HEADER HYDROLASE 12-MAY-13 4BN0
TITLE STRUCTURE OF FUTALOSINE HYDROLASE MUTANT OF HELICOBACTER PYLORI STRAIN
TITLE 2 26695
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MTA/SAH NUCLEOSIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: 5-METHYLTHIOADENOSINE NUCLEOSIDASE, S-ADENOSYLHOMOCYSTEINE
COMPND 5 NUCLEOSIDASE, FUTALOSINE HYDROLASE;
COMPND 6 EC: 3.2.2.9;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;
SOURCE 3 ORGANISM_TAXID: 85962;
SOURCE 4 STRAIN: 26695;
SOURCE 5 ATCC: 700392;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET28A
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.Q.KIM,W.A.OFFEN,K.A.STUBBS,G.J.DAVIES
REVDAT 4 20-DEC-23 4BN0 1 SHEET
REVDAT 3 22-JAN-14 4BN0 1 JRNL
REVDAT 2 15-JAN-14 4BN0 1 JRNL
REVDAT 1 11-SEP-13 4BN0 0
JRNL AUTH R.Q.KIM,W.A.OFFEN,G.J.DAVIES,K.A.STUBBS
JRNL TITL STRUCTURAL ENZYMOLOGY OF HELICOBACTER PYLORI
JRNL TITL 2 METHYLTHIOADENOSINE NUCLEOSIDASE IN THE FUTALOSINE PATHWAY
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 177 2014
JRNL REFN ISSN 0907-4449
JRNL PMID 24419390
JRNL DOI 10.1107/S1399004713026655
REMARK 2
REMARK 2 RESOLUTION. 2.11 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 2.11
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 48768
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2425
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) : 2.11
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.17
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3551
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.2820
REMARK 3 BIN FREE R VALUE SET COUNT : 161
REMARK 3 BIN FREE R VALUE : 0.3530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6689
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 165
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.66800
REMARK 3 B22 (A**2) : 0.54500
REMARK 3 B33 (A**2) : -1.07500
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.16200
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.275
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.220
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.177
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.433
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6799 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6636 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9191 ; 1.718 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15249 ; 0.901 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 881 ; 6.408 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 263 ;36.616 ;25.323
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1170 ;16.882 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;20.808 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1107 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7648 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1476 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1357 ; 0.222 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 32 ; 0.162 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3185 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 118 ; 0.142 ; 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): 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): 3547 ; 0.723 ; 0.889
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3546 ; 0.723 ; 0.888
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4419 ; 1.258 ; 1.324
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3252 ; 0.726 ; 0.976
