HEADER LYASE 19-DEC-08 3FLU
TITLE CRYSTAL STRUCTURE OF DIHYDRODIPICOLINATE SYNTHASE FROM THE PATHOGEN
TITLE 2 NEISSERIA MENINGITIDIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDRODIPICOLINATE SYNTHASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DHDPS;
COMPND 5 EC: 4.2.1.52;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS SEROGROUP B;
SOURCE 3 ORGANISM_TAXID: 491;
SOURCE 4 STRAIN: SEROGROUP B;
SOURCE 5 GENE: DAPA, NMB0929;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 STAR(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-151/D
KEYWDS TIM BARREL, BETA-ALPHA-BARREL, AMINO-ACID BIOSYNTHESIS,
KEYWDS 2 DIAMINOPIMELATE BIOSYNTHESIS, LYASE, LYSINE BIOSYNTHESIS, SCHIFF
KEYWDS 3 BASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.R.A.DEVENISH,A.T.HADFIELD
REVDAT 4 01-NOV-23 3FLU 1 REMARK SEQADV
REVDAT 3 01-NOV-17 3FLU 1 REMARK
REVDAT 2 13-JUL-11 3FLU 1 VERSN
REVDAT 1 23-JUN-09 3FLU 0
JRNL AUTH S.R.A.DEVENISH,F.H.A.HUISMAN,E.J.PARKER,A.T.HADFIELD,
JRNL AUTH 2 J.A.GERRARD
JRNL TITL CLONING AND CHARACTERISATION OF DIHYDRODIPICOLINATE SYNTHASE
JRNL TITL 2 FROM THE PATHOGEN NEISSERIA MENINGITIDIS.
JRNL REF BIOCHIM.BIOPHYS.ACTA 2009
JRNL REFN ISSN 0006-3002
JRNL PMID 19236959
JRNL DOI 10.1016/J.BBAPAP.2009.02.003
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 115.47
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 84214
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) : 0.151
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4201
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5813
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.15
REMARK 3 BIN R VALUE (WORKING SET) : 0.1690
REMARK 3 BIN FREE R VALUE SET COUNT : 276
REMARK 3 BIN FREE R VALUE : 0.2510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8722
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 264
REMARK 3 SOLVENT ATOMS : 938
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.23
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.34000
REMARK 3 B22 (A**2) : -0.70000
REMARK 3 B33 (A**2) : 0.36000
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): 0.152
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.138
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.086
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.030
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9263 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12625 ; 1.133 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1209 ; 6.825 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 363 ;35.065 ;24.793
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1476 ;12.642 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 49 ;16.803 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1473 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6833 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4770 ; 0.213 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6376 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 799 ; 0.137 ; 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): 51 ; 0.242 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 29 ; 0.179 ; 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): 6087 ; 1.726 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9543 ; 2.259 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3544 ; 4.421 ; 4.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3060 ; 6.212 ; 6.000
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 : D A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 9
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 D 3 D 13 4
REMARK 3 1 A 3 A 13 4
REMARK 3 1 B 3 B 13 4
REMARK 3 1 C 3 C 13 4
REMARK 3 2 D 28 D 63 4
REMARK 3 2 A 28 A 63 4
REMARK 3 2 B 28 B 63 4
REMARK 3 2 C 28 C 63 4
REMARK 3 3 D 67 D 82 4
REMARK 3 3 A 67 A 82 4
REMARK 3 3 B 67 B 82 4
REMARK 3 3 C 67 C 82 4
REMARK 3 4 D 86 D 144 4
REMARK 3 4 A 86 A 144 4
REMARK 3 4 B 86 B 144 4
REMARK 3 4 C 86 C 144 4
REMARK 3 5 D 155 D 174 4
REMARK 3 5 A 155 A 174 4
REMARK 3 5 B 155 B 174 4
REMARK 3 5 C 155 C 174 4
REMARK 3 6 D 181 D 228 4
REMARK 3 6 A 181 A 228 4
REMARK 3 6 B 181 B 228 4
REMARK 3 6 C 181 C 228 4
REMARK 3 7 D 237 D 261 4
REMARK 3 7 A 237 A 261 4
REMARK 3 7 B 237 B 261 4
REMARK 3 7 C 237 C 261 4
REMARK 3 8 D 267 D 273 4
REMARK 3 8 A 267 A 273 4
REMARK 3 8 B 267 B 273 4
REMARK 3 8 C 267 C 273 4
REMARK 3 9 D 277 D 290 4
REMARK 3 9 A 277 A 290 4
REMARK 3 9 B 277 B 290 4
REMARK 3 9 C 277 C 290 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 D (A): 1719 ; 0.200 ; 1.000
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1719 ; 0.230 ; 1.000
REMARK 3 MEDIUM POSITIONAL 1 B (A): 1719 ; 0.250 ; 1.000
REMARK 3 MEDIUM POSITIONAL 1 C (A): 1719 ; 0.200 ; 1.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 1719 ; 1.740 ; 2.000
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1719 ; 1.470 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 1719 ; 1.520 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 1719 ; 1.370 ; 2.000
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 3FLU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-DEC-08.
