HEADER LYASE 11-NOV-06 2E2E
TITLE TPR DOMAIN OF NRFG MEDIATES THE COMPLEX FORMATION BETWEEN HEME LYASE
TITLE 2 AND FORMATE-DEPENDENT NITRITE REDUCTASE IN ESCHERICHIA COLI O157:H7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FORMATE-DEPENDENT NITRITE REDUCTASE COMPLEX NRFG SUBUNIT;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: TETRATRICOPEPTIDE REPEAT MOTIF;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: O157 : H7 EDL933;
SOURCE 5 GENE: NRFG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODONPLUS RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24A
KEYWDS TPR, CYTOCHROME C BIOGENESIS, O157:H7 EDL933, NRFG, FORMATE-DEPENDENT
KEYWDS 2 NITRITE REDUCTASE COMPLEX, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.HAN,K.KIM,J.OH,J.PARK,Y.KIM
REVDAT 5 13-MAR-24 2E2E 1 SEQADV
REVDAT 4 13-JUL-11 2E2E 1 VERSN
REVDAT 3 24-FEB-09 2E2E 1 VERSN
REVDAT 2 16-SEP-08 2E2E 1 JRNL
REVDAT 1 23-OCT-07 2E2E 0
JRNL AUTH D.HAN,K.KIM,J.OH,J.PARK,Y.KIM
JRNL TITL TPR DOMAIN OF NRFG MEDIATES COMPLEX FORMATION BETWEEN HEME
JRNL TITL 2 LYASE AND FORMATE-DEPENDENT NITRITE REDUCTASE IN ESCHERICHIA
JRNL TITL 3 COLI O157:H7.
JRNL REF PROTEINS V. 70 900 2008
JRNL REFN ISSN 0887-3585
JRNL PMID 17803240
JRNL DOI 10.1002/PROT.21597
REMARK 2
REMARK 2 RESOLUTION. 2.05 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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 22119
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) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2450
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1603
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.65
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 155
REMARK 3 BIN FREE R VALUE : 0.3040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2812
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.07000
REMARK 3 B22 (A**2) : -1.97000
REMARK 3 B33 (A**2) : -3.10000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.271
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.211
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.163
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.697
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2884 ; 0.013 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3898 ; 1.433 ; 1.929
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 338 ; 8.395 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 164 ;35.864 ;24.512
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 500 ;18.199 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;21.860 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 416 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2236 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1402 ; 0.229 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1941 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 170 ; 0.187 ; 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): 73 ; 0.211 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.157 ; 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): 1750 ; 0.746 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2714 ; 1.204 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1294 ; 2.071 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1184 ; 3.141 ; 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 : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 31 A 206 1
REMARK 3 1 B 31 B 206 1
REMARK 3 2 A 31 A 206 1
REMARK 3 2 B 31 B 206 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2812 ; 0.01 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 2812 ; 0.05 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 31 A 50
REMARK 3 RESIDUE RANGE : A 56 A 206
REMARK 3 ORIGIN FOR THE GROUP (A): 11.6222 22.5293 30.0725
REMARK 3 T TENSOR
REMARK 3 T11: -0.1026 T22: -0.0945
REMARK 3 T33: -0.0596 T12: 0.0256
REMARK 3 T13: -0.0301 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 1.9209 L22: 3.9242
REMARK 3 L33: 2.4389 L12: 2.4958
REMARK 3 L13: 0.7050 L23: 0.8221
REMARK 3 S TENSOR
REMARK 3 S11: -0.1353 S12: 0.1820 S13: 0.2450
REMARK 3 S21: -0.3554 S22: 0.2084 S23: 0.1566
REMARK 3 S31: 0.3885 S32: 0.0833 S33: -0.0731
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 31 B 50
REMARK 3 RESIDUE RANGE : B 56 B 206
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2948 4.9709 5.5416
REMARK 3 T TENSOR
REMARK 3 T11: -0.1096 T22: -0.0959
REMARK 3 T33: -0.0523 T12: 0.0198
REMARK 3 T13: 0.0363 T23: -0.0352
REMARK 3 L TENSOR
REMARK 3 L11: 1.7931 L22: 3.7857
REMARK 3 L33: 2.4967 L12: 2.3825
REMARK 3 L13: -0.6854 L23: -0.8410
REMARK 3 S TENSOR
REMARK 3 S11: -0.1641 S12: 0.1929 S13: -0.2498
REMARK 3 S21: -0.3655 S22: 0.2294 S23: -0.1502
REMARK 3 S31: -0.3859 S32: -0.0817 S33: -0.0653
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 2E2E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-NOV-06.