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4772 ; 1.217 ; 1.439
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 0 A 231
REMARK 3 ORIGIN FOR THE GROUP (A): 26.5040 15.8160 6.8550
REMARK 3 T TENSOR
REMARK 3 T11: 0.1877 T22: 0.2907
REMARK 3 T33: 0.0751 T12: -0.0117
REMARK 3 T13: -0.0042 T23: 0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 0.2622 L22: 0.4497
REMARK 3 L33: 1.3039 L12: 0.3235
REMARK 3 L13: 0.1130 L23: -0.0391
REMARK 3 S TENSOR
REMARK 3 S11: 0.0354 S12: -0.0011 S13: 0.0069
REMARK 3 S21: 0.0299 S22: -0.0008 S23: 0.0550
REMARK 3 S31: -0.0617 S32: 0.2017 S33: -0.0346
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 231
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8110 -0.4730 -9.0770
REMARK 3 T TENSOR
REMARK 3 T11: 0.2167 T22: 0.2800
REMARK 3 T33: 0.0591 T12: -0.0416
REMARK 3 T13: 0.0106 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 1.3180 L22: 0.3930
REMARK 3 L33: 1.4634 L12: 0.3426
REMARK 3 L13: -0.4366 L23: 0.5151
REMARK 3 S TENSOR
REMARK 3 S11: -0.1051 S12: 0.1776 S13: 0.0347
REMARK 3 S21: 0.0514 S22: -0.0242 S23: 0.0607
REMARK 3 S31: 0.1925 S32: -0.1891 S33: 0.1292
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C -1 C 231
REMARK 3 ORIGIN FOR THE GROUP (A): -4.3760 11.1070 35.6760
REMARK 3 T TENSOR
REMARK 3 T11: 0.1577 T22: 0.5021
REMARK 3 T33: 0.1093 T12: -0.0723
REMARK 3 T13: -0.0049 T23: -0.0776
REMARK 3 L TENSOR
REMARK 3 L11: 0.5551 L22: 0.0544
REMARK 3 L33: 1.6917 L12: 0.0995
REMARK 3 L13: -0.1985 L23: -0.0608
REMARK 3 S TENSOR
REMARK 3 S11: -0.1200 S12: 0.0667 S13: -0.0308
REMARK 3 S21: -0.0114 S22: 0.0539 S23: -0.0681
REMARK 3 S31: 0.0595 S32: -0.6377 S33: 0.0661
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 2 D 231
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6610 6.7050 53.3590
REMARK 3 T TENSOR
REMARK 3 T11: 0.2259 T22: 0.3279
REMARK 3 T33: 0.0077 T12: 0.0004
REMARK 3 T13: 0.0013 T23: -0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 0.5531 L22: 0.0932
REMARK 3 L33: 1.5277 L12: 0.2034
REMARK 3 L13: 0.0596 L23: -0.1432
REMARK 3 S TENSOR
REMARK 3 S11: 0.0043 S12: -0.0630 S13: 0.0316
REMARK 3 S21: -0.0019 S22: -0.0363 S23: 0.0081
REMARK 3 S31: 0.1302 S32: 0.1254 S33: 0.0320
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 4BN0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1290056801.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9163
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48788
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.110
REMARK 200 RESOLUTION RANGE LOW (A) : 39.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 6.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.11
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: PDB ENTRY 4BMX
REMARK 200
REMARK 200 REMARK: A BATCH OF BAD QUALITY IMAGES WAS REMOVED
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 25% PEG-3350, 0.2
REMARK 280 M NACL
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 37.84500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 ALA A 201
REMARK 465 ASP A 202
REMARK 465 GLU A 203
REMARK 465 GLU A 204
REMARK 465 ALA A 205
REMARK 465 ASN A 206
REMARK 465 MET A 207
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ALA B 201
REMARK 465 ASP B 202
REMARK 465 GLU B 203
REMARK 465 GLU B 204
REMARK 465 ALA B 205
REMARK 465 ASN B 206
REMARK 465 MET B 207
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 ASP C 199
