HEADER OXIDOREDUCTASE 23-JAN-06 2FSS
TITLE CANDIDA BOIDINII FORMATE DEHYDROGENASE (FDH) K47E MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FORMATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 1.2.1.2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA BOIDINII;
SOURCE 3 ORGANISM_TAXID: 5477;
SOURCE 4 GENE: CBFDH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRCHIS2A, PVLKS3
KEYWDS ROSSMANN FOLD, PROTEIN HOMO DIMER, NAD BINDING SITE, FORMATE BINDING
KEYWDS 2 SITE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SCHIRWITZ,A.SCHMIDT,V.S.LAMZIN
REVDAT 5 10-NOV-21 2FSS 1 REMARK SEQADV
REVDAT 4 18-OCT-17 2FSS 1 REMARK
REVDAT 3 28-APR-09 2FSS 1 JRNL
REVDAT 2 24-FEB-09 2FSS 1 VERSN
REVDAT 1 13-FEB-07 2FSS 0
JRNL AUTH K.SCHIRWITZ,A.SCHMIDT,V.S.LAMZIN
JRNL TITL HIGH-RESOLUTION STRUCTURES OF FORMATE DEHYDROGENASE FROM
JRNL TITL 2 CANDIDA BOIDINII.
JRNL REF PROTEIN SCI. V. 16 1146 2007
JRNL REFN ISSN 0961-8368
JRNL PMID 17525463
JRNL DOI 10.1110/PS.062741707
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 150929
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7992
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10546
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.3150
REMARK 3 BIN FREE R VALUE SET COUNT : 565
REMARK 3 BIN FREE R VALUE : 0.3720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10830
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 947
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : 0.00000
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): 0.121
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.122
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.056
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11144 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15144 ; 1.410 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1402 ; 6.328 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 503 ;37.917 ;24.851
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1895 ;15.236 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;10.791 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1705 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8406 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5633 ; 0.205 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 7743 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 900 ; 0.136 ; 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): 79 ; 0.195 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 26 ; 0.152 ; 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): 7087 ; 0.815 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11150 ; 1.340 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4594 ; 2.148 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3986 ; 3.228 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2FSS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000036267.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUL-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.84140
