HEADER HYDROLASE 30-JAN-04 1S82
TITLE PORCINE TRYPSIN COMPLEXED WITH BORATE AND ETHYLENE GLYCOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPSIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.21.4
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 ORGAN: PANCREAS
KEYWDS HYDROLASE, SERINE PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.R.TRANSUE,J.M.KRAHN,S.A.GABEL,E.F.DEROSE,R.E.LONDON
REVDAT 4 23-AUG-23 1S82 1 REMARK LINK
REVDAT 3 11-OCT-17 1S82 1 REMARK
REVDAT 2 24-FEB-09 1S82 1 VERSN
REVDAT 1 16-MAR-04 1S82 0
JRNL AUTH T.R.TRANSUE,J.M.KRAHN,S.A.GABEL,E.F.DEROSE,R.E.LONDON
JRNL TITL X-RAY AND NMR CHARACTERIZATION OF COVALENT COMPLEXES OF
JRNL TITL 2 TRYPSIN, BORATE, AND ALCOHOLS.
JRNL REF BIOCHEMISTRY V. 43 2829 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15005618
JRNL DOI 10.1021/BI035782Y
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : AMBER98
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 17042
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 SET) : 0.176
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 897
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1642
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 245
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.38700
REMARK 3 B22 (A**2) : -1.86300
REMARK 3 B33 (A**2) : -1.52400
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1S82 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000021484.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MSC/YALE DOUBLE FOCUSING MIRRORS
REMARK 200 OPTICS : MSC/YALE DOUBLE FOCUSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17042
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 6.594
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.8073
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.33
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.36500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.563
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1AKS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M MGCL2, 50MM HEPES, 5MM CACL2,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K, PH 8
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 37.95700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 23.36800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.76500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 23.36800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.95700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.76500
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 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 HIS A 71 -59.29 -128.13
REMARK 500 SER A 147 -67.02 -90.13
REMARK 500 SER A 214 -68.95 -124.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 70 OE1
REMARK 620 2 ASN A 72 O 89.1
REMARK 620 3 VAL A 75 O 164.6 85.9
REMARK 620 4 GLU A 77 OE1 104.2 86.0 90.0
REMARK 620 5 GLU A 80 OE2 95.0 172.3 91.7 86.6
REMARK 620 6 HOH A 293 O 78.1 92.4 87.6 177.2 94.8
REMARK 620 7 HOH A 468 O 90.4 90.1 104.2 14.5 83.4 168.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 4 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 EDO A 5 O2
REMARK 620 2 ASP A 189 OD1 168.9
REMARK 620 3 SER A 190 O 101.0 77.3
REMARK 620 4 SER A 190 OG 103.2 87.1 74.8
REMARK 620 5 HOH A 300 O 78.2 109.9 142.4 69.0
REMARK 620 6 HOH A 454 O 86.4 83.0 99.4 169.5 117.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 11
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SBE A 12
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1S5S RELATED DB: PDB
REMARK 900 RELATED ID: 1S6H RELATED DB: PDB
REMARK 900 RELATED ID: 1S6F RELATED DB: PDB
REMARK 900 RELATED ID: 1S81 RELATED DB: PDB
REMARK 900 RELATED ID: 1S83 RELATED DB: PDB
REMARK 900 RELATED ID: 1S84 RELATED DB: PDB
REMARK 900 RELATED ID: 1S85 RELATED DB: PDB
DBREF 1S82 A 16 245 UNP P00761 TRYP_PIG 9 231
SEQRES 1 A 223 ILE VAL GLY GLY TYR THR CYS ALA ALA ASN SER ILE PRO
SEQRES 2 A 223 TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY
SEQRES 3 A 223 GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA
SEQRES 4 A 223 HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 A 223 HIS ASN ILE ASP VAL LEU GLU GLY ASN GLU GLN PHE ILE
SEQRES 6 A 223 ASN ALA ALA LYS ILE ILE THR HIS PRO ASN PHE ASN GLY
SEQRES 7 A 223 ASN THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER
