HEADER ENDONUCLEASE 12-JAN-98 1A2W
TITLE CRYSTAL STRUCTURE OF A 3D DOMAIN-SWAPPED DIMER OF BOVINE PANCREATIC
TITLE 2 RIBONUCLEASE A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SWAPPED HELICAL DOMAIN;
COMPND 5 EC: 3.1.27.5;
COMPND 6 OTHER_DETAILS: SWAPPED HELICAL DOMAIN CONTAINS RESIDUES 1-15, HINGE
COMPND 7 LOOPS CONTAIN RESIDUES 16-22, MAJOR DOMAIN CONTAINS RESIDUES 23-124
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: PANCREAS
KEYWDS ENDONUCLEASE, RIBONUCLEASE, DOMAIN SWAPPING, HYDROLASE, PROTEIN-
KEYWDS 2 PROTEIN INTERACTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.LIU,P.J.HART,M.P.SCHLUNEGGER,D.S.EISENBERG
REVDAT 3 02-AUG-23 1A2W 1 REMARK
REVDAT 2 24-FEB-09 1A2W 1 VERSN
REVDAT 1 29-APR-98 1A2W 0
JRNL AUTH Y.LIU,P.J.HART,M.P.SCHLUNEGGER,D.EISENBERG
JRNL TITL THE CRYSTAL STRUCTURE OF A 3D DOMAIN-SWAPPED DIMER OF RNASE
JRNL TITL 2 A AT A 2.1-A RESOLUTION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 95 3437 1998
JRNL REFN ISSN 0027-8424
JRNL PMID 9520384
JRNL DOI 10.1073/PNAS.95.7.3437
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.MAZZARELLA,S.CAPASSO,D.DEMASI,G.DI LORENZO,C.A.MATTIA,
REMARK 1 AUTH 2 A.ZAGARI
REMARK 1 TITL BOVINE SEMINAL RIBONUCLEASE: STRUCTURE AT 1.9 A RESOLUTION
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 49 389 1993
REMARK 1 REFN ISSN 0907-4449
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.L.BIRDSALL,A.MCPHERSON
REMARK 1 TITL CRYSTAL STRUCTURE DISPOSITION OF THYMIDYLIC ACID TETRAMER IN
REMARK 1 TITL 2 COMPLEX WITH RIBONUCLEASE A
REMARK 1 REF J.BIOL.CHEM. V. 267 22230 1992
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 16471
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) : 0.192
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1598
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1776
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE : 0.2670
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.16
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 197
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1902
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 92
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 10.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.560
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.380
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.690 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.220 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 0.940 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.550 ; 2.500
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 : PARAM19.SOL
REMARK 3 PARAMETER FILE 2 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 3 : PARAM.SO4
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 2 : TOPH19.PEP
REMARK 3 TOPOLOGY FILE 3 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1A2W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170324.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : OCT-97
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.5
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16601
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.26300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PDB ENTRY 1RTB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM PHOSPHATE BUFFER (PH 7.5) 1.6 M
REMARK 280 AMMONIUM SULFATE 0.6 M NACL 2% PEG400
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.27333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.13667
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 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: 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 CL CL A 501 O HOH A 444 1.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CL CL B 502 O HOH A 430 2654 1.97
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 GLN A 60 -146.38 -119.23
REMARK 500 LYS A 61 105.01 -56.16
REMARK 500 ASN A 71 30.79 -95.24