REMARK 200 MONOCHROMATOR : TRIANGULAR MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 158925
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 19.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA-CACODYLATE PH 6.5, 30% PEG
REMARK 280 8000, 0.15M AMMONIUMSULFATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 6190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 6270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -115.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 APPLY THE FOLLOWING TO CHAINS: B, C
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 43.13262
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -67.60931
REMARK 350 BIOMT3 2 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 0
REMARK 465 VAL A 354
REMARK 465 THR A 355
REMARK 465 LYS A 356
REMARK 465 ALA A 357
REMARK 465 TYR A 358
REMARK 465 GLY A 359
REMARK 465 LYS A 360
REMARK 465 HIS A 361
REMARK 465 ASP A 362
REMARK 465 LYS A 363
REMARK 465 LYS A 364
REMARK 465 MET B 0
REMARK 465 LYS B 12
REMARK 465 HIS B 13
REMARK 465 ALA B 14
REMARK 465 ALA B 15
REMARK 465 ASP B 16
REMARK 465 GLU B 17
REMARK 465 GLU B 18
REMARK 465 VAL B 354
REMARK 465 THR B 355
REMARK 465 LYS B 356
REMARK 465 ALA B 357
REMARK 465 TYR B 358
REMARK 465 GLY B 359
REMARK 465 LYS B 360
REMARK 465 HIS B 361
REMARK 465 ASP B 362
REMARK 465 LYS B 363
REMARK 465 LYS B 364
REMARK 465 MET C 0
REMARK 465 VAL C 354
REMARK 465 THR C 355
REMARK 465 LYS C 356
REMARK 465 ALA C 357
REMARK 465 TYR C 358
REMARK 465 GLY C 359
REMARK 465 LYS C 360
REMARK 465 HIS C 361
REMARK 465 ASP C 362
REMARK 465 LYS C 363
REMARK 465 LYS C 364
REMARK 465 MET D 0
REMARK 465 ASP D 9
REMARK 465 ALA D 10
REMARK 465 GLY D 11
REMARK 465 LYS D 12
REMARK 465 HIS D 13
REMARK 465 ALA D 14
REMARK 465 ALA D 15
REMARK 465 ASP D 16
REMARK 465 GLU D 17
REMARK 465 ASP D 46
REMARK 465 GLU D 47
REMARK 465 GLU D 48
REMARK 465 GLY D 49
REMARK 465 GLY D 50
REMARK 465 ASN D 51
REMARK 465 SER D 52
REMARK 465 VAL D 354
REMARK 465 THR D 355
REMARK 465 LYS D 356
REMARK 465 ALA D 357
REMARK 465 TYR D 358
REMARK 465 GLY D 359
REMARK 465 LYS D 360
REMARK 465 HIS D 361
REMARK 465 ASP D 362
REMARK 465 LYS D 363
REMARK 465 LYS D 364
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 70 63.67 -176.52
REMARK 500 TRP A 150 103.21 -160.77
REMARK 500 ALA A 257 -86.55 -98.88
REMARK 500 ALA A 304 -150.05 -137.31
REMARK 500 TYR A 312 -6.75 -142.43
REMARK 500 ILE A 347 -62.34 -90.93
REMARK 500 ALA B 10 -126.73 -106.08
REMARK 500 LEU B 28 17.78 51.01
REMARK 500 ASN B 51 -53.18 77.48