REMARK 100 THE DEPOSITION ID IS D_1000050749.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA, SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84251
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.999
REMARK 200 RESOLUTION RANGE LOW (A) : 115.684
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.09600
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) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.34900
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: PHASER
REMARK 200 STARTING MODEL: 1YXC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM SULFATE, 100MM BIS
REMARK 280 -TRIS.HCL, PH 5.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
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 40.33350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.06100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.84200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.06100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.33350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.84200
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 19150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -381.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -5
REMARK 465 ILE A -4
REMARK 465 ASP A -3
REMARK 465 GLY B -5
REMARK 465 ILE B -4
REMARK 465 ASP B -3
REMARK 465 PRO B -2
REMARK 465 PHE B -1
REMARK 465 THR B 0
REMARK 465 GLY C -5
REMARK 465 ILE C -4
REMARK 465 ASP C -3
REMARK 465 PRO C -2
REMARK 465 PHE C -1
REMARK 465 GLY D -5
REMARK 465 ILE D -4
REMARK 465 ASP D -3
REMARK 465 PRO D -2
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 TYR A 107 -52.64 74.25
REMARK 500 VAL A 140 -61.92 69.44
REMARK 500 TYR B 107 -50.85 73.43
REMARK 500 VAL B 140 -62.28 70.78
REMARK 500 TYR C 107 -53.97 77.06
REMARK 500 VAL C 140 -60.89 70.37
REMARK 500 ALA C 210 65.30 -151.59
REMARK 500 THR D 0 83.42 -155.27
REMARK 500 MET D 1 123.01 -28.61
REMARK 500 TYR D 107 -52.18 74.98
REMARK 500 VAL D 140 -60.80 71.51
REMARK 500 ALA D 210 66.19 -153.71
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 SO4 A 292
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 293
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 294
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 295
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 296
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 297
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 298
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 299
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 292
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 293
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 294
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 295
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 296
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 297
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 298
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 299
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 292
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 293