SEQRES 8 A 223 SER PRO ALA THR LEU ASN SER ARG VAL ALA THR VAL SER
SEQRES 9 A 223 LEU PRO ARG SER CYS ALA ALA ALA GLY THR GLU CYS LEU
SEQRES 10 A 223 ILE SER GLY TRP GLY ASN THR LYS SER SER GLY SER SER
SEQRES 11 A 223 TYR PRO SER LEU LEU GLN CYS LEU LYS ALA PRO VAL LEU
SEQRES 12 A 223 SER ASP SER SER CYS LYS SER SER TYR PRO GLY GLN ILE
SEQRES 13 A 223 THR GLY ASN MET ILE CYS VAL GLY PHE LEU GLU GLY GLY
SEQRES 14 A 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 A 223 CYS ASN GLY GLN LEU GLN GLY ILE VAL SER TRP GLY TYR
SEQRES 16 A 223 GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS
SEQRES 17 A 223 VAL CYS ASN TYR VAL ASN TRP ILE GLN GLN THR ILE ALA
SEQRES 18 A 223 ALA ASN
HET CA A 1 1
HET SO4 A 2 5
HET SO4 A 3 5
HET NA A 4 1
HET EDO A 5 10
HET EDO A 6 10
HET EDO A 7 10
HET EDO A 8 10
HET EDO A 9 10
HET EDO A 10 10
HET EDO A 11 10
HET SBE A 12 11
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
HETNAM NA SODIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SBE 1,3,2-DIOXABOROLAN-2-OL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 CA CA 2+
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 NA NA 1+
FORMUL 6 EDO 7(C2 H6 O2)
FORMUL 13 SBE C2 H5 B O3
FORMUL 14 HOH *245(H2 O)
HELIX 1 1 ALA A 55 TYR A 59 5 5
HELIX 2 2 SER A 164 TYR A 172 1 9
HELIX 3 3 TYR A 234 ASN A 245 1 12
SHEET 1 A 7 TYR A 20 THR A 21 0
SHEET 2 A 7 GLN A 156 PRO A 161 -1 O CYS A 157 N TYR A 20
SHEET 3 A 7 GLU A 135 GLY A 140 -1 N ILE A 138 O LEU A 158
SHEET 4 A 7 PRO A 198 CYS A 201 -1 O VAL A 200 N LEU A 137
SHEET 5 A 7 GLN A 204 TRP A 215 -1 O GLN A 204 N CYS A 201
SHEET 6 A 7 GLY A 226 LYS A 230 -1 O VAL A 227 N TRP A 215
SHEET 7 A 7 MET A 180 VAL A 183 -1 N ILE A 181 O TYR A 228
SHEET 1 B 7 GLN A 30 ASN A 34 0
SHEET 2 B 7 HIS A 40 ASN A 48 -1 O CYS A 42 N LEU A 33
SHEET 3 B 7 TRP A 51 SER A 54 -1 O VAL A 53 N SER A 45
SHEET 4 B 7 MET A 104 LEU A 108 -1 O MET A 104 N SER A 54
SHEET 5 B 7 GLN A 81 THR A 90 -1 N ALA A 86 O LYS A 107
SHEET 6 B 7 GLN A 64 LEU A 67 -1 N VAL A 65 O ILE A 83
SHEET 7 B 7 GLN A 30 ASN A 34 -1 N SER A 32 O ARG A 66
SSBOND 1 CYS A 22 CYS A 157 1555 1555 1.97
SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.06
SSBOND 3 CYS A 128 CYS A 232 1555 1555 2.03
SSBOND 4 CYS A 136 CYS A 201 1555 1555 2.06
SSBOND 5 CYS A 168 CYS A 182 1555 1555 2.05
SSBOND 6 CYS A 191 CYS A 220 1555 1555 2.06
LINK BD SBE A 12 OG SER A 195 1555 1555 1.39
LINK CA CA A 1 OE1 GLU A 70 1555 1555 2.21
LINK CA CA A 1 O ASN A 72 1555 1555 2.09
LINK CA CA A 1 O VAL A 75 1555 1555 2.11
LINK CA CA A 1 OE1BGLU A 77 1555 1555 2.29
LINK CA CA A 1 OE2 GLU A 80 1555 1555 2.13
LINK CA CA A 1 O HOH A 293 1555 1555 2.11
LINK CA CA A 1 O AHOH A 468 1555 1555 2.24
LINK NA NA A 4 O2 EDO A 5 1555 1555 2.24
LINK NA NA A 4 OD1 ASP A 189 1555 1555 2.74
LINK NA NA A 4 O SER A 190 1555 1555 2.59
LINK NA NA A 4 OG SER A 190 1555 1555 2.63
LINK NA NA A 4 O HOH A 300 1555 1555 2.69
LINK NA NA A 4 O HOH A 454 1555 1555 2.40
SITE 1 AC1 7 GLU A 70 ASN A 72 VAL A 75 GLU A 77
SITE 2 AC1 7 GLU A 80 HOH A 293 HOH A 468
SITE 1 AC2 6 ASN A 48 ARG A 66 HOH A 326 HOH A 412
SITE 2 AC2 6 HOH A 478 HOH A 490
SITE 1 AC3 5 ASN A 95 ASN A 97 THR A 98 HOH A 413
SITE 2 AC3 5 HOH A 483
SITE 1 AC4 6 EDO A 5 ASP A 189 SER A 190 GLY A 226
SITE 2 AC4 6 HOH A 300 HOH A 454
SITE 1 AC5 11 NA A 4 SBE A 12 SER A 190 CYS A 191
SITE 2 AC5 11 GLN A 192 SER A 195 VAL A 213 TRP A 215
SITE 3 AC5 11 GLY A 216 HOH A 261 HOH A 300
SITE 1 AC6 3 THR A 21 HOH A 299 HOH A 486
SITE 1 AC7 3 LYS A 87 LYS A 107 GLU A 135
SITE 1 AC8 7 GLY A 96 ASN A 97 LEU A 99 SER A 127
SITE 2 AC8 7 GLN A 204 GLN A 210 HOH A 385
SITE 1 AC9 9 SER A 37 LYS A 60 SER A 164 ASP A 165
SITE 2 AC9 9 SER A 166 HOH A 392 HOH A 395 HOH A 484
SITE 3 AC9 9 HOH A 485
SITE 1 BC1 6 ILE A 47 ASN A 48 TYR A 217 GLN A 239
SITE 2 BC1 6 ILE A 242 HOH A 479
SITE 1 BC2 9 HIS A 91 ASN A 101 GLY A 148 SER A 149
SITE 2 BC2 9 ASN A 179 ASN A 233 HOH A 306 HOH A 316
SITE 3 BC2 9 HOH A 343
SITE 1 BC3 9 EDO A 5 PHE A 41 HIS A 57 GLN A 192
SITE 2 BC3 9 GLY A 193 SER A 195 HOH A 282 HOH A 376
SITE 3 BC3 9 HOH A 403
CRYST1 75.914 55.530 46.736 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 0.013173 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018008 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021397 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