REMARK 500 HIS B 70 68.06 -161.82
REMARK 500 VAL B 115 78.16 -100.09
REMARK 500 TRP B 150 104.03 -163.55
REMARK 500 ASP B 195 -167.36 -161.25
REMARK 500 LEU B 199 86.81 39.49
REMARK 500 ALA B 257 -84.91 -91.47
REMARK 500 ALA B 304 -148.64 -134.48
REMARK 500 TYR B 312 -4.07 -140.30
REMARK 500 LEU C 28 16.04 59.85
REMARK 500 ASN C 51 4.38 93.56
REMARK 500 ALA C 72 43.09 113.25
REMARK 500 TRP C 150 102.97 -161.12
REMARK 500 ALA C 257 -85.69 -93.41
REMARK 500 ALA C 304 -148.46 -132.88
REMARK 500 LEU D 7 -154.16 -137.70
REMARK 500 TYR D 21 -35.33 -135.86
REMARK 500 LEU D 28 14.30 51.67
REMARK 500 GLU D 151 84.89 -152.44
REMARK 500 ALA D 257 -84.08 -91.95
REMARK 500 ALA D 304 -148.44 -134.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TYR B 21 GLY B 22 126.13
REMARK 500 GLY B 22 CYS B 23 -141.71
REMARK 500 ALA B 198 LEU B 199 49.62
REMARK 500 LYS D 19 LEU D 20 145.63
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 D 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2005
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2A1Z RELATED DB: PDB
REMARK 900 CBFDH K328V MUTANT
DBREF 2FSS A 2 364 GB 7657869 CAA09466 2 364
DBREF 2FSS B 2 364 GB 7657869 CAA09466 2 364
DBREF 2FSS C 2 364 GB 7657869 CAA09466 2 364
DBREF 2FSS D 2 364 GB 7657869 CAA09466 2 364
SEQADV 2FSS MET A 0 GB 7657869 CLONING ARTIFACT
SEQADV 2FSS ALA A 1 GB 7657869 CLONING ARTIFACT
SEQADV 2FSS GLU A 47 GB 7657869 LYS 47 ENGINEERED MUTATION
SEQADV 2FSS MET B 0 GB 7657869 CLONING ARTIFACT
SEQADV 2FSS ALA B 1 GB 7657869 CLONING ARTIFACT
SEQADV 2FSS GLU B 47 GB 7657869 LYS 47 ENGINEERED MUTATION
SEQADV 2FSS MET C 0 GB 7657869 CLONING ARTIFACT
SEQADV 2FSS ALA C 1 GB 7657869 CLONING ARTIFACT
SEQADV 2FSS GLU C 47 GB 7657869 LYS 47 ENGINEERED MUTATION
SEQADV 2FSS MET D 0 GB 7657869 CLONING ARTIFACT
SEQADV 2FSS ALA D 1 GB 7657869 CLONING ARTIFACT
SEQADV 2FSS GLU D 47 GB 7657869 LYS 47 ENGINEERED MUTATION
SEQRES 1 A 365 MET ALA LYS ILE VAL LEU VAL LEU TYR ASP ALA GLY LYS
SEQRES 2 A 365 HIS ALA ALA ASP GLU GLU LYS LEU TYR GLY CYS THR GLU
SEQRES 3 A 365 ASN LYS LEU GLY ILE ALA ASN TRP LEU LYS ASP GLN GLY
SEQRES 4 A 365 HIS GLU LEU ILE THR THR SER ASP GLU GLU GLY GLY ASN
SEQRES 5 A 365 SER VAL LEU ASP GLN HIS ILE PRO ASP ALA ASP ILE ILE
SEQRES 6 A 365 ILE THR THR PRO PHE HIS PRO ALA TYR ILE THR LYS GLU
SEQRES 7 A 365 ARG ILE ASP LYS ALA LYS LYS LEU LYS LEU VAL VAL VAL
SEQRES 8 A 365 ALA GLY VAL GLY SER ASP HIS ILE ASP LEU ASP TYR ILE
SEQRES 9 A 365 ASN GLN THR GLY LYS LYS ILE SER VAL LEU GLU VAL THR
SEQRES 10 A 365 GLY SER ASN VAL VAL SER VAL ALA GLU HIS VAL VAL MET
SEQRES 11 A 365 THR MET LEU VAL LEU VAL ARG ASN PHE VAL PRO ALA HIS
SEQRES 12 A 365 GLU GLN ILE ILE ASN HIS ASP TRP GLU VAL ALA ALA ILE
SEQRES 13 A 365 ALA LYS ASP ALA TYR ASP ILE GLU GLY LYS THR ILE ALA