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 294
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 295
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 296
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 297
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 298
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 299
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 292
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 293
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 294
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 295
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 296
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 297
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 298
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 299
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YXC RELATED DB: PDB
REMARK 900 THE HOMOLOGOUS PROTEIN FROM E. COLI
REMARK 900 RELATED ID: 1YXD RELATED DB: PDB
REMARK 900 THE HOMOLOGOUS PROTEIN FROM E. COLI SOAKED WITH THE INHIBITOR LYSINE
DBREF 3FLU A 1 291 UNP Q9JZR4 DAPA_NEIMB 1 291
DBREF 3FLU B 1 291 UNP Q9JZR4 DAPA_NEIMB 1 291
DBREF 3FLU C 1 291 UNP Q9JZR4 DAPA_NEIMB 1 291
DBREF 3FLU D 1 291 UNP Q9JZR4 DAPA_NEIMB 1 291
SEQADV 3FLU GLY A -5 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU ILE A -4 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU ASP A -3 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU PRO A -2 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU PHE A -1 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU THR A 0 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU GLY B -5 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU ILE B -4 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU ASP B -3 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU PRO B -2 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU PHE B -1 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU THR B 0 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU GLY C -5 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU ILE C -4 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU ASP C -3 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU PRO C -2 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU PHE C -1 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU THR C 0 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU GLY D -5 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU ILE D -4 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU ASP D -3 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU PRO D -2 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU PHE D -1 UNP Q9JZR4 EXPRESSION TAG
SEQADV 3FLU THR D 0 UNP Q9JZR4 EXPRESSION TAG
SEQRES 1 A 297 GLY ILE ASP PRO PHE THR MET LEU GLN GLY SER LEU VAL
SEQRES 2 A 297 ALA LEU ILE THR PRO MET ASN GLN ASP GLY SER ILE HIS
SEQRES 3 A 297 TYR GLU GLN LEU ARG ASP LEU ILE ASP TRP HIS ILE GLU
SEQRES 4 A 297 ASN GLY THR ASP GLY ILE VAL ALA VAL GLY THR THR GLY
SEQRES 5 A 297 GLU SER ALA THR LEU SER VAL GLU GLU HIS THR ALA VAL
