HEADER HORMONE 11-MAR-09 3GKY
TITLE THE STRUCTURAL BASIS OF AN ER STRESS-ASSOCIATED BOTTLENECK IN A
TITLE 2 PROTEIN FOLDING LANDSCAPE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN A CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: INSULIN B CHAIN;
COMPND 7 CHAIN: B, D;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 4 ORGANISM_COMMON: PIG;
SOURCE 5 ORGANISM_TAXID: 9823;
SOURCE 6 OTHER_DETAILS: BIOSYNTHETIC SEQUENCE;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 10 ORGANISM_COMMON: PIG;
SOURCE 11 ORGANISM_TAXID: 9823;
SOURCE 12 OTHER_DETAILS: BIOSYNTHETIC SEQUENCE
KEYWDS PROTEIN FOLDING, ER STRESS-ASSOCIATED, TR TRANSITION RECEPTOR
KEYWDS 2 BINDING, CARBOHYDRATE METABOLISM, CLEAVAGE ON PAIR OF BASIC
KEYWDS 3 RESIDUES, DIABETES MELLITUS, DISEASE MUTATION, DISULFIDE BOND,
KEYWDS 4 GLUCOSE METABOLISM, HORMONE, PHARMACEUTICAL, SECRETED
EXPDTA X-RAY DIFFRACTION
AUTHOR M.LIU,Z.L.WAN,Y.C.CHU,H.ALDDIN,B.KLAPROTH,M.A.WEISS
REVDAT 4 06-SEP-23 3GKY 1 REMARK SEQADV
REVDAT 3 24-JAN-18 3GKY 1 AUTHOR
REVDAT 2 22-DEC-09 3GKY 1 JRNL
REVDAT 1 24-MAR-09 3GKY 0
JRNL AUTH M.LIU,Z.L.WAN,Y.C.CHU,H.ALADDIN,B.KLAPROTH,M.CHOQUETTE,
JRNL AUTH 2 Q.X.HUA,R.B.MACKIN,J.S.RAO,P.DE MEYTS,P.G.KATSOYANNIS,
JRNL AUTH 3 P.ARVAN,M.A.WEISS
JRNL TITL CRYSTAL STRUCTURE OF A "NONFOLDABLE" INSULIN: IMPAIRED
JRNL TITL 2 FOLDING EFFICIENCY DESPITE NATIVE ACTIVITY.
JRNL REF J.BIOL.CHEM. V. 284 35259 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19850922
JRNL DOI 10.1074/JBC.M109.046888
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.N.BAKER,T.L.BLUJDELL,J.F.CUTFIELD,S.M.CUTFIELD,E.J.DODSON,
REMARK 1 AUTH 2 G.G.DODSON,D.HODGKIN,N.W.ISAACS,C.D.REYNOLDS
REMARK 1 TITL THE STRUCTURE OF 2ZN PIG INSULIN CRYSTAL AT 1.5 A RESOLUTION
REMARK 1 REF PHILOS.TRANS.R.SOC.LONDON, V. 319 369 1988
REMARK 1 REF 2 SER.B
REMARK 1 REFN ISSN 0080-4622
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.BENTLEY,E.DODSON,G.DODSON,D.HODGKIN,D.MERCOLA
REMARK 1 TITL STRUCTURE OF INSULIN IN 4-ZINC INSULIN
REMARK 1 REF NATURE V. 261 166 1976
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 3
REMARK 1 AUTH U.DEREWENDA,Z.DEREWENDA,E.DODSON,G.DODSON,C.REYNOLD,G.SMITH,
REMARK 1 AUTH 2 C.SPARKS,D.SWENSON
REMARK 1 TITL PHENOL STABILIZES MORE HELIX IN A NEW SYMMETRICAL ZINC
REMARK 1 TITL 2 INSULIN HEXAMER
REMARK 1 REF NATURE V. 338 594 1989
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 4
REMARK 1 AUTH Q.X.HUA,S.NAKAGAWA,S.Q.HU,W.JIA,S.WANG,M.A.WEISS
REMARK 1 TITL TOWARD THE ACTIVE CONFORMATION OF INSULIN: STEREOSPECIFIC
REMARK 1 TITL 2 MODULATION OF A STRUCTURAL SWITH IN THE B CHAIN
REMARK 1 REF J.BIOL.CHEM. V. 281 24900 2006
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 1.80 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.58
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) (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 7299
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) : 0.209
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 789
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2970
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 133
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 810
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 125
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.62000
REMARK 3 B22 (A**2) : -1.62000
REMARK 3 B33 (A**2) : 3.24000
REMARK 3 B12 (A**2) : 1.10000
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) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.12
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) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.600
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) : 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 3GKY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-09.