REMARK 465 ASN C 200
REMARK 465 ALA C 201
REMARK 465 ASP C 202
REMARK 465 GLU C 203
REMARK 465 GLU C 204
REMARK 465 ALA C 205
REMARK 465 ASN C 206
REMARK 465 MET C 207
REMARK 465 SER C 208
REMARK 465 PHE C 209
REMARK 465 ASP C 210
REMARK 465 ALA C 211
REMARK 465 PHE C 212
REMARK 465 LEU C 213
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 ALA D 201
REMARK 465 ASP D 202
REMARK 465 GLU D 203
REMARK 465 GLU D 204
REMARK 465 ALA D 205
REMARK 465 ASN D 206
REMARK 465 MET D 207
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 ASP A 25 CG OD1 OD2
REMARK 470 LYS A 85 CE NZ
REMARK 470 GLU A 126 CG CD OE1 OE2
REMARK 470 GLU A 138 CG CD OE1 OE2
REMARK 470 LYS A 158 CD CE NZ
REMARK 470 GLU A 159 CG CD OE1 OE2
REMARK 470 LYS A 169 CD CE NZ
REMARK 470 SER A 208 OG
REMARK 470 GLU A 214 CD OE1 OE2
REMARK 470 LYS A 215 CD CE NZ
REMARK 470 LYS B 85 CG CD CE NZ
REMARK 470 LYS B 88 CG CD CE NZ
REMARK 470 GLU B 126 CG CD OE1 OE2
REMARK 470 LYS B 133 CE NZ
REMARK 470 GLU B 138 CG CD OE1 OE2
REMARK 470 LYS B 158 CG CD CE NZ
REMARK 470 ASN B 200 CG OD1 ND2
REMARK 470 PHE B 212 CE2
REMARK 470 LEU B 213 CG CD1 CD2
REMARK 470 GLU B 214 O
REMARK 470 LYS B 215 CD CE NZ
REMARK 470 LYS B 222 CD CE NZ
REMARK 470 LYS C 85 CD CE NZ
REMARK 470 GLU C 126 CG CD OE1 OE2
REMARK 470 GLU C 138 CG CD OE1 OE2
REMARK 470 HIS C 140 CG ND1 CD2 CE1 NE2
REMARK 470 LYS C 158 CG CD CE NZ
REMARK 470 GLU C 159 CG CD OE1 OE2
REMARK 470 LYS C 169 CD CE NZ
REMARK 470 GLU C 214 CG CD OE1 OE2
REMARK 470 LYS C 215 CG CD CE NZ
REMARK 470 GLN C 218 CG CD OE1 NE2
REMARK 470 GLN D 3 CG CD OE1 NE2
REMARK 470 ASN D 43 CG OD1 ND2
REMARK 470 LYS D 85 CD CE NZ
REMARK 470 LYS D 88 CG CD CE NZ
REMARK 470 GLU D 126 CG CD OE1 OE2
REMARK 470 LYS D 133 CE NZ
REMARK 470 GLU D 138 CG CD OE1 OE2
REMARK 470 LYS D 169 CD CE NZ
REMARK 470 LYS D 215 CG CD 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 42 -122.77 51.81
REMARK 500 LYS A 52 175.72 63.01
REMARK 500 SER A 118 -149.80 -131.75
REMARK 500 ASP A 199 -158.77 -133.63
REMARK 500 LYS B 52 176.75 70.09
REMARK 500 ASN B 90 -6.04 84.17
REMARK 500 SER B 118 -151.30 -142.24
REMARK 500 ASP B 152 30.00 -89.39
REMARK 500 GLU B 174 -161.61 -161.59
REMARK 500 PHE B 209 -35.47 -161.58
REMARK 500 LEU C 31 134.74 -170.23
REMARK 500 HIS C 42 -123.46 54.34
REMARK 500 LYS C 52 172.39 66.31
REMARK 500 ASN C 90 -11.52 90.12
REMARK 500 SER C 118 -150.68 -134.71
REMARK 500 GLU C 138 21.09 -69.38
REMARK 500 GLN C 139 12.83 -146.81
REMARK 500 HIS C 140 2.15 58.51
REMARK 500 ASP C 152 23.26 -79.91
REMARK 500 GLU C 174 -159.52 -166.67
REMARK 500 LYS D 52 173.97 74.46
REMARK 500 ASN D 90 -8.25 84.85
REMARK 500 SER D 118 -155.73 -126.16
REMARK 500 GLU D 174 -158.60 -159.13
REMARK 500 ASP D 199 -151.58 -167.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BMX RELATED DB: PDB
REMARK 900 NATIVE STRUCTURE OF FUTALOSINE HYDROLASE OF HELICOBACTER PYLORI
REMARK 900 STRAIN 26695
REMARK 900 RELATED ID: 4BMY RELATED DB: PDB
REMARK 900 STRUCTURE OF FUTALOSINE HYDROLASE MUTANT OF HELICOBACTER PYLORI
REMARK 900 STRAIN 26695
REMARK 900 RELATED ID: 4BMZ RELATED DB: PDB
REMARK 900 STRUCTURE OF FUTALOSINE HYDROLASE MUTANT OF HELICOBACTER PYLORI
REMARK 900 STRAIN 26695
DBREF 4BN0 A 1 231 UNP O24915 MTNN_HELPY 1 231
DBREF 4BN0 B 1 231 UNP O24915 MTNN_HELPY 1 231
DBREF 4BN0 C 1 231 UNP O24915 MTNN_HELPY 1 231
DBREF 4BN0 D 1 231 UNP O24915 MTNN_HELPY 1 231