SEQRES 6 A 297 ILE GLU ALA VAL VAL LYS HIS VAL ALA LYS ARG VAL PRO
SEQRES 7 A 297 VAL ILE ALA GLY THR GLY ALA ASN ASN THR VAL GLU ALA
SEQRES 8 A 297 ILE ALA LEU SER GLN ALA ALA GLU LYS ALA GLY ALA ASP
SEQRES 9 A 297 TYR THR LEU SER VAL VAL PRO TYR TYR ASN LYS PRO SER
SEQRES 10 A 297 GLN GLU GLY ILE TYR GLN HIS PHE LYS THR ILE ALA GLU
SEQRES 11 A 297 ALA THR SER ILE PRO MET ILE ILE TYR ASN VAL PRO GLY
SEQRES 12 A 297 ARG THR VAL VAL SER MET THR ASN ASP THR ILE LEU ARG
SEQRES 13 A 297 LEU ALA GLU ILE PRO ASN ILE VAL GLY VAL LYS GLU ALA
SEQRES 14 A 297 SER GLY ASN ILE GLY SER ASN ILE GLU LEU ILE ASN ARG
SEQRES 15 A 297 ALA PRO GLU GLY PHE VAL VAL LEU SER GLY ASP ASP HIS
SEQRES 16 A 297 THR ALA LEU PRO PHE MET LEU CYS GLY GLY HIS GLY VAL
SEQRES 17 A 297 ILE THR VAL ALA ALA ASN ALA ALA PRO LYS LEU PHE ALA
SEQRES 18 A 297 ASP MET CYS ARG ALA ALA LEU GLN GLY ASP ILE ALA LEU
SEQRES 19 A 297 ALA ARG GLU LEU ASN ASP ARG LEU ILE PRO ILE TYR ASP
SEQRES 20 A 297 THR MET PHE CYS GLU PRO SER PRO ALA ALA PRO LYS TRP
SEQRES 21 A 297 ALA VAL SER ALA LEU GLY ARG CYS GLU PRO HIS VAL ARG
SEQRES 22 A 297 LEU PRO LEU VAL PRO LEU THR GLU ASN GLY GLN ALA LYS
SEQRES 23 A 297 VAL ARG ALA ALA LEU LYS ALA SER GLY GLN LEU
SEQRES 1 B 297 GLY ILE ASP PRO PHE THR MET LEU GLN GLY SER LEU VAL
SEQRES 2 B 297 ALA LEU ILE THR PRO MET ASN GLN ASP GLY SER ILE HIS
SEQRES 3 B 297 TYR GLU GLN LEU ARG ASP LEU ILE ASP TRP HIS ILE GLU
SEQRES 4 B 297 ASN GLY THR ASP GLY ILE VAL ALA VAL GLY THR THR GLY
SEQRES 5 B 297 GLU SER ALA THR LEU SER VAL GLU GLU HIS THR ALA VAL
SEQRES 6 B 297 ILE GLU ALA VAL VAL LYS HIS VAL ALA LYS ARG VAL PRO
SEQRES 7 B 297 VAL ILE ALA GLY THR GLY ALA ASN ASN THR VAL GLU ALA
SEQRES 8 B 297 ILE ALA LEU SER GLN ALA ALA GLU LYS ALA GLY ALA ASP
SEQRES 9 B 297 TYR THR LEU SER VAL VAL PRO TYR TYR ASN LYS PRO SER
SEQRES 10 B 297 GLN GLU GLY ILE TYR GLN HIS PHE LYS THR ILE ALA GLU
SEQRES 11 B 297 ALA THR SER ILE PRO MET ILE ILE TYR ASN VAL PRO GLY
SEQRES 12 B 297 ARG THR VAL VAL SER MET THR ASN ASP THR ILE LEU ARG
SEQRES 13 B 297 LEU ALA GLU ILE PRO ASN ILE VAL GLY VAL LYS GLU ALA
SEQRES 14 B 297 SER GLY ASN ILE GLY SER ASN ILE GLU LEU ILE ASN ARG
SEQRES 15 B 297 ALA PRO GLU GLY PHE VAL VAL LEU SER GLY ASP ASP HIS
SEQRES 16 B 297 THR ALA LEU PRO PHE MET LEU CYS GLY GLY HIS GLY VAL
SEQRES 17 B 297 ILE THR VAL ALA ALA ASN ALA ALA PRO LYS LEU PHE ALA
SEQRES 18 B 297 ASP MET CYS ARG ALA ALA LEU GLN GLY ASP ILE ALA LEU
SEQRES 19 B 297 ALA ARG GLU LEU ASN ASP ARG LEU ILE PRO ILE TYR ASP
SEQRES 20 B 297 THR MET PHE CYS GLU PRO SER PRO ALA ALA PRO LYS TRP
SEQRES 21 B 297 ALA VAL SER ALA LEU GLY ARG CYS GLU PRO HIS VAL ARG
SEQRES 22 B 297 LEU PRO LEU VAL PRO LEU THR GLU ASN GLY GLN ALA LYS
SEQRES 23 B 297 VAL ARG ALA ALA LEU LYS ALA SER GLY GLN LEU
SEQRES 1 C 297 GLY ILE ASP PRO PHE THR MET LEU GLN GLY SER LEU VAL
SEQRES 2 C 297 ALA LEU ILE THR PRO MET ASN GLN ASP GLY SER ILE HIS
SEQRES 3 C 297 TYR GLU GLN LEU ARG ASP LEU ILE ASP TRP HIS ILE GLU
SEQRES 4 C 297 ASN GLY THR ASP GLY ILE VAL ALA VAL GLY THR THR GLY
SEQRES 5 C 297 GLU SER ALA THR LEU SER VAL GLU GLU HIS THR ALA VAL
