HEADER HYDROLASE 24-SEP-12 4H9H
TITLE RADIATION DAMAGE STUDY OF LYSOZYME - 0.98 MGY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C, ALLERGEN GAL D IV;
COMPND 5 EC: 3.2.1.17
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: BANTAM,CHICKENS;
SOURCE 4 ORGANISM_TAXID: 9031
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.A.SUTTON
REVDAT 4 15-NOV-17 4H9H 1 REMARK
REVDAT 3 01-JAN-14 4H9H 1 JRNL
REVDAT 2 11-DEC-13 4H9H 1 JRNL
REVDAT 1 15-MAY-13 4H9H 0
JRNL AUTH K.A.SUTTON,P.J.BLACK,K.R.MERCER,E.F.GARMAN,R.L.OWEN,
JRNL AUTH 2 E.H.SNELL,W.A.BERNHARD
JRNL TITL INSIGHTS INTO THE MECHANISM OF X-RAY-INDUCED DISULFIDE-BOND
JRNL TITL 2 CLEAVAGE IN LYSOZYME CRYSTALS BASED ON EPR, OPTICAL
JRNL TITL 3 ABSORPTION AND X-RAY DIFFRACTION STUDIES.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 69 2381 2013
JRNL REFN ISSN 0907-4449
JRNL PMID 24311579
JRNL DOI 10.1107/S0907444913022117
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.2_862
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.92
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 36583
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1829
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 26.9235 - 2.8211 0.95 2752 149 0.1902 0.1820
REMARK 3 2 2.8211 - 2.2395 0.98 2705 149 0.1879 0.1973
REMARK 3 3 2.2395 - 1.9565 0.99 2679 159 0.1830 0.1917
REMARK 3 4 1.9565 - 1.7777 0.99 2700 120 0.1819 0.2151
REMARK 3 5 1.7777 - 1.6503 1.00 2669 158 0.1864 0.2234
REMARK 3 6 1.6503 - 1.5530 1.00 2641 156 0.1779 0.2041
REMARK 3 7 1.5530 - 1.4752 1.00 2640 159 0.1907 0.2223
REMARK 3 8 1.4752 - 1.4110 1.00 2692 129 0.1897 0.2114
REMARK 3 9 1.4110 - 1.3567 1.00 2691 105 0.2115 0.2414
REMARK 3 10 1.3567 - 1.3099 1.00 2637 139 0.2124 0.2531
REMARK 3 11 1.3099 - 1.2689 1.00 2661 120 0.2068 0.2112
REMARK 3 12 1.2689 - 1.2327 1.00 2637 150 0.2189 0.2086
REMARK 3 13 1.2327 - 1.2002 1.00 2650 136 0.2320 0.2466
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.60
REMARK 3 K_SOL : 0.46
REMARK 3 B_SOL : 52.20
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.330
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.31
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.40560
REMARK 3 B22 (A**2) : 0.40560
REMARK 3 B33 (A**2) : -0.81130
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 1061
REMARK 3 ANGLE : 1.148 1431
REMARK 3 CHIRALITY : 0.087 147
REMARK 3 PLANARITY : 0.005 190
REMARK 3 DIHEDRAL : 13.038 384
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4H9H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-OCT-12.
