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HEADER HYDROLASE 23-MAR-12 4EB0
TITLE CRYSTAL STRUCTURE OF LEAF-BRANCH COMPOST BACTERIAL CUTINASE HOMOLOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LCC;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 36-293;
COMPND 5 EC: 3.1.1.74;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RP;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET25B
KEYWDS HYDROLASE, SERINE ESTERASE, CUTINASE HOMOLOG, PET DEGRADATION,
KEYWDS 2 METAGENOME
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SULAIMAN,D.J.YOU,K.EIKO,Y.KOGA,S.KANAYA
REVDAT 1 27-MAR-13 4EB0 0
JRNL AUTH S.SULAIMAN,D.J.YOU,K.EIKO,Y.KOGA,S.KANAYA
JRNL TITL CRYSTAL STRUCTURE OF LEAF-BRANCH COMPOST BACTERIAL CUTINASE
JRNL TITL 2 HOMOLOG
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 32818
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) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1741
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2374
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.1880
REMARK 3 BIN FREE R VALUE SET COUNT : 127
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1962
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 315
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.67000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : 0.70000
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): 0.074
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.075
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.043
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.126
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2023 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2764 ; 1.000 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 257 ; 7.429 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 87 ;32.304 ;22.759
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 283 ;10.840 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;12.062 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 310 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1578 ; 0.020 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1298 ; 1.466 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2088 ; 2.175 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 725 ; 3.398 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 676 ; 4.458 ; 4.500
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 : 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 4EB0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-MAR-12.
REMARK 100 THE RCSB ID CODE IS RCSB071392.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : HORIZONTAL FOCUSING MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER SMART 6500
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35110
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.700
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : 0.10600
REMARK 200 FOR THE DATA SET : 31.6570
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.70
REMARK 200 R MERGE FOR SHELL (I) : 0.41900
REMARK 200 R SYM FOR SHELL (I) : 0.41900
REMARK 200 FOR SHELL : 0.419
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1JFR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) POLYETHYLENE GLYCOL (PEG)
REMARK 280 3350, 200MM SODIUM THIOCYANATE, PH 7.0, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
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 20.45550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.36300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.54200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.36300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.45550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.54200