REMARK 100 THE DEPOSITION ID IS D_1000026138.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAY-05; 13-MAY-05
REMARK 200 TEMPERATURE (KELVIN) : NULL; NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : PAL/PLS; PAL/PLS
REMARK 200 BEAMLINE : 4A; 6B
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950, 0.97956, 0.97171; NULL
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210; ADSC QUANTUM
REMARK 200 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22119
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 45.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
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) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
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: MAD; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 42.91200
REMARK 290 SMTRY3 2 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: DIMERIC
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 PRO A 30
REMARK 465 SER A 51
REMARK 465 GLN A 52
REMARK 465 GLN A 53
REMARK 465 ASN A 54
REMARK 465 PRO A 55
REMARK 465 PRO B 30
REMARK 465 SER B 51
REMARK 465 GLN B 52
REMARK 465 GLN B 53
REMARK 465 ASN B 54
REMARK 465 PRO B 55
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 TRP A 32 -50.27 -121.20
REMARK 500 ALA A 34 80.81 -153.03
REMARK 500 ARG A 36 110.33 74.34
REMARK 500 GLN A 40 -152.78 -68.05
REMARK 500 ARG A 41 -119.72 -141.27
REMARK 500 GLN A 42 -16.52 -141.82
REMARK 500 LEU A 59 73.54 -104.88
REMARK 500 ASN A 106 119.74 -160.46
REMARK 500 ALA A 121 30.49 -90.57
REMARK 500 ASP A 140 99.79 -161.41
REMARK 500 HIS A 203 79.25 -113.47
REMARK 500 TRP B 32 -50.21 -120.72
REMARK 500 ALA B 34 80.40 -153.41
REMARK 500 ARG B 36 110.26 75.11
REMARK 500 GLN B 40 -152.79 -67.99
REMARK 500 ARG B 41 -119.84 -141.04
REMARK 500 GLN B 42 -16.47 -141.57
REMARK 500 LEU B 59 73.55 -104.64
REMARK 500 ASN B 106 119.49 -161.38
REMARK 500 ASP B 140 101.54 -160.89
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 GLN A 48 PHE A 49 148.22
REMARK 500 PHE A 49 ALA A 50 -116.57
REMARK 500 GLN B 48 PHE B 49 147.94
REMARK 500 PHE B 49 ALA B 50 -69.45
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 BME A1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B4001
DBREF 2E2E A 30 198 UNP Q8X5S3 NRFG_ECO57 30 198
DBREF 2E2E B 30 198 UNP Q8X5S3 NRFG_ECO57 30 198
SEQADV 2E2E LEU A 199 UNP Q8X5S3 EXPRESSION TAG
SEQADV 2E2E GLU A 200 UNP Q8X5S3 EXPRESSION TAG
SEQADV 2E2E HIS A 201 UNP Q8X5S3 EXPRESSION TAG
SEQADV 2E2E HIS A 202 UNP Q8X5S3 EXPRESSION TAG
SEQADV 2E2E HIS A 203 UNP Q8X5S3 EXPRESSION TAG
SEQADV 2E2E HIS A 204 UNP Q8X5S3 EXPRESSION TAG
SEQADV 2E2E HIS A 205 UNP Q8X5S3 EXPRESSION TAG
SEQADV 2E2E HIS A 206 UNP Q8X5S3 EXPRESSION TAG
SEQADV 2E2E LEU B 199 UNP Q8X5S3 EXPRESSION TAG
SEQADV 2E2E GLU B 200 UNP Q8X5S3 EXPRESSION TAG
SEQADV 2E2E HIS B 201 UNP Q8X5S3 EXPRESSION TAG
SEQADV 2E2E HIS B 202 UNP Q8X5S3 EXPRESSION TAG
SEQADV 2E2E HIS B 203 UNP Q8X5S3 EXPRESSION TAG
SEQADV 2E2E HIS B 204 UNP Q8X5S3 EXPRESSION TAG
SEQADV 2E2E HIS B 205 UNP Q8X5S3 EXPRESSION TAG
SEQADV 2E2E HIS B 206 UNP Q8X5S3 EXPRESSION TAG
SEQRES 1 A 177 PRO LYS TRP GLN ALA VAL ARG ALA GLU TYR GLN ARG GLN