REMARK 100 THE DEPOSITION ID IS D_1000075187.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36618
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 4.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.03200
REMARK 200 R SYM (I) : 0.03000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.31100
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7.5% SODIUM CHLORIDE, 100 MM SODIUM
REMARK 280 ACETATE PH 4.8, 25% ETHYLENE GLYCOL, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 18.43500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.38650
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.38650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.65250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.38650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.38650
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 9.21750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.38650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.38650
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.65250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.38650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.38650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 9.21750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 18.43500
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 346 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 380 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 381 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 311 O HOH A 409 2.17
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 ARG A 68 27.17 -141.49
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 CL A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4H8X RELATED DB: PDB
REMARK 900 SAME PROTEIN CRYSTAL, DIFFERENT ABSORBED DOSE
REMARK 900 RELATED ID: 4H8Y RELATED DB: PDB
REMARK 900 SAME PROTEIN CRYSTAL, DIFFERENT ABSORBED DOSE
REMARK 900 RELATED ID: 4H8Z RELATED DB: PDB
REMARK 900 SAME PROTEIN CRYSTAL, DIFFERENT ABSORBED DOSE
REMARK 900 RELATED ID: 4H90 RELATED DB: PDB
REMARK 900 SAME PROTEIN CRYSTAL, DIFFERENT ABSORBED DOSE
REMARK 900 RELATED ID: 4H91 RELATED DB: PDB
REMARK 900 SAME PROTEIN CRYSTAL, DIFFERENT ABSORBED DOSE
REMARK 900 RELATED ID: 4H92 RELATED DB: PDB
REMARK 900 SAME PROTEIN CRYSTAL, DIFFERENT ABSORBED DOSE
REMARK 900 RELATED ID: 4H93 RELATED DB: PDB
REMARK 900 SAME PROTEIN CRYSTAL, DIFFERENT ABSORBED DOSE
REMARK 900 RELATED ID: 4H94 RELATED DB: PDB
REMARK 900 SAME PROTEIN CRYSTAL, DIFFERENT ABSORBED DOSE
REMARK 900 RELATED ID: 4H9A RELATED DB: PDB
REMARK 900 SAME PROTEIN CRYSTAL, DIFFERENT ABSORBED DOSE
REMARK 900 RELATED ID: 4H9B RELATED DB: PDB
REMARK 900 SAME PROTEIN CRYSTAL, DIFFERENT ABSORBED DOSE
REMARK 900 RELATED ID: 4H9C RELATED DB: PDB
REMARK 900 SAME PROTEIN CRYSTAL, DIFFERENT ABSORBED DOSE
REMARK 900 RELATED ID: 4H9E RELATED DB: PDB
REMARK 900 SAME PROTEIN CRYSTAL, DIFFERENT ABSORBED DOSE
REMARK 900 RELATED ID: 4H9F RELATED DB: PDB
REMARK 900 SAME PROTEIN CRYSTAL, DIFFERENT ABSORBED DOSE
REMARK 900 RELATED ID: 4H9I RELATED DB: PDB
REMARK 900 SAME PROTEIN CRYSTAL, DIFFERENT ABSORBED DOSE
DBREF 4H9H A 1 129 UNP P00698 LYSC_CHICK 19 147
SEQRES 1 A 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 A 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 A 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 A 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 A 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 A 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 A 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 A 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 A 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 A 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
HET CL A 201 1
HET EDO A 202 4
HET CL A 203 1
HET CL A 204 1
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 CL 3(CL 1-)
FORMUL 3 EDO C2 H6 O2
FORMUL 6 HOH *109(H2 O)
HELIX 1 1 GLY A 4 HIS A 15 1 12
HELIX 2 2 ASN A 19 TYR A 23 5 5
HELIX 3 3 SER A 24 ASN A 37 1 14
HELIX 4 4 PRO A 79 SER A 85 5 7
HELIX 5 5 ILE A 88 SER A 100 1 13
HELIX 6 6 ASN A 103 ALA A 107 5 5
HELIX 7 7 TRP A 108 CYS A 115 1 8
HELIX 8 8 ASP A 119 ARG A 125 5 7
SHEET 1 A 3 THR A 43 ARG A 45 0
SHEET 2 A 3 THR A 51 TYR A 53 -1 O ASP A 52 N ASN A 44
SHEET 3 A 3 ILE A 58 ASN A 59 -1 O ILE A 58 N TYR A 53
SSBOND 1 CYS A 6 CYS A 127 1555 1555 2.06
SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.10
SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.04
SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.05
SITE 1 AC1 4 GLY A 67 ARG A 68 THR A 69 SER A 72
SITE 1 AC2 8 GLN A 57 ILE A 58 ASN A 59 TRP A 63
SITE 2 AC2 8 ALA A 107 HOH A 336 HOH A 351 HOH A 358
SITE 1 AC3 3 TYR A 23 ASN A 113 HOH A 409
SITE 1 AC4 3 SER A 24 GLY A 26 GLN A 121
CRYST1 78.773 78.773 36.870 90.00 90.00 90.00 P 43 21 2 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 0.012695 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012695 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027122 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