SEQADV 4BN0 MET A -19 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 GLY A -18 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER A -17 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER A -16 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS A -15 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS A -14 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS A -13 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS A -12 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS A -11 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS A -10 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER A -9 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER A -8 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 GLY A -7 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 LEU A -6 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 VAL A -5 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 PRO A -4 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 ARG A -3 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 GLY A -2 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER A -1 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS A 0 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 GLN A 14 UNP O24915 GLU 14 ENGINEERED MUTATION
SEQADV 4BN0 MET B -19 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 GLY B -18 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER B -17 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER B -16 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS B -15 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS B -14 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS B -13 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS B -12 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS B -11 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS B -10 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER B -9 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER B -8 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 GLY B -7 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 LEU B -6 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 VAL B -5 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 PRO B -4 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 ARG B -3 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 GLY B -2 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER B -1 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS B 0 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 GLN B 14 UNP O24915 GLU 14 ENGINEERED MUTATION
SEQADV 4BN0 MET C -19 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 GLY C -18 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER C -17 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER C -16 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS C -15 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS C -14 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS C -13 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS C -12 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS C -11 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS C -10 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER C -9 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER C -8 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 GLY C -7 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 LEU C -6 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 VAL C -5 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 PRO C -4 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 ARG C -3 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 GLY C -2 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER C -1 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS C 0 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 GLN C 14 UNP O24915 GLU 14 ENGINEERED MUTATION