SEQRES 14 A 365 THR ILE GLY ALA GLY ARG ILE GLY TYR ARG VAL LEU GLU
SEQRES 15 A 365 ARG LEU VAL PRO PHE ASN PRO LYS GLU LEU LEU TYR TYR
SEQRES 16 A 365 ASP TYR GLN ALA LEU PRO LYS ASP ALA GLU GLU LYS VAL
SEQRES 17 A 365 GLY ALA ARG ARG VAL GLU ASN ILE GLU GLU LEU VAL ALA
SEQRES 18 A 365 GLN ALA ASP ILE VAL THR VAL ASN ALA PRO LEU HIS ALA
SEQRES 19 A 365 GLY THR LYS GLY LEU ILE ASN LYS GLU LEU LEU SER LYS
SEQRES 20 A 365 PHE LYS LYS GLY ALA TRP LEU VAL ASN THR ALA ARG GLY
SEQRES 21 A 365 ALA ILE CYS VAL ALA GLU ASP VAL ALA ALA ALA LEU GLU
SEQRES 22 A 365 SER GLY GLN LEU ARG GLY TYR GLY GLY ASP VAL TRP PHE
SEQRES 23 A 365 PRO GLN PRO ALA PRO LYS ASP HIS PRO TRP ARG ASP MET
SEQRES 24 A 365 ARG ASN LYS TYR GLY ALA GLY ASN ALA MET THR PRO HIS
SEQRES 25 A 365 TYR SER GLY THR THR LEU ASP ALA GLN THR ARG TYR ALA
SEQRES 26 A 365 GLN GLY THR LYS ASN ILE LEU GLU SER PHE PHE THR GLY
SEQRES 27 A 365 LYS PHE ASP TYR ARG PRO GLN ASP ILE ILE LEU LEU ASN
SEQRES 28 A 365 GLY GLU TYR VAL THR LYS ALA TYR GLY LYS HIS ASP LYS
SEQRES 29 A 365 LYS
SEQRES 1 B 365 MET ALA LYS ILE VAL LEU VAL LEU TYR ASP ALA GLY LYS
SEQRES 2 B 365 HIS ALA ALA ASP GLU GLU LYS LEU TYR GLY CYS THR GLU
SEQRES 3 B 365 ASN LYS LEU GLY ILE ALA ASN TRP LEU LYS ASP GLN GLY
SEQRES 4 B 365 HIS GLU LEU ILE THR THR SER ASP GLU GLU GLY GLY ASN
SEQRES 5 B 365 SER VAL LEU ASP GLN HIS ILE PRO ASP ALA ASP ILE ILE
SEQRES 6 B 365 ILE THR THR PRO PHE HIS PRO ALA TYR ILE THR LYS GLU
SEQRES 7 B 365 ARG ILE ASP LYS ALA LYS LYS LEU LYS LEU VAL VAL VAL
SEQRES 8 B 365 ALA GLY VAL GLY SER ASP HIS ILE ASP LEU ASP TYR ILE
SEQRES 9 B 365 ASN GLN THR GLY LYS LYS ILE SER VAL LEU GLU VAL THR
SEQRES 10 B 365 GLY SER ASN VAL VAL SER VAL ALA GLU HIS VAL VAL MET
SEQRES 11 B 365 THR MET LEU VAL LEU VAL ARG ASN PHE VAL PRO ALA HIS
SEQRES 12 B 365 GLU GLN ILE ILE ASN HIS ASP TRP GLU VAL ALA ALA ILE
SEQRES 13 B 365 ALA LYS ASP ALA TYR ASP ILE GLU GLY LYS THR ILE ALA
SEQRES 14 B 365 THR ILE GLY ALA GLY ARG ILE GLY TYR ARG VAL LEU GLU
SEQRES 15 B 365 ARG LEU VAL PRO PHE ASN PRO LYS GLU LEU LEU TYR TYR
SEQRES 16 B 365 ASP TYR GLN ALA LEU PRO LYS ASP ALA GLU GLU LYS VAL
SEQRES 17 B 365 GLY ALA ARG ARG VAL GLU ASN ILE GLU GLU LEU VAL ALA
SEQRES 18 B 365 GLN ALA ASP ILE VAL THR VAL ASN ALA PRO LEU HIS ALA
SEQRES 19 B 365 GLY THR LYS GLY LEU ILE ASN LYS GLU LEU LEU SER LYS
SEQRES 20 B 365 PHE LYS LYS GLY ALA TRP LEU VAL ASN THR ALA ARG GLY
SEQRES 21 B 365 ALA ILE CYS VAL ALA GLU ASP VAL ALA ALA ALA LEU GLU
SEQRES 22 B 365 SER GLY GLN LEU ARG GLY TYR GLY GLY ASP VAL TRP PHE
SEQRES 23 B 365 PRO GLN PRO ALA PRO LYS ASP HIS PRO TRP ARG ASP MET
SEQRES 24 B 365 ARG ASN LYS TYR GLY ALA GLY ASN ALA MET THR PRO HIS
SEQRES 25 B 365 TYR SER GLY THR THR LEU ASP ALA GLN THR ARG TYR ALA
