HEADER PROTEIN BINDING 02-JUL-01 1JIE
TITLE CRYSTAL STRUCTURE OF BLEOMYCIN-BINDING PROTEIN FROM BLEOMYCIN-
TITLE 2 PRODUCING STREPTOMYCES VERTICILLUS COMPLEXED WITH METAL-FREE
TITLE 3 BLEOMYCIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BLEOMYCIN-BINDING PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES VERTICILLUS;
SOURCE 3 ORGANISM_TAXID: 29309;
SOURCE 4 GENE: BLMA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HB101;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PKKTRP
KEYWDS PROTEIN-LIGAND COMPLEX, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SUGIYAMA,T.KUMAGAI,M.HAYASHIDA,M.MARUYAMA,Y.MATOBA
REVDAT 5 25-OCT-23 1JIE 1 REMARK
REVDAT 4 04-OCT-17 1JIE 1 REMARK
REVDAT 3 24-FEB-09 1JIE 1 VERSN
REVDAT 2 18-DEC-02 1JIE 1 REMARK
REVDAT 1 06-FEB-02 1JIE 0
JRNL AUTH M.SUGIYAMA,T.KUMAGAI,M.HAYASHIDA,M.MARUYAMA,Y.MATOBA
JRNL TITL THE 1.6-A CRYSTAL STRUCTURE OF THE COPPER(II)-BOUND
JRNL TITL 2 BLEOMYCIN COMPLEXED WITH THE BLEOMYCIN-BINDING PROTEIN FROM
JRNL TITL 3 BLEOMYCIN-PRODUCING STREPTOMYCES VERTICILLUS.
JRNL REF J.BIOL.CHEM. V. 277 2311 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11706014
JRNL DOI 10.1074/JBC.M103278200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.KAWANO,T.KUMAGAI,K.MUTA,Y.MATOBA,J.DAVIES,M.SUGIYAMA
REMARK 1 TITL THE 1.5 A CRYSTAL STRUCTURE OF A BLEOMYCIN RESISTANCE
REMARK 1 TITL 2 DETERMINANT FROM BLEOMYCIN-PRODUCING STREPTOMYCES
REMARK 1 TITL 3 VERTICILLUS
REMARK 1 REF J.MOL.BIOL. V. 295 915 2000
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1999.3404
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.MARUYAMA,T.KUMAGAI,Y.MATOBA,M.HAYASHIDA,T.FUJII,Y.HATA,
REMARK 1 AUTH 2 M.SUGIYAMA
REMARK 1 TITL CRYSTAL STRUCTURES OF THE TRANSPOSON TN5-CARRIED BLEOMYCIN
REMARK 1 TITL 2 RESISTANCE DETERMINANT UNCOMPLEXED AND COMPLEXED WITH
REMARK 1 TITL 3 BLEOMYCIN
REMARK 1 REF J.BIOL.CHEM. V. 276 9992 2001
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.M009874200
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.KUMAGAI,K.MUTA,Y.MATOBA,Y.KAWANO,N.KAMIYA,J.DAVIES,
REMARK 1 AUTH 2 M.SUGIYAMA
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES OF
REMARK 1 TITL 2 BLEOMYCIN-BINDING PROTEIN FROM BLEOMYCIN-PRODUCING
REMARK 1 TITL 3 STREPTOMYCES VERTICILLUS
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 54 127 1998
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444997008871
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 75.9
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.156
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.160
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 10.900
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1862
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 17018
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.143
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.148
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 11.100
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 1592
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 14369
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1868
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 192
REMARK 3 SOLVENT ATOMS : 139
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2199.0
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 5
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 8949
REMARK 3 NUMBER OF RESTRAINTS : 8738
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 ANGLE DISTANCES (A) : 0.030
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.022
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.050
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.060
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.010
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.040
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JIE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013806.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-99
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : R-AXIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19023
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 80.3
REMARK 200 DATA REDUNDANCY : 3.480
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 55.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.16900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.250
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1QTO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, AMMONIUM ACETATE, SODIUM
REMARK 280 CACODYLATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
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 41.71000
REMARK 290 SMTRY3 2 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HOMODIMER.