SEQRES 6 C 297 ILE GLU ALA VAL VAL LYS HIS VAL ALA LYS ARG VAL PRO
SEQRES 7 C 297 VAL ILE ALA GLY THR GLY ALA ASN ASN THR VAL GLU ALA
SEQRES 8 C 297 ILE ALA LEU SER GLN ALA ALA GLU LYS ALA GLY ALA ASP
SEQRES 9 C 297 TYR THR LEU SER VAL VAL PRO TYR TYR ASN LYS PRO SER
SEQRES 10 C 297 GLN GLU GLY ILE TYR GLN HIS PHE LYS THR ILE ALA GLU
SEQRES 11 C 297 ALA THR SER ILE PRO MET ILE ILE TYR ASN VAL PRO GLY
SEQRES 12 C 297 ARG THR VAL VAL SER MET THR ASN ASP THR ILE LEU ARG
SEQRES 13 C 297 LEU ALA GLU ILE PRO ASN ILE VAL GLY VAL LYS GLU ALA
SEQRES 14 C 297 SER GLY ASN ILE GLY SER ASN ILE GLU LEU ILE ASN ARG
SEQRES 15 C 297 ALA PRO GLU GLY PHE VAL VAL LEU SER GLY ASP ASP HIS
SEQRES 16 C 297 THR ALA LEU PRO PHE MET LEU CYS GLY GLY HIS GLY VAL
SEQRES 17 C 297 ILE THR VAL ALA ALA ASN ALA ALA PRO LYS LEU PHE ALA
SEQRES 18 C 297 ASP MET CYS ARG ALA ALA LEU GLN GLY ASP ILE ALA LEU
SEQRES 19 C 297 ALA ARG GLU LEU ASN ASP ARG LEU ILE PRO ILE TYR ASP
SEQRES 20 C 297 THR MET PHE CYS GLU PRO SER PRO ALA ALA PRO LYS TRP
SEQRES 21 C 297 ALA VAL SER ALA LEU GLY ARG CYS GLU PRO HIS VAL ARG
SEQRES 22 C 297 LEU PRO LEU VAL PRO LEU THR GLU ASN GLY GLN ALA LYS
SEQRES 23 C 297 VAL ARG ALA ALA LEU LYS ALA SER GLY GLN LEU
SEQRES 1 D 297 GLY ILE ASP PRO PHE THR MET LEU GLN GLY SER LEU VAL
SEQRES 2 D 297 ALA LEU ILE THR PRO MET ASN GLN ASP GLY SER ILE HIS
SEQRES 3 D 297 TYR GLU GLN LEU ARG ASP LEU ILE ASP TRP HIS ILE GLU
SEQRES 4 D 297 ASN GLY THR ASP GLY ILE VAL ALA VAL GLY THR THR GLY
SEQRES 5 D 297 GLU SER ALA THR LEU SER VAL GLU GLU HIS THR ALA VAL
SEQRES 6 D 297 ILE GLU ALA VAL VAL LYS HIS VAL ALA LYS ARG VAL PRO
SEQRES 7 D 297 VAL ILE ALA GLY THR GLY ALA ASN ASN THR VAL GLU ALA
SEQRES 8 D 297 ILE ALA LEU SER GLN ALA ALA GLU LYS ALA GLY ALA ASP
SEQRES 9 D 297 TYR THR LEU SER VAL VAL PRO TYR TYR ASN LYS PRO SER
SEQRES 10 D 297 GLN GLU GLY ILE TYR GLN HIS PHE LYS THR ILE ALA GLU
SEQRES 11 D 297 ALA THR SER ILE PRO MET ILE ILE TYR ASN VAL PRO GLY
SEQRES 12 D 297 ARG THR VAL VAL SER MET THR ASN ASP THR ILE LEU ARG
SEQRES 13 D 297 LEU ALA GLU ILE PRO ASN ILE VAL GLY VAL LYS GLU ALA
SEQRES 14 D 297 SER GLY ASN ILE GLY SER ASN ILE GLU LEU ILE ASN ARG
SEQRES 15 D 297 ALA PRO GLU GLY PHE VAL VAL LEU SER GLY ASP ASP HIS
SEQRES 16 D 297 THR ALA LEU PRO PHE MET LEU CYS GLY GLY HIS GLY VAL
SEQRES 17 D 297 ILE THR VAL ALA ALA ASN ALA ALA PRO LYS LEU PHE ALA
SEQRES 18 D 297 ASP MET CYS ARG ALA ALA LEU GLN GLY ASP ILE ALA LEU
SEQRES 19 D 297 ALA ARG GLU LEU ASN ASP ARG LEU ILE PRO ILE TYR ASP
SEQRES 20 D 297 THR MET PHE CYS GLU PRO SER PRO ALA ALA PRO LYS TRP
SEQRES 21 D 297 ALA VAL SER ALA LEU GLY ARG CYS GLU PRO HIS VAL ARG
SEQRES 22 D 297 LEU PRO LEU VAL PRO LEU THR GLU ASN GLY GLN ALA LYS
SEQRES 23 D 297 VAL ARG ALA ALA LEU LYS ALA SER GLY GLN LEU
HET SO4 A 292 5
HET SO4 A 293 5
HET SO4 A 294 5
HET SO4 A 295 5
HET SO4 A 296 5
HET GOL A 297 6
HET GOL A 298 6
HET GOL A 299 6
HET GOL A 300 6
HET GOL A 301 6
HET GOL A 302 6
HET GOL A 303 6
HET SO4 B 292 5
HET SO4 B 293 5
HET SO4 B 294 5
HET SO4 B 295 5
HET GOL B 296 6
HET GOL B 297 6
HET GOL B 298 6
HET GOL B 299 6