SEQRES 26 B 365 GLN GLY THR LYS ASN ILE LEU GLU SER PHE PHE THR GLY
SEQRES 27 B 365 LYS PHE ASP TYR ARG PRO GLN ASP ILE ILE LEU LEU ASN
SEQRES 28 B 365 GLY GLU TYR VAL THR LYS ALA TYR GLY LYS HIS ASP LYS
SEQRES 29 B 365 LYS
SEQRES 1 C 365 MET ALA LYS ILE VAL LEU VAL LEU TYR ASP ALA GLY LYS
SEQRES 2 C 365 HIS ALA ALA ASP GLU GLU LYS LEU TYR GLY CYS THR GLU
SEQRES 3 C 365 ASN LYS LEU GLY ILE ALA ASN TRP LEU LYS ASP GLN GLY
SEQRES 4 C 365 HIS GLU LEU ILE THR THR SER ASP GLU GLU GLY GLY ASN
SEQRES 5 C 365 SER VAL LEU ASP GLN HIS ILE PRO ASP ALA ASP ILE ILE
SEQRES 6 C 365 ILE THR THR PRO PHE HIS PRO ALA TYR ILE THR LYS GLU
SEQRES 7 C 365 ARG ILE ASP LYS ALA LYS LYS LEU LYS LEU VAL VAL VAL
SEQRES 8 C 365 ALA GLY VAL GLY SER ASP HIS ILE ASP LEU ASP TYR ILE
SEQRES 9 C 365 ASN GLN THR GLY LYS LYS ILE SER VAL LEU GLU VAL THR
SEQRES 10 C 365 GLY SER ASN VAL VAL SER VAL ALA GLU HIS VAL VAL MET
SEQRES 11 C 365 THR MET LEU VAL LEU VAL ARG ASN PHE VAL PRO ALA HIS
SEQRES 12 C 365 GLU GLN ILE ILE ASN HIS ASP TRP GLU VAL ALA ALA ILE
SEQRES 13 C 365 ALA LYS ASP ALA TYR ASP ILE GLU GLY LYS THR ILE ALA
SEQRES 14 C 365 THR ILE GLY ALA GLY ARG ILE GLY TYR ARG VAL LEU GLU
SEQRES 15 C 365 ARG LEU VAL PRO PHE ASN PRO LYS GLU LEU LEU TYR TYR
SEQRES 16 C 365 ASP TYR GLN ALA LEU PRO LYS ASP ALA GLU GLU LYS VAL
SEQRES 17 C 365 GLY ALA ARG ARG VAL GLU ASN ILE GLU GLU LEU VAL ALA
SEQRES 18 C 365 GLN ALA ASP ILE VAL THR VAL ASN ALA PRO LEU HIS ALA
SEQRES 19 C 365 GLY THR LYS GLY LEU ILE ASN LYS GLU LEU LEU SER LYS
SEQRES 20 C 365 PHE LYS LYS GLY ALA TRP LEU VAL ASN THR ALA ARG GLY
SEQRES 21 C 365 ALA ILE CYS VAL ALA GLU ASP VAL ALA ALA ALA LEU GLU
SEQRES 22 C 365 SER GLY GLN LEU ARG GLY TYR GLY GLY ASP VAL TRP PHE
SEQRES 23 C 365 PRO GLN PRO ALA PRO LYS ASP HIS PRO TRP ARG ASP MET
SEQRES 24 C 365 ARG ASN LYS TYR GLY ALA GLY ASN ALA MET THR PRO HIS
SEQRES 25 C 365 TYR SER GLY THR THR LEU ASP ALA GLN THR ARG TYR ALA
SEQRES 26 C 365 GLN GLY THR LYS ASN ILE LEU GLU SER PHE PHE THR GLY
SEQRES 27 C 365 LYS PHE ASP TYR ARG PRO GLN ASP ILE ILE LEU LEU ASN
SEQRES 28 C 365 GLY GLU TYR VAL THR LYS ALA TYR GLY LYS HIS ASP LYS
SEQRES 29 C 365 LYS
SEQRES 1 D 365 MET ALA LYS ILE VAL LEU VAL LEU TYR ASP ALA GLY LYS
SEQRES 2 D 365 HIS ALA ALA ASP GLU GLU LYS LEU TYR GLY CYS THR GLU
SEQRES 3 D 365 ASN LYS LEU GLY ILE ALA ASN TRP LEU LYS ASP GLN GLY
SEQRES 4 D 365 HIS GLU LEU ILE THR THR SER ASP GLU GLU GLY GLY ASN
SEQRES 5 D 365 SER VAL LEU ASP GLN HIS ILE PRO ASP ALA ASP ILE ILE
SEQRES 6 D 365 ILE THR THR PRO PHE HIS PRO ALA TYR ILE THR LYS GLU
SEQRES 7 D 365 ARG ILE ASP LYS ALA LYS LYS LEU LYS LEU VAL VAL VAL
SEQRES 8 D 365 ALA GLY VAL GLY SER ASP HIS ILE ASP LEU ASP TYR ILE
SEQRES 9 D 365 ASN GLN THR GLY LYS LYS ILE SER VAL LEU GLU VAL THR
SEQRES 10 D 365 GLY SER ASN VAL VAL SER VAL ALA GLU HIS VAL VAL MET