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: 6290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PHE A 33 CB - CG - CD1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 42 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 109 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP B 270 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 35 -144.95 -142.88
REMARK 500 ASP A 70 87.11 -152.13
REMARK 500 ASP B 235 -146.13 -130.84
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 BLM B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BLM A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QTO RELATED DB: PDB
REMARK 900 1QTO CONTAINS THE SAME PROTEIN UNCOMPLEXED WITH BLEOMYCIN
REMARK 900 RELATED ID: 1ECS RELATED DB: PDB
REMARK 900 1ECS CONTAINS THE SIMILAR PROTEIN(BLEOMYCIN RESISTANCE PROTEIN)
REMARK 900 UNCOMPLEXED WITH BLEOMYCIN
REMARK 900 RELATED ID: 1EWJ RELATED DB: PDB
REMARK 900 1EWJ CONTAINS THE SIMILAR PROTEIN(BLEOMYCIN RESISTANCE DETERMINANT)
REMARK 900 COMPLEXED WITH METAL-FREE BLEOMYCIN
REMARK 900 RELATED ID: 1JIF RELATED DB: PDB
REMARK 900 1JIF CONTAINS THE SAME PROTEIN COMPLEXED WITH COPPER(II)-BLEOMYCIN
DBREF 1JIE A 1 122 UNP Q53793 Q53793_9ACTO 1 122
DBREF 1JIE B 201 322 UNP Q53793 Q53793_9ACTO 1 122
SEQRES 1 A 122 MET VAL LYS PHE LEU GLY ALA VAL PRO VAL LEU THR ALA
SEQRES 2 A 122 VAL ASP VAL PRO ALA ASN VAL SER PHE TRP VAL ASP THR
SEQRES 3 A 122 LEU GLY PHE GLU LYS ASP PHE GLY ASP ARG ASP PHE ALA
SEQRES 4 A 122 GLY VAL ARG ARG GLY ASP ILE ARG LEU HIS ILE SER ARG
SEQRES 5 A 122 THR GLU HIS GLN ILE VAL ALA ASP ASN THR SER ALA TRP
SEQRES 6 A 122 ILE GLU VAL THR ASP PRO ASP ALA LEU HIS GLU GLU TRP
SEQRES 7 A 122 ALA ARG ALA VAL SER THR ASP TYR ALA ASP THR SER GLY
SEQRES 8 A 122 PRO ALA MET THR PRO VAL GLY GLU SER PRO ALA GLY ARG
SEQRES 9 A 122 GLU PHE ALA VAL ARG ASP PRO ALA GLY ASN CYS VAL HIS
SEQRES 10 A 122 PHE THR ALA GLY GLU
SEQRES 1 B 122 MET VAL LYS PHE LEU GLY ALA VAL PRO VAL LEU THR ALA
SEQRES 2 B 122 VAL ASP VAL PRO ALA ASN VAL SER PHE TRP VAL ASP THR
SEQRES 3 B 122 LEU GLY PHE GLU LYS ASP PHE GLY ASP ARG ASP PHE ALA
SEQRES 4 B 122 GLY VAL ARG ARG GLY ASP ILE ARG LEU HIS ILE SER ARG
SEQRES 5 B 122 THR GLU HIS GLN ILE VAL ALA ASP ASN THR SER ALA TRP
SEQRES 6 B 122 ILE GLU VAL THR ASP PRO ASP ALA LEU HIS GLU GLU TRP
SEQRES 7 B 122 ALA ARG ALA VAL SER THR ASP TYR ALA ASP THR SER GLY
SEQRES 8 B 122 PRO ALA MET THR PRO VAL GLY GLU SER PRO ALA GLY ARG
SEQRES 9 B 122 GLU PHE ALA VAL ARG ASP PRO ALA GLY ASN CYS VAL HIS
SEQRES 10 B 122 PHE THR ALA GLY GLU
HET BLM A 402 96
HET BLM B 401 96
HETNAM BLM BLEOMYCIN A2
HETSYN BLM N1-[3-(DIMETHYLSULFONIO)-PROPYL]BLEOMYCINAMIDE
FORMUL 3 BLM 2(C55 H85 N17 O21 S3)