HET GOL B 300 6
HET GOL B 301 6
HET SO4 C 292 5
HET SO4 C 293 5
HET SO4 C 294 5
HET SO4 C 295 5
HET SO4 C 296 5
HET SO4 C 297 5
HET GOL C 298 6
HET GOL C 299 6
HET GOL C 300 6
HET GOL C 301 6
HET GOL C 302 6
HET GOL C 303 6
HET GOL C 304 6
HET GOL C 305 6
HET SO4 D 292 5
HET SO4 D 293 5
HET SO4 D 294 5
HET GOL D 295 6
HET GOL D 296 6
HET GOL D 297 6
HET GOL D 298 6
HET GOL D 299 6
HET GOL D 300 6
HET GOL D 301 6
HET GOL D 302 6
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 SO4 18(O4 S 2-)
FORMUL 10 GOL 29(C3 H8 O3)
FORMUL 52 HOH *938(H2 O)
HELIX 1 1 HIS A 20 ASN A 34 1 15
HELIX 2 2 GLU A 47 LEU A 51 5 5
HELIX 3 3 SER A 52 ALA A 68 1 17
HELIX 4 4 ASN A 81 ALA A 95 1 15
HELIX 5 5 SER A 111 THR A 126 1 16
HELIX 6 6 VAL A 135 VAL A 140 1 6
HELIX 7 7 THR A 144 ALA A 152 1 9
HELIX 8 8 ASN A 166 ALA A 177 1 12
HELIX 9 9 ASP A 187 HIS A 189 5 3
HELIX 10 10 THR A 190 CYS A 197 1 8
HELIX 11 11 VAL A 205 ALA A 209 5 5
HELIX 12 12 ALA A 210 GLY A 224 1 15
HELIX 13 13 ASP A 225 ASP A 241 1 17
HELIX 14 14 PRO A 249 LEU A 259 1 11
HELIX 15 15 THR A 274 SER A 288 1 15
HELIX 16 16 HIS B 20 GLY B 35 1 16
HELIX 17 17 SER B 52 ALA B 68 1 17
HELIX 18 18 ASN B 81 ALA B 95 1 15
HELIX 19 19 SER B 111 THR B 126 1 16
HELIX 20 20 VAL B 135 VAL B 140 1 6
HELIX 21 21 THR B 144 ALA B 152 1 9
HELIX 22 22 ASN B 166 ALA B 177 1 12
HELIX 23 23 ASP B 187 HIS B 189 5 3
HELIX 24 24 THR B 190 CYS B 197 1 8
HELIX 25 25 VAL B 205 ALA B 209 5 5
HELIX 26 26 ALA B 210 GLN B 223 1 14
HELIX 27 27 ASP B 225 ASP B 241 1 17
HELIX 28 28 PRO B 249 LEU B 259 1 11
HELIX 29 29 THR B 274 SER B 288 1 15
HELIX 30 30 HIS C 20 ASN C 34 1 15
HELIX 31 31 GLU C 47 LEU C 51 5 5
HELIX 32 32 SER C 52 ALA C 68 1 17
HELIX 33 33 ASN C 81 GLY C 96 1 16
HELIX 34 34 SER C 111 THR C 126 1 16
HELIX 35 35 VAL C 135 VAL C 140 1 6
HELIX 36 36 THR C 144 ALA C 152 1 9
HELIX 37 37 ASN C 166 ALA C 177 1 12
HELIX 38 38 ASP C 187 HIS C 189 5 3
HELIX 39 39 THR C 190 CYS C 197 1 8
HELIX 40 40 VAL C 205 ALA C 209 5 5
HELIX 41 41 ALA C 210 GLN C 223 1 14
HELIX 42 42 ASP C 225 ASP C 241 1 17
HELIX 43 43 PRO C 249 LEU C 259 1 11
HELIX 44 44 THR C 274 SER C 288 1 15
HELIX 45 45 HIS D 20 ASN D 34 1 15
HELIX 46 46 GLU D 47 LEU D 51 5 5
HELIX 47 47 SER D 52 ALA D 68 1 17
HELIX 48 48 ASN D 81 GLY D 96 1 16
HELIX 49 49 SER D 111 ALA D 125 1 15
HELIX 50 50 VAL D 135 VAL D 140 1 6
HELIX 51 51 THR D 144 ALA D 152 1 9
HELIX 52 52 ASN D 166 ALA D 177 1 12
HELIX 53 53 ASP D 187 HIS D 189 5 3
HELIX 54 54 THR D 190 CYS D 197 1 8
HELIX 55 55 VAL D 205 ALA D 209 5 5
HELIX 56 56 ALA D 210 GLY D 224 1 15
HELIX 57 57 ASP D 225 ASP D 241 1 17
HELIX 58 58 PRO D 249 LEU D 259 1 11
HELIX 59 59 THR D 274 SER D 288 1 15
SHEET 1 A 9 GLY A 4 ALA A 8 0
SHEET 2 A 9 GLY A 38 ALA A 41 1 O VAL A 40 N VAL A 7
SHEET 3 A 9 VAL A 73 GLY A 76 1 O ILE A 74 N ILE A 39
SHEET 4 A 9 TYR A 99 VAL A 103 1 O TYR A 99 N ALA A 75
SHEET 5 A 9 MET A 130 ASN A 134 1 O ILE A 131 N THR A 100
SHEET 6 A 9 ILE A 157 GLU A 162 1 O LYS A 161 N ILE A 132
SHEET 7 A 9 VAL A 182 SER A 185 1 O LEU A 184 N VAL A 160
SHEET 8 A 9 GLY A 201 THR A 204 1 O ILE A 203 N SER A 185