REMARK 500 ASP B 14 81.37 -156.91
REMARK 500 LYS B 37 -75.04 -50.99
REMARK 500 GLN B 60 -130.47 -112.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AVE
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE ACTIVE SITE CONTAINS RESIDUES FROM DIFFERENT
REMARK 800 SUBUNITS.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 601
DBREF 1A2W A 1 124 UNP P61823 RNAS1_BOVIN 27 150
DBREF 1A2W B 1 124 UNP P61823 RNAS1_BOVIN 27 150
SEQRES 1 A 124 LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET
SEQRES 2 A 124 ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS
SEQRES 3 A 124 ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG
SEQRES 4 A 124 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA
SEQRES 5 A 124 ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS
SEQRES 6 A 124 LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR
SEQRES 7 A 124 MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS
SEQRES 8 A 124 TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS
SEQRES 9 A 124 HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO
SEQRES 10 A 124 VAL HIS PHE ASP ALA SER VAL
SEQRES 1 B 124 LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET
SEQRES 2 B 124 ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS
SEQRES 3 B 124 ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG
SEQRES 4 B 124 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA
SEQRES 5 B 124 ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS
SEQRES 6 B 124 LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR
SEQRES 7 B 124 MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS
SEQRES 8 B 124 TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS
SEQRES 9 B 124 HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO
SEQRES 10 B 124 VAL HIS PHE ASP ALA SER VAL
HET CL A 501 1
HET CL B 502 1
HET SO4 B 601 5
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
FORMUL 3 CL 2(CL 1-)
FORMUL 5 SO4 O4 S 2-
FORMUL 6 HOH *92(H2 O)
HELIX 1 1 ALA A 4 HIS A 12 1 9
HELIX 2 2 TYR A 25 SER A 32 1 8
HELIX 3 3 LEU A 51 SER A 59 1 9
HELIX 4 4 ALA B 4 HIS B 12 1 9
HELIX 5 5 THR B 17 SER B 32 1 16
HELIX 6 6 LEU B 51 SER B 59 1 9
SHEET 1 A 3 VAL A 43 VAL A 47 0
SHEET 2 A 3 MET A 79 GLU A 86 -1 N CYS A 84 O ASN A 44
SHEET 3 A 3 TYR A 97 LYS A 104 -1 N LYS A 104 O MET A 79
SHEET 1 B 4 LYS A 61 VAL A 63 0
SHEET 2 B 4 CYS A 72 GLN A 74 -1 N GLN A 74 O LYS A 61
SHEET 3 B 4 HIS A 105 ALA A 109 -1 N VAL A 108 O TYR A 73
SHEET 4 B 4 HIS A 119 VAL A 124 -1 N VAL A 124 O HIS A 105
SHEET 1 C 3 VAL B 43 VAL B 47 0
SHEET 2 C 3 MET B 79 GLU B 86 -1 N CYS B 84 O ASN B 44
SHEET 3 C 3 TYR B 97 LYS B 104 -1 N LYS B 104 O MET B 79
SHEET 1 D 4 LYS B 61 VAL B 63 0
SHEET 2 D 4 CYS B 72 GLN B 74 -1 N GLN B 74 O LYS B 61
SHEET 3 D 4 ILE B 106 ALA B 109 -1 N VAL B 108 O TYR B 73
SHEET 4 D 4 HIS B 119 SER B 123 -1 N ALA B 122 O ILE B 107
SSBOND 1 CYS A 26 CYS A 84 1555 1555 2.03
SSBOND 2 CYS A 40 CYS A 95 1555 1555 2.02
SSBOND 3 CYS A 58 CYS A 110 1555 1555 2.03
SSBOND 4 CYS A 65 CYS A 72 1555 1555 2.03
SSBOND 5 CYS B 26 CYS B 84 1555 1555 2.03
SSBOND 6 CYS B 40 CYS B 95 1555 1555 2.03
SSBOND 7 CYS B 58 CYS B 110 1555 1555 2.03
SSBOND 8 CYS B 65 CYS B 72 1555 1555 2.03
CISPEP 1 TYR A 92 PRO A 93 0 0.16
CISPEP 2 ASN A 113 PRO A 114 0 0.00
CISPEP 3 TYR B 92 PRO B 93 0 0.16
CISPEP 4 ASN B 113 PRO B 114 0 0.14
SITE 1 AVE 3 HIS B 12 LYS A 41 HIS A 119
SITE 1 AC1 3 HIS A 119 HOH A 444 HIS B 12
SITE 1 AC2 3 ARG A 33 HOH A 430 ARG B 39
SITE 1 AC3 9 GLN A 11 HIS A 12 HOH A 403 HOH A 490
SITE 2 AC3 9 LYS B 41 HIS B 119 PHE B 120 HOH B 476
SITE 3 AC3 9 HOH B 481
CRYST1 57.000 57.000 81.410 90.00 90.00 120.00 P 32 6
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 0.017544 0.010129 0.000000 0.00000
SCALE2 0.000000 0.020258 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012284 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