SEQRES 2 A 177 ARG ASP PRO LEU HIS GLN PHE ALA SER GLN GLN ASN PRO
SEQRES 3 A 177 GLU ALA GLN LEU GLN ALA LEU GLN ASP LYS ILE ARG ALA
SEQRES 4 A 177 ASN PRO GLN ASN SER GLU GLN TRP ALA LEU LEU GLY GLU
SEQRES 5 A 177 TYR TYR LEU TRP GLN ASN ASP TYR SER ASN SER LEU LEU
SEQRES 6 A 177 ALA TYR ARG GLN ALA LEU GLN LEU ARG GLY GLU ASN ALA
SEQRES 7 A 177 GLU LEU TYR ALA ALA LEU ALA THR VAL LEU TYR TYR GLN
SEQRES 8 A 177 ALA SER GLN HIS MET THR ALA GLN THR ARG ALA MET ILE
SEQRES 9 A 177 ASP LYS ALA LEU ALA LEU ASP SER ASN GLU ILE THR ALA
SEQRES 10 A 177 LEU MET LEU LEU ALA SER ASP ALA PHE MET GLN ALA ASN
SEQRES 11 A 177 TYR ALA GLN ALA ILE GLU LEU TRP GLN LYS VAL MET ASP
SEQRES 12 A 177 LEU ASN SER PRO ARG ILE ASN ARG THR GLN LEU VAL GLU
SEQRES 13 A 177 SER ILE ASN MET ALA LYS LEU LEU GLN ARG ARG SER ASP
SEQRES 14 A 177 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 177 PRO LYS TRP GLN ALA VAL ARG ALA GLU TYR GLN ARG GLN
SEQRES 2 B 177 ARG ASP PRO LEU HIS GLN PHE ALA SER GLN GLN ASN PRO
SEQRES 3 B 177 GLU ALA GLN LEU GLN ALA LEU GLN ASP LYS ILE ARG ALA
SEQRES 4 B 177 ASN PRO GLN ASN SER GLU GLN TRP ALA LEU LEU GLY GLU
SEQRES 5 B 177 TYR TYR LEU TRP GLN ASN ASP TYR SER ASN SER LEU LEU
SEQRES 6 B 177 ALA TYR ARG GLN ALA LEU GLN LEU ARG GLY GLU ASN ALA
SEQRES 7 B 177 GLU LEU TYR ALA ALA LEU ALA THR VAL LEU TYR TYR GLN
SEQRES 8 B 177 ALA SER GLN HIS MET THR ALA GLN THR ARG ALA MET ILE
SEQRES 9 B 177 ASP LYS ALA LEU ALA LEU ASP SER ASN GLU ILE THR ALA
SEQRES 10 B 177 LEU MET LEU LEU ALA SER ASP ALA PHE MET GLN ALA ASN
SEQRES 11 B 177 TYR ALA GLN ALA ILE GLU LEU TRP GLN LYS VAL MET ASP
SEQRES 12 B 177 LEU ASN SER PRO ARG ILE ASN ARG THR GLN LEU VAL GLU
SEQRES 13 B 177 SER ILE ASN MET ALA LYS LEU LEU GLN ARG ARG SER ASP
SEQRES 14 B 177 LEU GLU HIS HIS HIS HIS HIS HIS
HET BME A1001 4
HET IMD A3001 5
HET BME B2001 4
HET IMD B4001 5
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM IMD IMIDAZOLE
FORMUL 3 BME 2(C2 H6 O S)
FORMUL 4 IMD 2(C3 H5 N2 1+)
FORMUL 7 HOH *190(H2 O)
HELIX 1 1 LEU A 59 ASN A 69 1 11
HELIX 2 2 ASN A 72 GLN A 86 1 15
HELIX 3 3 ASP A 88 GLY A 104 1 17
HELIX 4 4 ASN A 106 ALA A 121 1 16
HELIX 5 5 THR A 126 ASP A 140 1 15
HELIX 6 6 GLU A 143 GLN A 157 1 15
HELIX 7 7 ASN A 159 LEU A 173 1 15
HELIX 8 8 ASN A 179 HIS A 202 1 24
HELIX 9 9 LEU B 59 ASN B 69 1 11
HELIX 10 10 ASN B 72 GLN B 86 1 15
HELIX 11 11 ASP B 88 GLY B 104 1 17
HELIX 12 12 ASN B 106 ALA B 121 1 16
HELIX 13 13 THR B 126 ASP B 140 1 15
HELIX 14 14 GLU B 143 GLN B 157 1 15
HELIX 15 15 ASN B 159 LEU B 173 1 15
HELIX 16 16 ASN B 179 HIS B 202 1 24
CISPEP 1 TRP A 32 GLN A 33 0 14.30
CISPEP 2 GLU A 56 ALA A 57 0 -7.26
CISPEP 3 TRP B 32 GLN B 33 0 14.16
CISPEP 4 GLU B 56 ALA B 57 0 -7.34
SITE 1 AC1 3 ARG A 97 GLN A 128 HOH A3048
SITE 1 AC2 3 ARG B 97 HOH B4040 HOH B4064
SITE 1 AC3 2 HIS A 201 HIS A 203
SITE 1 AC4 2 HIS B 201 HIS B 203
CRYST1 47.802 85.824 49.073 90.00 89.99 90.00 P 1 21 1 4
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 0.020920 0.000000 -0.000003 0.00000
SCALE2 0.000000 0.011652 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020378 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