SHEET 9 A 9 GLY A 4 ALA A 8 1 N LEU A 6 O VAL A 202
SHEET 1 B 9 GLY B 4 ALA B 8 0
SHEET 2 B 9 GLY B 38 ALA B 41 1 O VAL B 40 N VAL B 7
SHEET 3 B 9 VAL B 73 GLY B 76 1 O GLY B 76 N ALA B 41
SHEET 4 B 9 TYR B 99 VAL B 103 1 O TYR B 99 N ALA B 75
SHEET 5 B 9 MET B 130 ASN B 134 1 O ILE B 131 N THR B 100
SHEET 6 B 9 ILE B 157 GLU B 162 1 O LYS B 161 N ILE B 132
SHEET 7 B 9 VAL B 182 SER B 185 1 O LEU B 184 N VAL B 160
SHEET 8 B 9 GLY B 201 THR B 204 1 O ILE B 203 N SER B 185
SHEET 9 B 9 GLY B 4 ALA B 8 1 N LEU B 6 O VAL B 202
SHEET 1 C 9 GLY C 4 ALA C 8 0
SHEET 2 C 9 GLY C 38 ALA C 41 1 O VAL C 40 N VAL C 7
SHEET 3 C 9 VAL C 73 GLY C 76 1 O GLY C 76 N ALA C 41
SHEET 4 C 9 TYR C 99 VAL C 103 1 O TYR C 99 N ALA C 75
SHEET 5 C 9 MET C 130 ASN C 134 1 O ILE C 131 N SER C 102
SHEET 6 C 9 ILE C 157 GLU C 162 1 O LYS C 161 N ILE C 132
SHEET 7 C 9 VAL C 182 SER C 185 1 O LEU C 184 N VAL C 160
SHEET 8 C 9 GLY C 201 THR C 204 1 O ILE C 203 N SER C 185
SHEET 9 C 9 GLY C 4 ALA C 8 1 N ALA C 8 O THR C 204
SHEET 1 D 9 GLY D 4 ALA D 8 0
SHEET 2 D 9 GLY D 38 ALA D 41 1 O VAL D 40 N VAL D 7
SHEET 3 D 9 VAL D 73 GLY D 76 1 O ILE D 74 N ALA D 41
SHEET 4 D 9 TYR D 99 VAL D 103 1 O TYR D 99 N ALA D 75
SHEET 5 D 9 MET D 130 ASN D 134 1 O ILE D 131 N THR D 100
SHEET 6 D 9 ILE D 157 GLU D 162 1 O LYS D 161 N ILE D 132
SHEET 7 D 9 VAL D 182 SER D 185 1 O LEU D 184 N VAL D 160
SHEET 8 D 9 GLY D 201 THR D 204 1 O ILE D 203 N SER D 185
SHEET 9 D 9 GLY D 4 ALA D 8 1 N LEU D 6 O VAL D 202
CISPEP 1 SER A 248 PRO A 249 0 6.76
CISPEP 2 LEU A 268 PRO A 269 0 14.97
CISPEP 3 SER B 248 PRO B 249 0 9.33
CISPEP 4 LEU B 268 PRO B 269 0 18.66
CISPEP 5 SER C 248 PRO C 249 0 11.36
CISPEP 6 LEU C 268 PRO C 269 0 15.17
CISPEP 7 SER D 248 PRO D 249 0 11.49
CISPEP 8 LEU D 268 PRO D 269 0 12.32
SITE 1 AC1 9 ASN A 80 TYR A 106 GOL A 298 HOH A 309
SITE 2 AC1 9 HOH A 452 HOH A 891 ASN B 80 TYR B 106
SITE 3 AC1 9 GOL B 297
SITE 1 AC2 6 TYR A 133 ARG A 138 GLY A 186 PHE A 244
SITE 2 AC2 6 SO4 A 294 HOH A 384
SITE 1 AC3 9 ALA A 8 GLY A 43 THR A 44 THR A 45
SITE 2 AC3 9 LEU A 101 TYR A 133 LYS A 161 ILE A 203
SITE 3 AC3 9 SO4 A 293
SITE 1 AC4 4 LEU A 213 ARG A 235 GLN A 290 HOH A 378
SITE 1 AC5 3 HIS A 189 HOH A 415 HOH A 873
SITE 1 AC6 6 ILE A 19 HIS A 20 TYR A 21 GLU A 22
SITE 2 AC6 6 ARG A 25 HOH A 317
SITE 1 AC7 10 SER A 48 ALA A 49 TYR A 106 SO4 A 292
SITE 2 AC7 10 HOH A 361 HOH A 362 HOH A 363 HOH A 509
SITE 3 AC7 10 ASN B 80 TYR B 107
SITE 1 AC8 6 TRP A 30 ASN A 34 PRO A 211 LYS A 212
SITE 2 AC8 6 HOH A 787 HOH A 796
SITE 1 AC9 1 SER A 257
SITE 1 BC1 6 ASN A 14 GLN A 15 GLU A 263 HIS A 265
SITE 2 BC1 6 ASP C 29 HIS C 66
SITE 1 BC2 5 SER A 111 GLN A 112 HOH A 364 HOH A 368
SITE 2 BC2 5 HOH A 624
SITE 1 BC3 5 THR A 144 ASN A 145 ASP A 146 SER A 169
SITE 2 BC3 5 HOH A 772
SITE 1 BC4 5 MET B 1 GLU B 179 GLY B 180 HIS B 200
SITE 2 BC4 5 HOH B 398
SITE 1 BC5 9 ALA B 8 GLY B 43 THR B 44 THR B 45
SITE 2 BC5 9 LEU B 101 TYR B 133 LYS B 161 ILE B 203
SITE 3 BC5 9 SO4 B 295
SITE 1 BC6 2 HIS B 189 HOH B 363
SITE 1 BC7 5 TYR B 133 ARG B 138 GLY B 186 PHE B 244
SITE 2 BC7 5 SO4 B 293
