HEADER HORMONE/GROWTH FACTOR 01-JAN-01 1HTV
TITLE CRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN;
COMPND 3 CHAIN: A, C, E, G, I, K;
COMPND 4 FRAGMENT: INSULIN A CHAIN;
COMPND 5 SYNONYM: DESTRIPEPTIDE INSULIN (DTRI);
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: INSULIN;
COMPND 9 CHAIN: B, D, F, H, J, L;
COMPND 10 FRAGMENT: INSULIN B CHAIN;
COMPND 11 SYNONYM: DESTRIPEPTIDE INSULIN (DTRI);
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HELIX, BETA SHEET, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.YE,W.CHANG,D.LIANG
REVDAT 3 03-APR-24 1HTV 1 REMARK LINK
REVDAT 2 24-FEB-09 1HTV 1 VERSN
REVDAT 1 23-MAY-01 1HTV 0
JRNL AUTH J.YE,W.CHANG,D.LIANG
JRNL TITL CRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN:
JRNL TITL 2 IMPLICATIONS FOR INSULIN DISSOCIATION.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1547 18 2001
JRNL REFN ISSN 0006-3002
JRNL PMID 11343787
JRNL DOI 10.1016/S0167-4838(01)00160-1
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.YE,Y.MAO,L.GUI,W.CHANG,D.LIANG
REMARK 1 TITL CRYSTAL STRUCTURAL STUDIES OF DESTRIPEPTIDE (B28-B30)
REMARK 1 TITL 2 INSULIN
REMARK 1 REF SCI.CHINA,SER.B V. 43 178 2000
REMARK 1 REFN ISSN 1001-652X
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.MAO,M.LI,Z.WAN,T.JIANG,X.AN,D.LIANG,F.LIU,C.HUANG,L.CHEN,
REMARK 1 AUTH 2 M.HU
REMARK 1 TITL PREPARATION OF DESTRIPEPTIDE (B28-B30) INSULIN AND
REMARK 1 TITL 2 DESTETRAPEPTIDE (B27-B30) INSULIN AND PRELIMINARY X-RAY
REMARK 1 TITL 3 CRYSTALLOGRAPHIC STUDY OF DESTRIPEPTIDE INSULIN
REMARK 1 REF PROG.NAT.SCI. V. 9 241 1999
REMARK 1 REFN ISSN 1002-008X
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 83.9
REMARK 3 NUMBER OF REFLECTIONS : 17539
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) : 0.196
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1762
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.99
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 53.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1228
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 136
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.025
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2286
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 171
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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) : 0.20
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
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) : 0.17
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.580
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) : 2.310 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.780 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.690 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.460 ; 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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HTV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1000012580.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JAN-99
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 3
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17764
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.4
REMARK 200 DATA REDUNDANCY : 18.00
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.18900
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: AMORE
REMARK 200 STARTING MODEL: CRYSTAL STRUCTURE OF 2ZN INSULIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, DIMETHYLFORMAMIDE,
REMARK 280 ZINC ACETATE, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298.0K
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 24.90500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.30000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.77500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.30000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.90500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.77500
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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -188.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L
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 ASN B 203 N - CA - C ANGL. DEV. = 17.2 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 VAL B 202 -153.20 -145.20
REMARK 500 SER E 509 -164.23 -105.06
REMARK 500 SER G 712 -162.95 -105.32
REMARK 500 SER I 909 -167.68 -115.37
REMARK 500 VAL J1002 178.24 -52.22
REMARK 500 VAL L1202 48.90 -141.70
REMARK 500 HIS L1205 139.50 -32.07
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 ZN B1300 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 210 NE2
REMARK 620 2 HIS F 610 NE2 98.6
REMARK 620 3 HOH F1301 O 163.1 94.5
REMARK 620 4 HIS J1010 NE2 94.6 96.1 94.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1300
