HEADER DNA BINDING PROTEIN 18-APR-18 6GCM
TITLE ESCHERICHIA COLI DPS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA PROTECTION DURING STARVATION PROTEIN;
COMPND 3 CHAIN: A, b;
COMPND 4 EC: 1.16.-.-;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA PROTECTION DURING STARVATION PROTEIN;
COMPND 7 CHAIN: B, C, E, F, G, H, I, J, K, L, c, d, g, h, i, j, k, l, m;
COMPND 8 EC: 1.16.-.-;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: DNA PROTECTION DURING STARVATION PROTEIN;
COMPND 11 CHAIN: D, e;
COMPND 12 EC: 1.16.-.-;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: DNA PROTECTION DURING STARVATION PROTEIN;
COMPND 16 CHAIN: f;
COMPND 17 EC: 1.16.-.-
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 7 ORGANISM_TAXID: 83333;
SOURCE 8 STRAIN: K12;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 11 ORGANISM_TAXID: 83333;
SOURCE 12 STRAIN: K12;
SOURCE 13 GENE: DPS, PEXB, VTM, B0812, JW0797;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 18 ORGANISM_TAXID: 83333;
SOURCE 19 STRAIN: K12
KEYWDS DNA-BINDING PROTEIN, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR V.V.KOVALENKO,N.G.LOIKO,E.V.TERESHKIN,K.B.TERESHKINA,A.L.CHULICHKOV,
AUTHOR 2 A.N.POPOV,Y.F.KRUPYANSKII
REVDAT 2 17-JAN-24 6GCM 1 REMARK
REVDAT 1 01-MAY-19 6GCM 0
JRNL AUTH V.V.KOVALENKO,N.G.LOIKO,E.V.TERESHKIN,K.B.TERESHKINA,
JRNL AUTH 2 A.L.CHULICHKOV,A.N.POPOV,Y.F.KRUPYANSKII
JRNL TITL ESCHERICHIA COLI DPS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 139323
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7407
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) : 2.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.51
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10263
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.44
REMARK 3 BIN R VALUE (WORKING SET) : 0.3770
REMARK 3 BIN FREE R VALUE SET COUNT : 534
REMARK 3 BIN FREE R VALUE : 0.4160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 29282
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 954
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.14000
REMARK 3 B22 (A**2) : -0.29000
REMARK 3 B33 (A**2) : 1.43000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.73000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.649
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.300
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.275
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.292
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.887
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 29711 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 40286 ; 1.583 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3679 ; 5.488 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1466 ;40.039 ;24.932
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5292 ;17.455 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 192 ;17.150 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4760 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 22232 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 14788 ; 2.106 ; 3.527
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 18443 ; 3.289 ; 5.281
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 14923 ; 2.912 ; 3.682
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 46663 ; 6.038 ;15.890
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6GCM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009689.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.972422
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 138619
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
REMARK 200 RESOLUTION RANGE LOW (A) : 150.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 1.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: 1DPS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, EVAPORATION,
REMARK 280 RECRYSTALLIZATION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 44800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -137.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 44820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -143.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: b, c, d, e, f, g, h, i, j, k,
REMARK 350 AND CHAINS: l, m
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 SER A 9
REMARK 465 LYS A 10
REMARK 465 ALA A 11
REMARK 465 THR A 12
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 ASN A 13 CG OD1 ND2
REMARK 470 LYS B 27 CD CE NZ
REMARK 470 LYS B 134 CG CD CE NZ
REMARK 470 LYS C 27 CD CE NZ
REMARK 470 LYS E 101 CE NZ
REMARK 470 LYS F 101 CE NZ
REMARK 470 LYS G 27 CE NZ
REMARK 470 LYS G 101 CD CE
REMARK 470 LYS H 101 CE NZ
REMARK 470 LYS I 27 CD CE NZ
REMARK 470 LYS I 101 CE NZ
REMARK 470 LYS J 101 NZ
REMARK 470 LYS L 101 CE NZ
REMARK 470 LYS L 134 CE NZ
REMARK 470 LYS b 10 CG CD CE NZ
REMARK 470 LYS c 27 CD CE NZ
REMARK 470 LYS c 134 CG CD CE NZ
REMARK 470 LYS d 27 CD CE NZ
REMARK 470 LYS f 101 CE NZ
REMARK 470 LYS g 101 CE NZ
REMARK 470 LYS h 27 CE NZ
REMARK 470 LYS h 101 CD CE
REMARK 470 LYS i 101 CE NZ