SEQRES 11 D 365 THR MET LEU VAL LEU VAL ARG ASN PHE VAL PRO ALA HIS
SEQRES 12 D 365 GLU GLN ILE ILE ASN HIS ASP TRP GLU VAL ALA ALA ILE
SEQRES 13 D 365 ALA LYS ASP ALA TYR ASP ILE GLU GLY LYS THR ILE ALA
SEQRES 14 D 365 THR ILE GLY ALA GLY ARG ILE GLY TYR ARG VAL LEU GLU
SEQRES 15 D 365 ARG LEU VAL PRO PHE ASN PRO LYS GLU LEU LEU TYR TYR
SEQRES 16 D 365 ASP TYR GLN ALA LEU PRO LYS ASP ALA GLU GLU LYS VAL
SEQRES 17 D 365 GLY ALA ARG ARG VAL GLU ASN ILE GLU GLU LEU VAL ALA
SEQRES 18 D 365 GLN ALA ASP ILE VAL THR VAL ASN ALA PRO LEU HIS ALA
SEQRES 19 D 365 GLY THR LYS GLY LEU ILE ASN LYS GLU LEU LEU SER LYS
SEQRES 20 D 365 PHE LYS LYS GLY ALA TRP LEU VAL ASN THR ALA ARG GLY
SEQRES 21 D 365 ALA ILE CYS VAL ALA GLU ASP VAL ALA ALA ALA LEU GLU
SEQRES 22 D 365 SER GLY GLN LEU ARG GLY TYR GLY GLY ASP VAL TRP PHE
SEQRES 23 D 365 PRO GLN PRO ALA PRO LYS ASP HIS PRO TRP ARG ASP MET
SEQRES 24 D 365 ARG ASN LYS TYR GLY ALA GLY ASN ALA MET THR PRO HIS
SEQRES 25 D 365 TYR SER GLY THR THR LEU ASP ALA GLN THR ARG TYR ALA
SEQRES 26 D 365 GLN GLY THR LYS ASN ILE LEU GLU SER PHE PHE THR GLY
SEQRES 27 D 365 LYS PHE ASP TYR ARG PRO GLN ASP ILE ILE LEU LEU ASN
SEQRES 28 D 365 GLY GLU TYR VAL THR LYS ALA TYR GLY LYS HIS ASP LYS
SEQRES 29 D 365 LYS
HET SO4 A2003 5
HET SO4 A2005 5
HET SO4 C2002 5
HET SO4 C2004 5
HET SO4 D2001 5
HETNAM SO4 SULFATE ION
FORMUL 5 SO4 5(O4 S 2-)
FORMUL 10 HOH *947(H2 O)
HELIX 1 1 GLY A 11 GLU A 17 1 7
HELIX 2 2 ASN A 26 GLY A 29 5 4
HELIX 3 3 ILE A 30 GLN A 37 1 8
HELIX 4 4 SER A 52 ILE A 58 1 7
HELIX 5 5 PRO A 59 ALA A 61 5 3
HELIX 6 6 THR A 75 ALA A 82 1 8
HELIX 7 7 ASP A 99 GLY A 107 1 9
HELIX 8 8 ASN A 119 ARG A 136 1 18
HELIX 9 9 ASN A 137 ASN A 147 1 11
HELIX 10 10 GLU A 151 LYS A 157 1 7
HELIX 11 11 GLY A 173 VAL A 184 1 12
HELIX 12 12 PRO A 185 ASN A 187 5 3
HELIX 13 13 PRO A 200 VAL A 207 1 8
HELIX 14 14 ASN A 214 ALA A 220 1 7
HELIX 15 15 ASN A 240 LYS A 246 1 7
HELIX 16 16 ARG A 258 CYS A 262 5 5
HELIX 17 17 VAL A 263 SER A 273 1 11
HELIX 18 18 HIS A 293 MET A 298 1 6
HELIX 19 19 TYR A 312 THR A 315 5 4
HELIX 20 20 THR A 316 THR A 336 1 21
HELIX 21 21 ARG A 342 GLN A 344 5 3
HELIX 22 22 ASN B 26 GLY B 29 5 4
HELIX 23 23 ILE B 30 ASP B 36 1 7
HELIX 24 24 SER B 52 ILE B 58 1 7
HELIX 25 25 PRO B 59 ALA B 61 5 3
HELIX 26 26 THR B 75 ALA B 82 1 8
HELIX 27 27 ASP B 99 GLY B 107 1 9
HELIX 28 28 ASN B 119 ARG B 136 1 18
HELIX 29 29 ASN B 137 ASN B 147 1 11
HELIX 30 30 GLU B 151 LYS B 157 1 7
HELIX 31 31 GLY B 173 VAL B 184 1 12
HELIX 32 32 PRO B 185 ASN B 187 5 3
HELIX 33 33 PRO B 200 GLY B 208 1 9
HELIX 34 34 ASN B 214 GLN B 221 1 8
HELIX 35 35 HIS B 232 LYS B 236 5 5
HELIX 36 36 ASN B 240 PHE B 247 1 8
HELIX 37 37 ARG B 258 CYS B 262 5 5
HELIX 38 38 VAL B 263 GLY B 274 1 12