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 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 SER A 165 -127.89 60.19
REMARK 500 HIS A 218 -83.73 -126.70
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 ILE A 119 ASN A 120 149.22
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 SCN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 304
DBREF 4EB0 A 36 293 UNP G9BY57 G9BY57_9BACT 36 293
SEQRES 1 A 258 SER ASN PRO TYR GLN ARG GLY PRO ASN PRO THR ARG SER
SEQRES 2 A 258 ALA LEU THR ALA ASP GLY PRO PHE SER VAL ALA THR TYR
SEQRES 3 A 258 THR VAL SER ARG LEU SER VAL SER GLY PHE GLY GLY GLY
SEQRES 4 A 258 VAL ILE TYR TYR PRO THR GLY THR SER LEU THR PHE GLY
SEQRES 5 A 258 GLY ILE ALA MET SER PRO GLY TYR THR ALA ASP ALA SER
SEQRES 6 A 258 SER LEU ALA TRP LEU GLY ARG ARG LEU ALA SER HIS GLY
SEQRES 7 A 258 PHE VAL VAL LEU VAL ILE ASN THR ASN SER ARG PHE ASP
SEQRES 8 A 258 TYR PRO ASP SER ARG ALA SER GLN LEU SER ALA ALA LEU
SEQRES 9 A 258 ASN TYR LEU ARG THR SER SER PRO SER ALA VAL ARG ALA
SEQRES 10 A 258 ARG LEU ASP ALA ASN ARG LEU ALA VAL ALA GLY HIS SER
SEQRES 11 A 258 MET GLY GLY GLY GLY THR LEU ARG ILE ALA GLU GLN ASN
SEQRES 12 A 258 PRO SER LEU LYS ALA ALA VAL PRO LEU THR PRO TRP HIS
SEQRES 13 A 258 THR ASP LYS THR PHE ASN THR SER VAL PRO VAL LEU ILE
SEQRES 14 A 258 VAL GLY ALA GLU ALA ASP THR VAL ALA PRO VAL SER GLN
SEQRES 15 A 258 HIS ALA ILE PRO PHE TYR GLN ASN LEU PRO SER THR THR
SEQRES 16 A 258 PRO LYS VAL TYR VAL GLU LEU ASP ASN ALA SER HIS PHE
SEQRES 17 A 258 ALA PRO ASN SER ASN ASN ALA ALA ILE SER VAL TYR THR
SEQRES 18 A 258 ILE SER TRP MET LYS LEU TRP VAL ASP ASN ASP THR ARG
SEQRES 19 A 258 TYR ARG GLN PHE LEU CYS ASN VAL ASN ASP PRO ALA LEU
SEQRES 20 A 258 SER ASP PHE ARG THR ASN ASN ARG HIS CYS GLN
HET SCN A 301 3
HET SCN A 302 3
HET SCN A 303 3
HET SCN A 304 3
HETNAM SCN THIOCYANATE ION
FORMUL 2 SCN 4(C N S 1-)
FORMUL 6 HOH *315(H2 O)
HELIX 1 1 ARG A 47 ALA A 52 5 6
HELIX 2 2 SER A 64 VAL A 68 5 5
HELIX 3 3 ASP A 98 SER A 101 5 4
HELIX 4 4 LEU A 102 HIS A 112 1 11
HELIX 5 5 TYR A 127 SER A 145 1 19
HELIX 6 6 PRO A 147 ALA A 152 1 6
HELIX 7 7 SER A 165 ASN A 178 1 14
HELIX 8 8 HIS A 218 LEU A 226 1 9
HELIX 9 9 PHE A 243 SER A 247 5 5
HELIX 10 10 ASN A 249 ASP A 265 1 17
HELIX 11 11 ASP A 267 LEU A 274 5 8
HELIX 12 12 ASN A 289 GLN A 293 5 5
SHEET 1 A 6 VAL A 58 VAL A 63 0
SHEET 2 A 6 GLY A 74 PRO A 79 -1 O ILE A 76 N TYR A 61
SHEET 3 A 6 VAL A 115 ILE A 119 -1 O VAL A 116 N TYR A 77
SHEET 4 A 6 PHE A 86 SER A 92 1 N ILE A 89 O VAL A 115
SHEET 5 A 6 LEU A 154 HIS A 164 1 O ASP A 155 N PHE A 86
SHEET 6 A 6 ALA A 184 LEU A 187 1 O LEU A 187 N GLY A 163
SHEET 1 B 3 VAL A 202 ALA A 207 0
SHEET 2 B 3 LYS A 232 LEU A 237 1 O VAL A 235 N GLY A 206
SHEET 3 B 3 LEU A 282 THR A 287 -1 O ARG A 286 N TYR A 234
SSBOND 1 CYS A 275 CYS A 292 1555 1555 2.05
SITE 1 AC1 5 GLY A 42 TYR A 223 ARG A 286 HOH A 452
SITE 2 AC1 5 HOH A 527
SITE 1 AC2 5 THR A 96 ARG A 124 PRO A 231 ARG A 290
SITE 2 AC2 5 HOH A 469
SITE 1 AC3 4 SER A 48 SER A 69 THR A 144 SER A 145
SITE 1 AC4 8 ARG A 47 ASN A 276 VAL A 277 ASN A 278
SITE 2 AC4 8 ASP A 279 HOH A 458 HOH A 493 HOH A 544
CRYST1 40.911 71.084 72.726 90.00 90.00 90.00 P 21 21 21 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 0.024443 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014068 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013750 0.00000
TER 1963 GLN A 293
MASTER 279 0 4 12 9 0 7 6 2289 1 14 20
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