SEQADV 4BN0 MET D -19 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 GLY D -18 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER D -17 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER D -16 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS D -15 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS D -14 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS D -13 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS D -12 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS D -11 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS D -10 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER D -9 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER D -8 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 GLY D -7 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 LEU D -6 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 VAL D -5 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 PRO D -4 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 ARG D -3 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 GLY D -2 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 SER D -1 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 HIS D 0 UNP O24915 EXPRESSION TAG
SEQADV 4BN0 GLN D 14 UNP O24915 GLU 14 ENGINEERED MUTATION
SEQRES 1 A 251 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 251 LEU VAL PRO ARG GLY SER HIS MET VAL GLN LYS ILE GLY
SEQRES 3 A 251 ILE LEU GLY ALA MET ARG GLU GLN ILE THR PRO ILE LEU
SEQRES 4 A 251 GLU LEU PHE GLY VAL ASP PHE GLU GLU ILE PRO LEU GLY
SEQRES 5 A 251 GLY ASN VAL PHE HIS LYS GLY VAL TYR HIS ASN LYS GLU
SEQRES 6 A 251 ILE ILE VAL ALA TYR SER LYS ILE GLY LYS VAL HIS SER
SEQRES 7 A 251 THR LEU THR THR THR SER MET ILE LEU ALA PHE GLY VAL
SEQRES 8 A 251 GLN LYS VAL LEU PHE SER GLY VAL ALA GLY SER LEU VAL
SEQRES 9 A 251 LYS ASP LEU LYS ILE ASN ASP LEU LEU VAL ALA ILE GLN
SEQRES 10 A 251 LEU VAL GLN HIS ASP VAL ASP LEU SER ALA PHE ASP HIS
SEQRES 11 A 251 PRO LEU GLY PHE ILE PRO GLU SER ALA ILE PHE ILE GLU
SEQRES 12 A 251 THR SER GLU SER LEU ASN ALA LEU ALA LYS GLU VAL ALA
SEQRES 13 A 251 ASN GLU GLN HIS ILE VAL LEU LYS GLU GLY VAL ILE ALA
SEQRES 14 A 251 SER GLY ASP GLN PHE VAL HIS SER LYS GLU ARG LYS GLU
SEQRES 15 A 251 PHE LEU VAL SER GLU PHE LYS ALA SER ALA VAL GLU MET
SEQRES 16 A 251 GLU GLY ALA SER VAL ALA PHE VAL CYS GLN LYS PHE GLY
SEQRES 17 A 251 VAL PRO CYS CYS VAL LEU ARG SER ILE SER ASP ASN ALA
SEQRES 18 A 251 ASP GLU GLU ALA ASN MET SER PHE ASP ALA PHE LEU GLU
SEQRES 19 A 251 LYS SER ALA GLN THR SER ALA LYS PHE LEU LYS SER MET
SEQRES 20 A 251 VAL ASP GLU LEU
SEQRES 1 B 251 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 251 LEU VAL PRO ARG GLY SER HIS MET VAL GLN LYS ILE GLY
SEQRES 3 B 251 ILE LEU GLY ALA MET ARG GLU GLN ILE THR PRO ILE LEU
SEQRES 4 B 251 GLU LEU PHE GLY VAL ASP PHE GLU GLU ILE PRO LEU GLY
SEQRES 5 B 251 GLY ASN VAL PHE HIS LYS GLY VAL TYR HIS ASN LYS GLU
SEQRES 6 B 251 ILE ILE VAL ALA TYR SER LYS ILE GLY LYS VAL HIS SER