HELIX 39 39 HIS B 293 MET B 298 1 6
HELIX 40 40 TYR B 312 THR B 315 5 4
HELIX 41 41 THR B 316 THR B 336 1 21
HELIX 42 42 ARG B 342 GLN B 344 5 3
HELIX 43 43 GLY C 11 GLU C 17 1 7
HELIX 44 44 ASN C 26 GLY C 29 5 4
HELIX 45 45 ILE C 30 ASP C 36 1 7
HELIX 46 46 SER C 52 ILE C 58 1 7
HELIX 47 47 PRO C 59 ALA C 61 5 3
HELIX 48 48 THR C 75 ALA C 82 1 8
HELIX 49 49 ASP C 99 GLY C 107 1 9
HELIX 50 50 ASN C 119 ARG C 136 1 18
HELIX 51 51 ASN C 137 ASN C 147 1 11
HELIX 52 52 GLU C 151 LYS C 157 1 7
HELIX 53 53 GLY C 173 VAL C 184 1 12
HELIX 54 54 PRO C 185 ASN C 187 5 3
HELIX 55 55 PRO C 200 VAL C 207 1 8
HELIX 56 56 ASN C 214 ALA C 222 1 9
HELIX 57 57 ASN C 240 SER C 245 1 6
HELIX 58 58 ARG C 258 CYS C 262 5 5
HELIX 59 59 VAL C 263 SER C 273 1 11
HELIX 60 60 HIS C 293 MET C 298 1 6
HELIX 61 61 TYR C 312 THR C 315 5 4
HELIX 62 62 THR C 316 THR C 336 1 21
HELIX 63 63 ARG C 342 GLN C 344 5 3
HELIX 64 64 ASN D 26 GLY D 29 5 4
HELIX 65 65 ILE D 30 ASP D 36 1 7
HELIX 66 66 VAL D 53 ILE D 58 1 6
HELIX 67 67 PRO D 59 ALA D 61 5 3
HELIX 68 68 THR D 75 ALA D 82 1 8
HELIX 69 69 ASP D 99 GLY D 107 1 9
HELIX 70 70 ASN D 119 ARG D 136 1 18
HELIX 71 71 ASN D 137 ASN D 147 1 11
HELIX 72 72 GLU D 151 LYS D 157 1 7
HELIX 73 73 GLY D 173 VAL D 184 1 12
HELIX 74 74 PRO D 185 ASN D 187 5 3
HELIX 75 75 PRO D 200 GLY D 208 1 9
HELIX 76 76 ASN D 214 GLN D 221 1 8
HELIX 77 77 ASN D 240 SER D 245 1 6
HELIX 78 78 ARG D 258 CYS D 262 5 5
HELIX 79 79 VAL D 263 SER D 273 1 11
HELIX 80 80 HIS D 293 MET D 298 1 6
HELIX 81 81 TYR D 312 THR D 315 5 4
HELIX 82 82 THR D 316 THR D 336 1 21
HELIX 83 83 ARG D 342 GLN D 344 5 3
SHEET 1 A 7 GLU A 40 THR A 44 0
SHEET 2 A 7 LYS A 2 VAL A 6 1 N LEU A 5 O ILE A 42
SHEET 3 A 7 ILE A 63 THR A 66 1 O ILE A 65 N VAL A 4
SHEET 4 A 7 LEU A 87 VAL A 90 1 O VAL A 89 N THR A 66
SHEET 5 A 7 SER A 111 GLU A 114 1 O LEU A 113 N VAL A 90
SHEET 6 A 7 ILE A 346 LEU A 349 -1 O LEU A 348 N VAL A 112
SHEET 7 A 7 GLU A 352 TYR A 353 -1 O GLU A 352 N LEU A 349
SHEET 1 B 7 ALA A 209 ARG A 211 0
SHEET 2 B 7 GLU A 190 TYR A 194 1 N TYR A 193 O ARG A 210
SHEET 3 B 7 THR A 166 ILE A 170 1 N ILE A 167 O GLU A 190
SHEET 4 B 7 ILE A 224 VAL A 227 1 O ILE A 224 N ALA A 168
SHEET 5 B 7 ALA A 251 ASN A 255 1 O VAL A 254 N VAL A 225
SHEET 6 B 7 LEU A 276 GLY A 281 1 O GLY A 280 N ASN A 255
SHEET 7 B 7 ASN A 306 MET A 308 1 O ALA A 307 N TYR A 279
SHEET 1 C 7 GLU B 40 THR B 44 0
SHEET 2 C 7 LYS B 2 VAL B 6 1 N ILE B 3 O GLU B 40
SHEET 3 C 7 ILE B 63 THR B 66 1 O ILE B 65 N VAL B 4
SHEET 4 C 7 LEU B 87 VAL B 90 1 O VAL B 89 N THR B 66
SHEET 5 C 7 SER B 111 GLU B 114 1 O LEU B 113 N VAL B 90
SHEET 6 C 7 ILE B 346 LEU B 349 -1 O ILE B 347 N VAL B 112
SHEET 7 C 7 GLU B 352 TYR B 353 -1 O GLU B 352 N LEU B 349
SHEET 1 D 7 ALA B 209 ARG B 211 0