FORMUL 5 HOH *139(H2 O)
HELIX 1 1 ASP A 15 THR A 26 1 12
HELIX 2 2 HIS A 55 ASP A 60 1 6
HELIX 3 3 ASP A 70 ARG A 80 1 11
HELIX 4 4 ASP B 215 THR B 226 1 12
HELIX 5 5 HIS B 255 ASP B 260 1 6
HELIX 6 6 ASP B 270 ALA B 279 1 10
SHEET 1 A 8 GLU A 30 GLY A 34 0
SHEET 2 A 8 PHE A 38 ARG A 43 -1 O GLY A 40 N ASP A 32
SHEET 3 A 8 ILE A 46 ARG A 52 -1 O ILE A 46 N ARG A 43
SHEET 4 A 8 PHE A 4 ALA A 13 1 O PRO A 9 N HIS A 49
SHEET 5 A 8 SER B 263 VAL B 268 -1 O SER B 263 N VAL A 10
SHEET 6 A 8 CYS B 315 ALA B 320 1 O CYS B 315 N ALA B 264
SHEET 7 A 8 GLU B 305 ARG B 309 -1 O PHE B 306 N PHE B 318
SHEET 8 A 8 ALA B 293 MET B 294 -1 O ALA B 293 N ARG B 309
SHEET 1 B 8 GLU B 230 GLY B 234 0
SHEET 2 B 8 PHE B 238 ARG B 243 -1 O GLY B 240 N ASP B 232
SHEET 3 B 8 ILE B 246 ARG B 252 -1 O ILE B 246 N ARG B 243
SHEET 4 B 8 PHE B 204 ALA B 213 1 O PRO B 209 N HIS B 249
SHEET 5 B 8 SER A 63 VAL A 68 -1 O SER A 63 N VAL B 210
SHEET 6 B 8 CYS A 115 ALA A 120 1 O CYS A 115 N ALA A 64
SHEET 7 B 8 GLY A 103 ARG A 109 -1 O ARG A 104 N ALA A 120
SHEET 8 B 8 ALA A 93 MET A 94 -1 O ALA A 93 N ARG A 109
SHEET 1 C 8 GLU B 230 GLY B 234 0
SHEET 2 C 8 PHE B 238 ARG B 243 -1 O GLY B 240 N ASP B 232
SHEET 3 C 8 ILE B 246 ARG B 252 -1 O ILE B 246 N ARG B 243
SHEET 4 C 8 PHE B 204 ALA B 213 1 O PRO B 209 N HIS B 249
SHEET 5 C 8 SER A 63 VAL A 68 -1 O SER A 63 N VAL B 210
SHEET 6 C 8 CYS A 115 ALA A 120 1 O CYS A 115 N ALA A 64
SHEET 7 C 8 GLY A 103 ARG A 109 -1 O ARG A 104 N ALA A 120
SHEET 8 C 8 GLY A 98 SER A 100 -1 N GLY A 98 O GLU A 105
SITE 1 AC1 31 LYS A 3 ASP A 32 PHE A 33 PHE A 38
SITE 2 AC1 31 ARG A 47 SER A 51 ARG A 52 ARG A 104
SITE 3 AC1 31 ALA B 259 ASP B 260 ASN B 261 THR B 262
SITE 4 AC1 31 TRP B 265 TYR B 286 ALA B 302 ARG B 309
SITE 5 AC1 31 GLY B 313 CYS B 315 GLU B 322 HOH B 520
SITE 6 AC1 31 HOH B 522 HOH B 533 HOH B 555 HOH B 569
SITE 7 AC1 31 HOH B 571 HOH B 575 HOH B 580 HOH B 592
SITE 8 AC1 31 HOH B 595 HOH B 609 HOH B 628
SITE 1 AC2 33 ALA A 59 ASP A 60 ASN A 61 THR A 62
SITE 2 AC2 33 TRP A 65 TYR A 86 THR A 89 PRO A 101
SITE 3 AC2 33 ALA A 102 ARG A 109 GLY A 113 CYS A 115
SITE 4 AC2 33 HIS A 117 GLU A 122 HOH A 511 HOH A 512
SITE 5 AC2 33 HOH A 513 HOH A 530 HOH A 550 HOH A 556
SITE 6 AC2 33 HOH A 559 HOH A 585 HOH A 603 HOH A 605
SITE 7 AC2 33 HOH A 620 HOH A 621 PHE B 233 PHE B 238
SITE 8 AC2 33 ARG B 247 SER B 251 ARG B 252 GLU B 299
SITE 9 AC2 33 ARG B 304
CRYST1 35.520 83.420 43.240 90.00 104.88 90.00 P 1 21 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 0.028153 0.000000 0.007480 0.00000
SCALE2 0.000000 0.011988 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023929 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