SEQRES 7 B 251 THR LEU THR THR THR SER MET ILE LEU ALA PHE GLY VAL
SEQRES 8 B 251 GLN LYS VAL LEU PHE SER GLY VAL ALA GLY SER LEU VAL
SEQRES 9 B 251 LYS ASP LEU LYS ILE ASN ASP LEU LEU VAL ALA ILE GLN
SEQRES 10 B 251 LEU VAL GLN HIS ASP VAL ASP LEU SER ALA PHE ASP HIS
SEQRES 11 B 251 PRO LEU GLY PHE ILE PRO GLU SER ALA ILE PHE ILE GLU
SEQRES 12 B 251 THR SER GLU SER LEU ASN ALA LEU ALA LYS GLU VAL ALA
SEQRES 13 B 251 ASN GLU GLN HIS ILE VAL LEU LYS GLU GLY VAL ILE ALA
SEQRES 14 B 251 SER GLY ASP GLN PHE VAL HIS SER LYS GLU ARG LYS GLU
SEQRES 15 B 251 PHE LEU VAL SER GLU PHE LYS ALA SER ALA VAL GLU MET
SEQRES 16 B 251 GLU GLY ALA SER VAL ALA PHE VAL CYS GLN LYS PHE GLY
SEQRES 17 B 251 VAL PRO CYS CYS VAL LEU ARG SER ILE SER ASP ASN ALA
SEQRES 18 B 251 ASP GLU GLU ALA ASN MET SER PHE ASP ALA PHE LEU GLU
SEQRES 19 B 251 LYS SER ALA GLN THR SER ALA LYS PHE LEU LYS SER MET
SEQRES 20 B 251 VAL ASP GLU LEU
SEQRES 1 C 251 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 251 LEU VAL PRO ARG GLY SER HIS MET VAL GLN LYS ILE GLY
SEQRES 3 C 251 ILE LEU GLY ALA MET ARG GLU GLN ILE THR PRO ILE LEU
SEQRES 4 C 251 GLU LEU PHE GLY VAL ASP PHE GLU GLU ILE PRO LEU GLY
SEQRES 5 C 251 GLY ASN VAL PHE HIS LYS GLY VAL TYR HIS ASN LYS GLU
SEQRES 6 C 251 ILE ILE VAL ALA TYR SER LYS ILE GLY LYS VAL HIS SER
SEQRES 7 C 251 THR LEU THR THR THR SER MET ILE LEU ALA PHE GLY VAL
SEQRES 8 C 251 GLN LYS VAL LEU PHE SER GLY VAL ALA GLY SER LEU VAL
SEQRES 9 C 251 LYS ASP LEU LYS ILE ASN ASP LEU LEU VAL ALA ILE GLN
SEQRES 10 C 251 LEU VAL GLN HIS ASP VAL ASP LEU SER ALA PHE ASP HIS
SEQRES 11 C 251 PRO LEU GLY PHE ILE PRO GLU SER ALA ILE PHE ILE GLU
SEQRES 12 C 251 THR SER GLU SER LEU ASN ALA LEU ALA LYS GLU VAL ALA
SEQRES 13 C 251 ASN GLU GLN HIS ILE VAL LEU LYS GLU GLY VAL ILE ALA
SEQRES 14 C 251 SER GLY ASP GLN PHE VAL HIS SER LYS GLU ARG LYS GLU
SEQRES 15 C 251 PHE LEU VAL SER GLU PHE LYS ALA SER ALA VAL GLU MET
SEQRES 16 C 251 GLU GLY ALA SER VAL ALA PHE VAL CYS GLN LYS PHE GLY
SEQRES 17 C 251 VAL PRO CYS CYS VAL LEU ARG SER ILE SER ASP ASN ALA
SEQRES 18 C 251 ASP GLU GLU ALA ASN MET SER PHE ASP ALA PHE LEU GLU
SEQRES 19 C 251 LYS SER ALA GLN THR SER ALA LYS PHE LEU LYS SER MET
SEQRES 20 C 251 VAL ASP GLU LEU
SEQRES 1 D 251 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 251 LEU VAL PRO ARG GLY SER HIS MET VAL GLN LYS ILE GLY
SEQRES 3 D 251 ILE LEU GLY ALA MET ARG GLU GLN ILE THR PRO ILE LEU
SEQRES 4 D 251 GLU LEU PHE GLY VAL ASP PHE GLU GLU ILE PRO LEU GLY
SEQRES 5 D 251 GLY ASN VAL PHE HIS LYS GLY VAL TYR HIS ASN LYS GLU
SEQRES 6 D 251 ILE ILE VAL ALA TYR SER LYS ILE GLY LYS VAL HIS SER
SEQRES 7 D 251 THR LEU THR THR THR SER MET ILE LEU ALA PHE GLY VAL
SEQRES 8 D 251 GLN LYS VAL LEU PHE SER GLY VAL ALA GLY SER LEU VAL
SEQRES 9 D 251 LYS ASP LEU LYS ILE ASN ASP LEU LEU VAL ALA ILE GLN
SEQRES 10 D 251 LEU VAL GLN HIS ASP VAL ASP LEU SER ALA PHE ASP HIS
SEQRES 11 D 251 PRO LEU GLY PHE ILE PRO GLU SER ALA ILE PHE ILE GLU
SEQRES 12 D 251 THR SER GLU SER LEU ASN ALA LEU ALA LYS GLU VAL ALA
SEQRES 13 D 251 ASN GLU GLN HIS ILE VAL LEU LYS GLU GLY VAL ILE ALA
SEQRES 14 D 251 SER GLY ASP GLN PHE VAL HIS SER LYS GLU ARG LYS GLU
SEQRES 15 D 251 PHE LEU VAL SER GLU PHE LYS ALA SER ALA VAL GLU MET
SEQRES 16 D 251 GLU GLY ALA SER VAL ALA PHE VAL CYS GLN LYS PHE GLY
SEQRES 17 D 251 VAL PRO CYS CYS VAL LEU ARG SER ILE SER ASP ASN ALA
SEQRES 18 D 251 ASP GLU GLU ALA ASN MET SER PHE ASP ALA PHE LEU GLU