REMARK 470 LYS j 27 CD CE NZ
REMARK 470 LYS j 101 CE NZ
REMARK 470 LYS k 101 NZ
REMARK 470 LYS m 101 CE NZ
REMARK 470 LYS m 134 CE NZ
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 112 -45.32 -135.91
REMARK 500 HIS B 112 -35.93 -146.03
REMARK 500 SER C 106 121.49 -33.95
REMARK 500 HIS C 112 -50.67 -132.75
REMARK 500 ASN D 13 -9.03 96.27
REMARK 500 HIS D 112 -42.18 -135.99
REMARK 500 ASP E 20 92.33 -64.94
REMARK 500 SER E 106 123.42 -34.98
REMARK 500 HIS E 112 -46.14 -135.04
REMARK 500 HIS F 112 -51.13 -130.47
REMARK 500 HIS G 112 -37.59 -134.49
REMARK 500 ASP H 23 -82.30 51.31
REMARK 500 SER H 106 130.57 -39.76
REMARK 500 HIS I 112 -43.23 -137.69
REMARK 500 HIS J 112 -50.31 -139.23
REMARK 500 SER K 106 132.38 -29.41
REMARK 500 HIS K 112 -30.64 -134.15
REMARK 500 ASN b 13 -5.07 65.44
REMARK 500 SER b 106 117.78 -38.23
REMARK 500 HIS b 112 -36.62 -134.14
REMARK 500 SER c 106 118.87 -37.27
REMARK 500 HIS c 112 -49.28 -135.99
REMARK 500 ASP d 20 47.90 -96.24
REMARK 500 SER d 106 126.99 -37.04
REMARK 500 HIS d 112 -41.44 -135.40
REMARK 500 HIS e 112 -49.24 -136.56
REMARK 500 ASP f 110 21.58 -146.49
REMARK 500 HIS f 112 -36.67 -132.63
REMARK 500 SER g 106 125.68 -38.34
REMARK 500 HIS g 112 -29.58 -143.03
REMARK 500 HIS h 112 -33.84 -135.56
REMARK 500 SER j 106 124.58 -32.76
REMARK 500 HIS k 112 -38.97 -139.38
REMARK 500 SER l 106 124.03 -34.23
REMARK 500 HIS l 112 -39.65 -133.44
REMARK 500 HIS m 112 -50.10 -133.35
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 C 236 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH L 238 DISTANCE = 7.65 ANGSTROMS
REMARK 525 HOH d 240 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH l 242 DISTANCE = 8.06 ANGSTROMS
DBREF 6GCM A 9 167 UNP P0ABT2 DPS_ECOLI 9 167
DBREF 6GCM B 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM C 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM D 12 167 UNP P0ABT2 DPS_ECOLI 12 167
DBREF 6GCM E 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM F 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM G 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM H 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM I 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM J 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM K 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM L 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM b 9 167 UNP P0ABT2 DPS_ECOLI 9 167
DBREF 6GCM c 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM d 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM e 12 167 UNP P0ABT2 DPS_ECOLI 12 167
DBREF 6GCM f 17 167 UNP P0ABT2 DPS_ECOLI 17 167
DBREF 6GCM g 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM h 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM i 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM j 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM k 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM l 14 167 UNP P0ABT2 DPS_ECOLI 14 167
DBREF 6GCM m 14 167 UNP P0ABT2 DPS_ECOLI 14 167
SEQRES 1 A 159 SER LYS ALA THR ASN LEU LEU TYR THR ARG ASN ASP VAL
SEQRES 2 A 159 SER ASP SER GLU LYS LYS ALA THR VAL GLU LEU LEU ASN
SEQRES 3 A 159 ARG GLN VAL ILE GLN PHE ILE ASP LEU SER LEU ILE THR
SEQRES 4 A 159 LYS GLN ALA HIS TRP ASN MET ARG GLY ALA ASN PHE ILE
SEQRES 5 A 159 ALA VAL HIS GLU MET LEU ASP GLY PHE ARG THR ALA LEU
SEQRES 6 A 159 ILE ASP HIS LEU ASP THR MET ALA GLU ARG ALA VAL GLN
SEQRES 7 A 159 LEU GLY GLY VAL ALA LEU GLY THR THR GLN VAL ILE ASN
SEQRES 8 A 159 SER LYS THR PRO LEU LYS SER TYR PRO LEU ASP ILE HIS
SEQRES 9 A 159 ASN VAL GLN ASP HIS LEU LYS GLU LEU ALA ASP ARG TYR
SEQRES 10 A 159 ALA ILE VAL ALA ASN ASP VAL ARG LYS ALA ILE GLY GLU
SEQRES 11 A 159 ALA LYS ASP ASP ASP THR ALA ASP ILE LEU THR ALA ALA
SEQRES 12 A 159 SER ARG ASP LEU ASP LYS PHE LEU TRP PHE ILE GLU SER
SEQRES 13 A 159 ASN ILE GLU
SEQRES 1 B 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 B 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 B 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 B 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 B 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 B 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 B 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 B 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 B 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 B 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 B 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 B 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 C 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 C 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 C 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 C 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 C 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 C 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 C 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 C 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 C 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 C 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 C 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 C 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 D 156 THR ASN LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER
SEQRES 2 D 156 GLU LYS LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL
SEQRES 3 D 156 ILE GLN PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA
SEQRES 4 D 156 HIS TRP ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS
SEQRES 5 D 156 GLU MET LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS
SEQRES 6 D 156 LEU ASP THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY
SEQRES 7 D 156 VAL ALA LEU GLY THR THR GLN VAL ILE ASN SER LYS THR
SEQRES 8 D 156 PRO LEU LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN
SEQRES 9 D 156 ASP HIS LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL
SEQRES 10 D 156 ALA ASN ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP
SEQRES 11 D 156 ASP ASP THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP
SEQRES 12 D 156 LEU ASP LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 E 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 E 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 E 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 E 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 E 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 E 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 E 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 E 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 E 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 E 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 E 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 E 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 F 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 F 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 F 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 F 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 F 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 F 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 F 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 F 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 F 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 F 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 F 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 F 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 G 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 G 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 G 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 G 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 G 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 G 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 G 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 G 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 G 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 G 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 G 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 G 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 H 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 H 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 H 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 H 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 H 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 H 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 H 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 H 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 H 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 H 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 H 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 H 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 I 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 I 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 I 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 I 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 I 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 I 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 I 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 I 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 I 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 I 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 I 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 I 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 J 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 J 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 J 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 J 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 J 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 J 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 J 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 J 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 J 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 J 