SITE 1 BC8 6 GLU A 275 HOH A 645 TRP B 254 SER B 257
SITE 2 BC8 6 ALA B 258 PRO B 264
SITE 1 BC9 10 ASN A 80 TYR A 107 SO4 A 292 SER B 48
SITE 2 BC9 10 ALA B 49 TYR B 106 HOH B 302 HOH B 304
SITE 3 BC9 10 HOH B 351 HOH B 705
SITE 1 CC1 5 ARG B 230 GLU B 231 ASP B 234 HOH B 447
SITE 2 CC1 5 ASN D 175
SITE 1 CC2 7 LYS A 286 HOH A 329 TRP B 30 ARG B 261
SITE 2 CC2 7 HOH B 395 HOH B 518 HOH B 570
SITE 1 CC3 6 SER B 111 GLN B 112 HOH B 357 HOH B 358
SITE 2 CC3 6 HOH B 614 HOH B 644
SITE 1 CC4 4 THR B 144 ASN B 145 ASP B 146 SER B 169
SITE 1 CC5 5 THR C 144 ASN C 145 SER C 169 HOH C 330
SITE 2 CC5 5 HOH C 352
SITE 1 CC6 8 ASN C 80 TYR C 106 GOL C 298 HOH C 315
SITE 2 CC6 8 ASN D 80 TYR D 106 GOL D 295 HOH D 369
SITE 1 CC7 10 ALA C 8 GLY C 43 THR C 44 THR C 45
SITE 2 CC7 10 LEU C 101 TYR C 133 LYS C 161 ILE C 203
SITE 3 CC7 10 SO4 C 297 GOL C 303
SITE 1 CC8 3 GLY C 180 HIS C 200 HOH C 367
SITE 1 CC9 4 HIS C 189 PHE C 244 HOH C 397 HOH C 723
SITE 1 DC1 6 TYR C 133 ARG C 138 LYS C 161 PHE C 244
SITE 2 DC1 6 SO4 C 294 HOH C 321
SITE 1 DC2 9 SER C 48 ALA C 49 GLY C 78 TYR C 106
SITE 2 DC2 9 SO4 C 293 GOL C 303 HOH C 946 ASN D 80
SITE 3 DC2 9 TYR D 107
SITE 1 DC3 2 TRP C 254 SER C 257
SITE 1 DC4 7 GLU B 22 ARG B 25 HOH B 487 ASN C 145
SITE 2 DC4 7 ASP C 146 LEU C 149 GLU C 172
SITE 1 DC5 3 THR C 274 GLU C 275 ASN C 276
SITE 1 DC6 5 TRP C 30 ASN C 34 PRO C 211 LYS C 212
SITE 2 DC6 5 HOH C 362
SITE 1 DC7 14 VAL C 42 GLY C 43 THR C 44 SER C 48
SITE 2 DC7 14 GLY C 76 THR C 77 GLY C 78 LEU C 101
SITE 3 DC7 14 SER C 102 VAL C 103 SO4 C 294 GOL C 298
SITE 4 DC7 14 HOH C 358 TYR D 107
SITE 1 DC8 4 LYS C 109 SO4 D 292 SO4 D 294 HOH D 379
SITE 1 DC9 5 SER C 111 GLN C 112 HOH C 369 HOH C 603
SITE 2 DC9 5 HOH C 765
SITE 1 EC1 8 GOL C 304 TYR D 133 VAL D 135 ARG D 138
SITE 2 EC1 8 ALA D 163 GLY D 186 PHE D 244 SO4 D 293
SITE 1 EC2 10 ALA D 8 GLY D 43 THR D 44 THR D 45
SITE 2 EC2 10 LEU D 101 TYR D 133 LYS D 161 ILE D 203
SITE 3 EC2 10 SO4 D 292 GOL D 296
SITE 1 EC3 4 GOL C 304 HIS D 189 HOH D 322 HOH D 872
SITE 1 EC4 9 ASN C 80 SO4 C 293 SER D 48 ALA D 49
SITE 2 EC4 9 GLY D 78 TYR D 106 GOL D 296 HOH D 685
SITE 3 EC4 9 HOH D 943
SITE 1 EC5 14 TYR C 107 VAL D 42 GLY D 43 THR D 44
SITE 2 EC5 14 SER D 48 GLY D 76 THR D 77 GLY D 78
SITE 3 EC5 14 LEU D 101 SER D 102 VAL D 103 SO4 D 293
SITE 4 EC5 14 GOL D 295 HOH D 685
SITE 1 EC6 5 HIS D 20 TYR D 21 GLU D 22 ARG D 25
SITE 2 EC6 5 HOH D 629
SITE 1 EC7 7 HIS B 189 ASP B 241 HOH B 392 ASN D 166
SITE 2 EC7 7 GLY D 168 SER D 169 GLU D 172
SITE 1 EC8 5 GLN A 90 TRP D 254 SER D 257 PRO D 264
SITE 2 EC8 5 HOH D 648
SITE 1 EC9 5 ASN D 14 GLN D 15 GLU D 263 HIS D 265
SITE 2 EC9 5 HOH D 802
SITE 1 FC1 4 THR D 144 ASN D 145 ASP D 146 SER D 169
SITE 1 FC2 6 SER D 111 GLN D 112 HOH D 331 HOH D 364
SITE 2 FC2 6 HOH D 686 HOH D 747
CRYST1 80.667 115.684 132.122 90.00 90.00 90.00 P 21 21 21 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012397 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008644 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007569 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