SHEET 2 D 7 GLU B 190 TYR B 194 1 N TYR B 193 O ARG B 210
SHEET 3 D 7 THR B 166 ILE B 170 1 N ILE B 167 O LEU B 192
SHEET 4 D 7 ILE B 224 VAL B 227 1 O THR B 226 N ILE B 170
SHEET 5 D 7 ALA B 251 ASN B 255 1 O VAL B 254 N VAL B 225
SHEET 6 D 7 LEU B 276 GLY B 281 1 O ARG B 277 N ALA B 251
SHEET 7 D 7 ASN B 306 MET B 308 1 O ALA B 307 N TYR B 279
SHEET 1 E 6 GLU C 40 THR C 44 0
SHEET 2 E 6 LYS C 2 VAL C 6 1 N LEU C 5 O ILE C 42
SHEET 3 E 6 ILE C 63 THR C 66 1 O ILE C 65 N VAL C 4
SHEET 4 E 6 LEU C 87 VAL C 90 1 O VAL C 89 N THR C 66
SHEET 5 E 6 SER C 111 GLU C 114 1 O LEU C 113 N VAL C 88
SHEET 6 E 6 ILE C 346 LEU C 348 -1 O LEU C 348 N VAL C 112
SHEET 1 F 7 ALA C 209 ARG C 211 0
SHEET 2 F 7 GLU C 190 TYR C 194 1 N LEU C 191 O ARG C 210
SHEET 3 F 7 THR C 166 ILE C 170 1 N ILE C 167 O LEU C 192
SHEET 4 F 7 ILE C 224 VAL C 227 1 O ILE C 224 N ALA C 168
SHEET 5 F 7 ALA C 251 ASN C 255 1 O TRP C 252 N VAL C 225
SHEET 6 F 7 LEU C 276 GLY C 281 1 O ARG C 277 N ALA C 251
SHEET 7 F 7 ASN C 306 MET C 308 1 O ALA C 307 N TYR C 279
SHEET 1 G 6 GLU D 40 THR D 44 0
SHEET 2 G 6 LYS D 2 VAL D 6 1 N LEU D 5 O ILE D 42
SHEET 3 G 6 ILE D 63 THR D 66 1 O ILE D 65 N VAL D 4
SHEET 4 G 6 LEU D 87 VAL D 90 1 O VAL D 89 N ILE D 64
SHEET 5 G 6 SER D 111 GLU D 114 1 O LEU D 113 N VAL D 90
SHEET 6 G 6 ILE D 346 LEU D 348 -1 O ILE D 347 N VAL D 112
SHEET 1 H 7 ALA D 209 ARG D 211 0
SHEET 2 H 7 GLU D 190 TYR D 194 1 N LEU D 191 O ARG D 210
SHEET 3 H 7 THR D 166 ILE D 170 1 N ILE D 167 O GLU D 190
SHEET 4 H 7 ILE D 224 VAL D 227 1 O THR D 226 N ILE D 170
SHEET 5 H 7 ALA D 251 ASN D 255 1 O TRP D 252 N VAL D 225
SHEET 6 H 7 LEU D 276 GLY D 281 1 O ARG D 277 N ALA D 251
SHEET 7 H 7 ASN D 306 MET D 308 1 O ALA D 307 N TYR D 279
CISPEP 1 GLU A 48 GLY A 49 0 -7.58
CISPEP 2 PHE A 285 PRO A 286 0 17.55
CISPEP 3 GLN A 287 PRO A 288 0 17.74
CISPEP 4 GLU B 48 GLY B 49 0 10.15
CISPEP 5 GLY B 49 GLY B 50 0 -1.68
CISPEP 6 GLY B 50 ASN B 51 0 9.31
CISPEP 7 PHE B 285 PRO B 286 0 -7.67
CISPEP 8 GLN B 287 PRO B 288 0 2.23
CISPEP 9 GLU C 48 GLY C 49 0 -2.98
CISPEP 10 PRO C 71 ALA C 72 0 -10.61
CISPEP 11 PHE C 285 PRO C 286 0 -6.79
CISPEP 12 GLN C 287 PRO C 288 0 -3.55
CISPEP 13 PHE D 285 PRO D 286 0 -4.78
CISPEP 14 GLN D 287 PRO D 288 0 -4.29
SITE 1 AC1 3 GLY D 173 ARG D 174 HOH D2018
SITE 1 AC2 6 LYS A 109 GLN C 197 ALA C 198 ARG C 211
SITE 2 AC2 6 HOH C2034 HOH C2192
SITE 1 AC3 4 ALA A 198 ARG A 211 HOH A2021 LYS C 109
SITE 1 AC4 3 GLY C 173 ARG C 174 HOH C2047
SITE 1 AC5 4 GLY A 173 ARG A 174 HOH A2056 HOH A2199
CRYST1 53.430 68.389 109.369 77.93 89.33 81.34 P 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018716 -0.002851 0.000388 0.00000
SCALE2 0.000000 0.014791 -0.003173 0.00000
SCALE3 0.000000 0.000000 0.009352 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