SEQRES 19 D 251 LYS SER ALA GLN THR SER ALA LYS PHE LEU LYS SER MET
SEQRES 20 D 251 VAL ASP GLU LEU
FORMUL 5 HOH *165(H2 O)
HELIX 1 1 MET A 11 GLU A 13 5 3
HELIX 2 2 GLN A 14 GLY A 23 1 10
HELIX 3 3 GLY A 54 GLY A 70 1 17
HELIX 4 4 LEU A 105 ASP A 109 5 5
HELIX 5 5 SER A 125 GLN A 139 1 15
HELIX 6 6 SER A 157 LYS A 169 1 13
HELIX 7 7 GLU A 176 GLY A 188 1 13
HELIX 8 8 SER A 208 GLU A 230 1 23
HELIX 9 9 MET B 11 GLU B 13 5 3
HELIX 10 10 GLN B 14 GLY B 23 1 10
HELIX 11 11 GLY B 54 GLY B 70 1 17
HELIX 12 12 LEU B 105 ASP B 109 5 5
HELIX 13 13 SER B 125 GLN B 139 1 15
HELIX 14 14 SER B 157 LYS B 169 1 13
HELIX 15 15 GLU B 176 GLY B 188 1 13
HELIX 16 16 LYS B 215 LEU B 231 1 17
HELIX 17 17 MET C 11 GLU C 13 5 3
HELIX 18 18 GLN C 14 GLY C 23 1 10
HELIX 19 19 GLY C 54 GLY C 70 1 17
HELIX 20 20 LEU C 105 ASP C 109 5 5
HELIX 21 21 SER C 125 GLU C 138 1 14
HELIX 22 22 SER C 157 LYS C 169 1 13
HELIX 23 23 GLU C 176 GLY C 188 1 13
HELIX 24 24 GLU C 214 ASP C 229 1 16
HELIX 25 25 MET D 11 GLU D 13 5 3
HELIX 26 26 GLN D 14 GLY D 23 1 10
HELIX 27 27 ILE D 53 GLY D 70 1 18
HELIX 28 28 LEU D 105 ASP D 109 5 5
HELIX 29 29 SER D 125 GLU D 138 1 14
HELIX 30 30 SER D 157 LYS D 169 1 13
HELIX 31 31 GLU D 176 PHE D 187 1 12
HELIX 32 32 SER D 208 GLU D 230 1 23
SHEET 1 AA 7 GLU A 27 LEU A 31 0
SHEET 2 AA 7 ASN A 34 TYR A 41 -1 O ASN A 34 N LEU A 31
SHEET 3 AA 7 LYS A 44 TYR A 50 -1 O LYS A 44 N TYR A 41
SHEET 4 AA 7 GLN A 3 GLY A 9 1 O GLN A 3 N GLU A 45
SHEET 5 AA 7 LYS A 73 SER A 82 1 O LYS A 73 N GLY A 6
SHEET 6 AA 7 CYS A 191 ILE A 197 1 O CYS A 192 N PHE A 76
SHEET 7 AA 7 LEU A 92 GLN A 100 -1 O LEU A 93 N ARG A 195
SHEET 1 AB 2 GLU A 27 LEU A 31 0
SHEET 2 AB 2 LYS A 73 SER A 82 1 O LYS A 73 N GLY A 6
SHEET 1 BA 7 GLU B 27 LEU B 31 0
SHEET 2 BA 7 ASN B 34 TYR B 41 -1 O ASN B 34 N LEU B 31
SHEET 3 BA 7 LYS B 44 TYR B 50 -1 O LYS B 44 N TYR B 41
SHEET 4 BA 7 GLN B 3 GLY B 9 1 O GLN B 3 N GLU B 45
SHEET 5 BA 7 LYS B 73 SER B 82 1 O LYS B 73 N GLY B 6
SHEET 6 BA 7 CYS B 191 ASP B 199 1 O CYS B 192 N PHE B 76
SHEET 7 BA 7 LEU B 92 GLN B 100 -1 O LEU B 93 N ARG B 195
SHEET 1 BB 2 GLU B 27 LEU B 31 0
SHEET 2 BB 2 LYS B 73 SER B 82 1 O LYS B 73 N GLY B 6
SHEET 1 CA10 GLU C 27 LEU C 31 0
SHEET 2 CA10 ASN C 34 TYR C 41 -1 O ASN C 34 N LEU C 31
SHEET 3 CA10 LYS C 44 TYR C 50 -1 O LYS C 44 N TYR C 41
SHEET 4 CA10 GLN C 3 GLY C 9 1 O GLN C 3 N GLU C 45
SHEET 5 CA10 LYS C 73 SER C 77 1 O LYS C 73 N GLY C 6
SHEET 6 CA10 CYS C 191 ILE C 197 1 O CYS C 192 N PHE C 76
SHEET 7 CA10 VAL C 79 SER C 82 1 N ALA C 80 O SER C 196
SHEET 8 CA10 ALA C 172 GLU C 174 -1 O VAL C 173 N GLY C 81
SHEET 9 CA10 LEU C 143 SER C 150 1 O ALA C 149 N GLU C 174
SHEET 10 CA10 LEU C 92 GLN C 100 1 O LEU C 92 N LYS C 144
SHEET 1 CB 2 GLU C 27 LEU C 31 0
SHEET 2 CB 2 CYS C 191 ILE C 197 1 O CYS C 192 N PHE C 76
SHEET 1 DA 7 GLU D 27 LEU D 31 0
SHEET 2 DA 7 ASN D 34 TYR D 41 -1 O ASN D 34 N LEU D 31
SHEET 3 DA 7 LYS D 44 TYR D 50 -1 O LYS D 44 N TYR D 41
SHEET 4 DA 7 GLN D 3 GLY D 9 1 O GLN D 3 N GLU D 45
SHEET 5 DA 7 LYS D 73 SER D 82 1 O LYS D 73 N GLY D 6
SHEET 6 DA 7 ILE D 122 GLU D 123 0
SHEET 7 DA 7 LEU D 92 GLN D 100 -1 O LEU D 98 N ILE D 122
CRYST1 64.230 75.690 97.010 90.00 106.38 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015569 0.000000 0.004576 0.00000
SCALE2 0.000000 0.013212 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010744 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