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 J 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 J 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 K 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 K 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 K 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 K 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 K 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 K 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 K 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 K 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 K 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 K 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 K 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 K 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 L 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 L 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 L 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 L 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 L 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 L 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 L 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 L 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 L 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 L 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 L 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 L 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 b 159 SER LYS ALA THR ASN LEU LEU TYR THR ARG ASN ASP VAL
SEQRES 2 b 159 SER ASP SER GLU LYS LYS ALA THR VAL GLU LEU LEU ASN
SEQRES 3 b 159 ARG GLN VAL ILE GLN PHE ILE ASP LEU SER LEU ILE THR
SEQRES 4 b 159 LYS GLN ALA HIS TRP ASN MET ARG GLY ALA ASN PHE ILE
SEQRES 5 b 159 ALA VAL HIS GLU MET LEU ASP GLY PHE ARG THR ALA LEU
SEQRES 6 b 159 ILE ASP HIS LEU ASP THR MET ALA GLU ARG ALA VAL GLN
SEQRES 7 b 159 LEU GLY GLY VAL ALA LEU GLY THR THR GLN VAL ILE ASN
SEQRES 8 b 159 SER LYS THR PRO LEU LYS SER TYR PRO LEU ASP ILE HIS
SEQRES 9 b 159 ASN VAL GLN ASP HIS LEU LYS GLU LEU ALA ASP ARG TYR
SEQRES 10 b 159 ALA ILE VAL ALA ASN ASP VAL ARG LYS ALA ILE GLY GLU
SEQRES 11 b 159 ALA LYS ASP ASP ASP THR ALA ASP ILE LEU THR ALA ALA
SEQRES 12 b 159 SER ARG ASP LEU ASP LYS PHE LEU TRP PHE ILE GLU SER
SEQRES 13 b 159 ASN ILE GLU
SEQRES 1 c 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 c 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 c 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 c 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 c 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 c 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 c 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 c 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 c 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 c 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 c 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 c 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 d 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 d 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 d 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 d 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 d 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 d 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 d 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 d 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 d 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 d 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 d 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 d 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 e 156 THR ASN LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER
SEQRES 2 e 156 GLU LYS LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL
SEQRES 3 e 156 ILE GLN PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA
SEQRES 4 e 156 HIS TRP ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS
SEQRES 5 e 156 GLU MET LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS
SEQRES 6 e 156 LEU ASP THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY
SEQRES 7 e 156 VAL ALA LEU GLY THR THR GLN VAL ILE ASN SER LYS THR
SEQRES 8 e 156 PRO LEU LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN
SEQRES 9 e 156 ASP HIS LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL
SEQRES 10 e 156 ALA ASN ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP
SEQRES 11 e 156 ASP ASP THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP
SEQRES 12 e 156 LEU ASP LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 f 151 THR ARG ASN ASP VAL SER ASP SER GLU LYS LYS ALA THR
SEQRES 2 f 151 VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN PHE ILE ASP
SEQRES 3 f 151 LEU SER LEU ILE THR LYS GLN ALA HIS TRP ASN MET ARG
SEQRES 4 f 151 GLY ALA ASN PHE ILE ALA VAL HIS GLU MET LEU ASP GLY
SEQRES 5 f 151 PHE ARG THR ALA LEU ILE ASP HIS LEU ASP THR MET ALA
SEQRES 6 f 151 GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA LEU GLY THR
