 LYS A 126 1 12
HELIX 7 7 ASP B 7 ASN B 20 1 14
HELIX 8 8 ALA B 24 GLY B 33 1 10
HELIX 9 9 SER B 35 ALA B 49 1 15
HELIX 10 10 PRO B 61 GLY B 65 5 5
HELIX 11 11 SER B 78 LYS B 80 5 3
HELIX 12 12 ASP B 81 SER B 91 1 11
HELIX 13 13 SER B 115 LYS B 126 1 12
SHEET 1 AA 2 ILE A 52 VAL A 59 0
SHEET 2 AA 2 ILE B 52 VAL B 59 -1 N THR B 53 O ASP A 58
SHEET 1 AB 9 VAL A 68 LEU A 76 0
SHEET 2 AB 9 ILE A 107 CYS A 113 -1 O ILE A 107 N ILE A 74
SHEET 3 AB 9 VAL A 95 THR A 101 -1 N THR A 96 O LYS A 110
SHEET 4 AB 9 ILE B 133 MET B 147 -1 N LEU B 142 O TYR A 100
SHEET 5 AB 9 VAL B 68 LEU B 76 -1 O GLY B 69 N VAL B 141
SHEET 6 AB 9 ILE B 107 CYS B 113 -1 O ILE B 107 N ILE B 74
SHEET 7 AB 9 VAL B 95 THR B 101 -1 N THR B 96 O LYS B 110
SHEET 8 AB 9 ILE A 133 MET A 147 -1 N LEU A 142 O TYR B 100
SHEET 9 AB 9 VAL A 68 LEU A 76 -1 O GLY A 69 N VAL A 141
LINK OD2 ASP A 58 MG MG A1154 1555 1555 2.20
LINK MG MG A1154 OD2 ASP B 58 1555 1555 2.14
SITE 1 AC1 2 ASP A 58 ASP B 58
SITE 1 AC2 12 TYR A 100 THR A 101 THR A 102 GLY A 103
SITE 2 AC2 12 TYR A 105 SER A 106 GLN A 128 THR A 136
SITE 3 AC2 12 GLU A 137 THR A 138 HOH A2064 HOH A2066
SITE 1 AC3 12 TYR B 100 THR B 101 THR B 102 GLY B 103
SITE 2 AC3 12 TYR B 105 SER B 106 GLN B 128 THR B 136
SITE 3 AC3 12 GLU B 137 THR B 138 HOH B2059 HOH B2069
CRYST1 103.117 103.117 52.401 90.00 90.00 90.00 P 4 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 0.009698 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009698 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019084 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