DBREF 1HTV A 101 121 UNP P01308 INS_HUMAN 90 110
DBREF 1HTV C 301 321 UNP P01308 INS_HUMAN 90 110
DBREF 1HTV E 501 521 UNP P01308 INS_HUMAN 90 110
DBREF 1HTV G 701 721 UNP P01308 INS_HUMAN 90 110
DBREF 1HTV I 901 921 UNP P01308 INS_HUMAN 90 110
DBREF 1HTV K 1101 1121 UNP P01308 INS_HUMAN 90 110
DBREF 1HTV B 201 227 UNP P01308 INS_HUMAN 25 51
DBREF 1HTV D 401 427 UNP P01308 INS_HUMAN 25 51
DBREF 1HTV F 601 627 UNP P01308 INS_HUMAN 25 51
DBREF 1HTV H 801 827 UNP P01308 INS_HUMAN 25 51
DBREF 1HTV J 1001 1027 UNP P01308 INS_HUMAN 25 51
DBREF 1HTV L 1201 1227 UNP P01308 INS_HUMAN 25 51
SEQRES 1 A 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 A 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 B 27 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 B 27 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 B 27 THR
SEQRES 1 C 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 C 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 D 27 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 D 27 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 D 27 THR
SEQRES 1 E 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 E 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 F 27 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 F 27 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 F 27 THR
SEQRES 1 G 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 G 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 H 27 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 H 27 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 H 27 THR
SEQRES 1 I 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 I 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 J 27 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 J 27 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 J 27 THR
SEQRES 1 K 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 K 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 L 27 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 L 27 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 L 27 THR
HET ZN B1300 1
HETNAM ZN ZINC ION
FORMUL 13 ZN ZN 2+
FORMUL 14 HOH *171(H2 O)
HELIX 1 1 GLY A 101 CYS A 107 1 7
HELIX 2 2 SER A 112 ASN A 118 1 7
HELIX 3 3 GLY B 208 GLY B 220 1 13
HELIX 4 4 GLU B 221 GLY B 223 5 3
HELIX 5 5 GLY C 301 CYS C 307 1 7
HELIX 6 6 SER C 312 ASN C 318 1 7
HELIX 7 7 CYS D 407 GLY D 420 1 14
HELIX 8 8 GLU D 421 GLY D 423 5 3
HELIX 9 9 GLY E 501 CYS E 507 1 7
HELIX 10 10 SER E 512 ASN E 518 1 7
HELIX 11 11 GLY F 608 GLY F 620 1 13
HELIX 12 12 GLU F 621 GLY F 623 5 3
HELIX 13 13 GLY G 701 CYS G 707 1 7
HELIX 14 14 SER G 712 GLU G 717 1 6
HELIX 15 15 CYS H 807 GLY H 820 1 14
HELIX 16 16 GLU H 821 GLY H 823 5 3
HELIX 17 17 GLY I 901 CYS I 907 1 7
HELIX 18 18 SER I 912 ASN I 918 1 7
HELIX 19 19 GLY J 1008 GLY J 1020 1 13
HELIX 20 20 GLU J 1021 GLY J 1023 5 3
HELIX 21 21 GLY K 1101 CYS K 1107 1 7
HELIX 22 22 SER K 1112 TYR K 1119 5 8
HELIX 23 23 GLY L 1208 GLY L 1220 1 13
HELIX 24 24 GLU L 1221 GLY L 1223 5 3
SHEET 1 A 2 PHE B 224 TYR B 226 0
SHEET 2 A 2 PHE D 424 TYR D 426 -1 O PHE D 424 N TYR B 226
SHEET 1 B 2 PHE F 624 TYR F 626 0
SHEET 2 B 2 PHE H 824 TYR H 826 -1 O PHE H 824 N TYR F 626
SHEET 1 C 2 PHE J1024 TYR J1026 0
SHEET 2 C 2 PHE L1224 TYR L1226 -1 O PHE L1224 N TYR J1026
SSBOND 1 CYS A 106 CYS A 111 1555 1555 2.03
SSBOND 2 CYS A 107 CYS B 207 1555 1555 2.03
SSBOND 3 CYS A 120 CYS B 219 1555 1555 2.03
SSBOND 4 CYS C 306 CYS C 311 1555 1555 2.03
SSBOND 5 CYS C 307 CYS D 407 1555 1555 2.03
SSBOND 6 CYS C 320 CYS D 419 1555 1555 2.03
SSBOND 7 CYS E 506 CYS E 511 1555 1555 2.03
SSBOND 8 CYS E 507 CYS F 607 1555 1555 2.03
SSBOND 9 CYS E 520 CYS F 619 1555 1555 2.02
SSBOND 10 CYS G 706 CYS G 711 1555 1555 2.03
SSBOND 11 CYS G 707 CYS H 807 1555 1555 2.03
SSBOND 12 CYS G 720 CYS H 819 1555 1555 2.02
SSBOND 13 CYS I 906 CYS I 911 1555 1555 2.03
SSBOND 14 CYS I 907 CYS J 1007 1555 1555 2.02
SSBOND 15 CYS I 920 CYS J 1019 1555 1555 2.02
SSBOND 16 CYS K 1106 CYS K 1111 1555 1555 2.03
SSBOND 17 CYS K 1107 CYS L 1207 1555 1555 2.04
SSBOND 18 CYS K 1120 CYS L 1219 1555 1555 2.03
LINK NE2 HIS B 210 ZN ZN B1300 1555 1555 2.19
LINK ZN ZN B1300 NE2 HIS F 610 1555 1555 2.14
LINK ZN ZN B1300 O HOH F1301 1555 1555 2.58
LINK ZN ZN B1300 NE2 HIS J1010 1555 1555 2.21
SITE 1 AC1 6 HIS B 210 HIS F 610 HOH F1301 HOH F1335
SITE 2 AC1 6 HOH F1341 HIS J1010
CRYST1 49.810 51.550 100.600 90.00 90.00 90.00 P 21 21 21 24
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 0.020076 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019399 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009940 0.00000
(ATOM LINES ARE NOT SHOWN.)
END