SEQRES 7 f 151 THR GLN VAL ILE ASN SER LYS THR PRO LEU LYS SER TYR
SEQRES 8 f 151 PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS LEU LYS GLU
SEQRES 9 f 151 LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN ASP VAL ARG
SEQRES 10 f 151 LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP THR ALA ASP
SEQRES 11 f 151 ILE LEU THR ALA ALA SER ARG ASP LEU ASP LYS PHE LEU
SEQRES 12 f 151 TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 g 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 g 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 g 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 g 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 g 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 g 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 g 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 g 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 g 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 g 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 g 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 g 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 h 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 h 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 h 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 h 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 h 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 h 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 h 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 h 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 h 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 h 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 h 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 h 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 i 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 i 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 i 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 i 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 i 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 i 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 i 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 i 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 i 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 i 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 i 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 i 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 j 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 j 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 j 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 j 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 j 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 j 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 j 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 j 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 j 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 j 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 j 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 j 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 k 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 k 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 k 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 k 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 k 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 k 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 k 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 k 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 k 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 k 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 k 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 k 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 l 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 l 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 l 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 l 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 l 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 l 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 l 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 l 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 l 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 l 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 l 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 l 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 m 154 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 2 m 154 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 3 m 154 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 4 m 154 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 5 m 154 LEU ASP GLY PHE ARG THR ALA LEU ILE ASP HIS LEU ASP
SEQRES 6 m 154 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 7 m 154 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 8 m 154 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 9 m 154 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 10 m 154 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 11 m 154 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 12 m 154 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
FORMUL 25 HOH *954(H2 O)
HELIX 1 AA1 SER A 22 ASN A 53 1 32
HELIX 2 AA2 ASN A 58 LEU A 87 1 30
HELIX 3 AA3 THR A 94 THR A 102 1 9
HELIX 4 AA4 ASN A 113 ALA A 139 1 27
HELIX 5 AA5 ASP A 141 SER A 164 1 24
HELIX 6 AA6 SER B 22 ASN B 53 1 32
HELIX 7 AA7 ASN B 58 LEU B 87 1 30
HELIX 8 AA8 THR B 94 THR B 102 1 9
HELIX 9 AA9 ASN B 113 ALA B 139 1 27
HELIX 10 AB1 ASP B 141 ASN B 165 1 25
HELIX 11 AB2 SER C 22 MET C 54 1 33
HELIX 12 AB3 ASN C 58 LEU C 87 1 30
HELIX 13 AB4 THR C 94 THR C 102 1 9
HELIX 14 AB5 ASN C 113 ALA C 139 1 27
HELIX 15 AB6 ASP C 141 ASN C 165 1 25
HELIX 16 AB7 SER D 22 ASN D 53 1 32
HELIX 17 AB8 ASN D 58 LEU D 87 1 30
HELIX 18 AB9 THR D 94 THR D 102 1 9
HELIX 19 AC1 ASN D 113 ALA D 139 1 27
HELIX 20 AC2 ASP D 141 ASN D 165 1 25
HELIX 21 AC3 SER E 22 MET E 54 1 33
HELIX 22 AC4 ASN E 58 LEU E 87 1 30
HELIX 23 AC5 THR E 94 THR E 102 1 9
HELIX 24 AC6 ASN E 113 ALA E 139 1 27
HELIX 25 AC7 ASP E 141 ASN E 165 1 25
HELIX 26 AC8 SER F 22 MET F 54 1 33
HELIX 27 AC9 ASN F 58 LEU F 87 1 30
HELIX 28 AD1 THR F 94 THR F 102 1 9
HELIX 29 AD2 ASN F 113 ALA F 139 1 27
HELIX 30 AD3 ASP F 141 ASN F 165 1 25
HELIX 31 AD4 SER G 22 MET G 54 1 33
HELIX 32 AD5 ASN G 58 LEU G 87 1 30
HELIX 33 AD6 THR G 94 THR G 102 1 9
HELIX 34 AD7 ASN G 113 ALA G 139 1 27
HELIX 35 AD8 ASP G 141 ASN G 165 1 25
HELIX 36 AD9 ASP H 23 MET H 54 1 32
HELIX 37 AE1 ASN H 58 LEU H 87 1 30
HELIX 38 AE2 THR H 94 THR H 102 1 9
HELIX 39 AE3 ASN H 113 ALA H 139 1 27
HELIX 40 AE4 ASP H 141 ASN H 165 1 25
HELIX 41 AE5 SER I 22 MET I 54 1 33
HELIX 42 AE6 ASN I 58 LEU I 87 1 30
HELIX 43 AE7 THR I 94 THR I 102 1 9
HELIX 44 AE8 ASN I 113 ALA I 139 1 27
HELIX 45 AE9 ASP I 141 ASN I 165 1 25
HELIX 46 AF1 SER J 22 MET J 54 1 33
HELIX 47 AF2 ASN J 58 LEU J 87 1 30
HELIX 48 AF3 THR J 94 THR J 102 1 9
HELIX 49 AF4 ASN J 113 ALA J 139 1 27
HELIX 50 AF5 ASP J 141 ASN J 165 1 25
HELIX 51 AF6 SER K 22 MET K 54 1 33
HELIX 52 AF7 ASN K 58 LEU K 87 1 30
HELIX 53 AF8 THR K 94 THR K 102 1 9
HELIX 54 AF9 ASN K 113 ALA K 139 1 27
HELIX 55 AG1 ASP K 141 ASN K 165 1 25
HELIX 56 AG2 SER L 22 ASN L 53 1 32
HELIX 57 AG3 ASN L 58 LEU L 87 1 30
HELIX 58 AG4 THR L 94 THR L 102 1 9
HELIX 59 AG5 ASN L 113 ALA L 139 1 27
HELIX 60 AG6 ASP L 141 SER L 164 1 24
HELIX 61 AG7 SER b 22 ASN b 53 1 32
HELIX 62 AG8 ASN b 58 LEU b 87 1 30
HELIX 63 AG9 THR b 94 THR b 102 1 9
HELIX 64 AH1 ASN b 113 ALA b 139 1 27
HELIX 65 AH2 ASP b 141 ILE b 166 1 26
HELIX 66 AH3 SER c 22 ASN c 53 1 32
HELIX 67 AH4 ASN c 58 LEU c 87 1 30
HELIX 68 AH5 THR c 94 THR c 102 1 9
HELIX 69 AH6 ASN c 113 ALA c 139 1 27
HELIX 70 AH7 ASP c 141 ASN c 165 1 25
HELIX 71 AH8 SER d 22 MET d 54 1 33
HELIX 72 AH9 ASN d 58 LEU d 87 1 30
HELIX 73 AI1 THR d 94 THR d 102 1 9
HELIX 74 AI2 ASN d 113 ALA d 139 1 27
HELIX 75 AI3 ASP d 141 ASN d 165 1 25
HELIX 76 AI4 SER e 22 ASN e 53 1 32
HELIX 77 AI5 ASN e 58 LEU e 87 1 30
HELIX 78 AI6 THR e 94 THR e 102 1 9
HELIX 79 AI7 ASN e 113 ALA e 139 1 27
HELIX 80 AI8 ASP e 141 ILE e 166 1 26
HELIX 81 AI9 SER f 22 ASN f 53 1 32
HELIX 82 AJ1 ASN f 58 LEU f 87 1 30
HELIX 83 AJ2 THR f 94 THR f 102 1 9
HELIX 84 AJ3 ASN f 113 ALA f 139 1 27
HELIX 85 AJ4 ASP f 141 SER f 164 1 24
HELIX 86 AJ5 SER g 22 MET g 54 1 33
HELIX 87 AJ6 ASN g 58 LEU g 87 1 30
HELIX 88 AJ7 THR g 94 THR g 102 1 9
HELIX 89 AJ8 ASN g 113 ALA g 139 1 27
HELIX 90 AJ9 ASP g 141 ASN g 165 1 25
HELIX 91 AK1 SER h 22 ASN h 53 1 32
HELIX 92 AK2 ASN h 58 LEU h 87 1 30
HELIX 93 AK3 THR h 94 THR h 102 1 9
HELIX 94 AK4 ASN h 113 ALA h 139 1 27
HELIX 95 AK5 ASP h 141 ASN h 165 1 25
HELIX 96 AK6 SER i 22 ASN i 53 1 32
HELIX 97 AK7 ASN i 58 LEU i 87 1 30
HELIX 98 AK8 THR i 94 THR i 102 1 9
HELIX 99 AK9 ASN i 113 ALA i 139 1 27
HELIX 100 AL1 ASP i 141 ASN i 165 1 25
HELIX 101 AL2 SER j 22 ASN j 53 1 32
HELIX 102 AL3 ASN j 58 LEU j 87 1 30
HELIX 103 AL4 THR j 94 THR j 102 1 9
HELIX 104 AL5 ASN j 113 ALA j 139 1 27
HELIX 105 AL6 ASP j 141 ASN j 165 1 25
HELIX 106 AL7 SER k 22 MET k 54 1 33
HELIX 107 AL8 ASN k 58 LEU k 87 1 30
HELIX 108 AL9 THR k 94 THR k 102 1 9
HELIX 109 AM1 ASN k 113 ALA k 139 1 27
HELIX 110 AM2 ASP k 141 ASN k 165 1 25
HELIX 111 AM3 SER l 22 ASN l 53 1 32
HELIX 112 AM4 ASN l 58 LEU l 87 1 30
HELIX 113 AM5 THR l 94 THR l 102 1 9
HELIX 114 AM6 ASN l 113 ALA l 139 1 27
HELIX 115 AM7 ASP l 141 SER l 164 1 24
HELIX 116 AM8 SER m 22 MET m 54 1 33
HELIX 117 AM9 ASN m 58 LEU m 87 1 30
HELIX 118 AN1 THR m 94 THR m 102 1 9
HELIX 119 AN2 ASN m 113 GLY m 137 1 25
HELIX 120 AN3 ASP m 141 ASN m 165 1 25
CRYST1 150.150 89.420 150.650 90.00 90.24 90.00 P 1 2 1 38
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 0.006660 0.000000 0.000028 0.00000
SCALE2 0.000000 0.011183 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006638 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