REMARK 100 THE DEPOSITION ID IS D_1000051990.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-FEB-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.948
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7299
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 22.580
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 390252.
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
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) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.18200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.400
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: 1TRZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.02 M TRIS, 0.05 M SODIUM CITRATE, 5%
REMARK 280 ACETONE, 0.03% PHENOL, 0.01% ZINC ACETATE, PH 8.1, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.11250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.58161
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 12.23733
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 39.11250
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 22.58161
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 12.23733
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 39.11250
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 22.58161
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 12.23733
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 45.16322
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 24.47467
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 45.16322
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 24.47467
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 45.16322
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 24.47467
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: 19390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -314.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 39.11250
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 67.74484
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -39.11250
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 67.74484
REMARK 350 BIOMT3 3 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 ZN ZN B 31 LIES ON A SPECIAL POSITION.
REMARK 375 CL CL B 32 LIES ON A SPECIAL POSITION.
REMARK 375 ZN ZN D 31 LIES ON A SPECIAL POSITION.
REMARK 375 CL CL D 32 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 36 LIES ON A SPECIAL POSITION.
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 ASN B 3 56.77 -117.28
REMARK 500 LYS B 29 35.26 -78.70
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 ZN B 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 32
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH C 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 32
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TRZ RELATED DB: PDB
REMARK 900 TR STATE INSULIN CRYSTAL STRUCTURE
DBREF 3GKY A 1 21 UNP P01315 INS_PIG 88 108
DBREF 3GKY B 1 30 UNP P01315 INS_PIG 25 54
DBREF 3GKY C 1 21 UNP P01315 INS_PIG 88 108
DBREF 3GKY D 1 30 UNP P01315 INS_PIG 25 54
SEQADV 3GKY HIS A 8 UNP P01315 THR 95 CONFLICT
SEQADV 3GKY VAL A 16 UNP P01315 LEU 103 CONFLICT
SEQADV 3GKY HIS C 8 UNP P01315 THR 95 CONFLICT
SEQADV 3GKY VAL C 16 UNP P01315 LEU 103 CONFLICT
SEQRES 1 A 21 GLY ILE VAL GLU GLN CYS CYS HIS SER ILE CYS SER LEU
SEQRES 2 A 21 TYR GLN VAL GLU ASN TYR CYS ASN
SEQRES 1 B 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 B 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 B 30 THR PRO LYS ALA
SEQRES 1 C 21 GLY ILE VAL GLU GLN CYS CYS HIS SER ILE CYS SER LEU
SEQRES 2 C 21 TYR GLN VAL GLU ASN TYR CYS ASN
SEQRES 1 D 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 D 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR
SEQRES 3 D 30 THR PRO LYS ALA
HET ZN B 31 1
HET CL B 32 1
HET IPH C 100 7
HET ZN D 31 1
HET CL D 32 1
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM IPH PHENOL
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 CL 2(CL 1-)
FORMUL 7 IPH C6 H6 O
FORMUL 10 HOH *125(H2 O)
HELIX 1 1 GLY A 1 CYS A 7 1 7
HELIX 2 2 SER A 12 ASN A 18 1 7
HELIX 3 3 GLY B 8 GLY B 20 1 13
HELIX 4 4 GLU B 21 GLY B 23 5 3
HELIX 5 5 GLY C 1 CYS C 7 1 7
HELIX 6 6 SER C 12 ASN C 18 1 7
HELIX 7 7 ASN D 3 GLY D 20 1 18
HELIX 8 8 GLU D 21 GLY D 23 5 3
SHEET 1 A 2 PHE B 24 TYR B 26 0
SHEET 2 A 2 PHE D 24 TYR D 26 -1 O PHE D 24 N TYR B 26
SSBOND 1 CYS A 6 CYS A 11 1555 1555 2.04
SSBOND 2 CYS A 7 CYS B 7 1555 1555 2.03
SSBOND 3 CYS A 20 CYS B 19 1555 1555 2.03
SSBOND 4 CYS C 6 CYS C 11 1555 1555 2.02
SSBOND 5 CYS C 7 CYS D 7 1555 1555 2.04
SSBOND 6 CYS C 20 CYS D 19 1555 1555 2.03
LINK NE2 HIS B 10 ZN ZN B 31 1555 1555 2.08
LINK NE2 HIS D 10 ZN ZN D 31 1555 1555 2.07
SITE 1 AC1 2 HIS B 10 CL B 32
SITE 1 AC2 2 ZN B 31 HOH B 89
SITE 1 AC3 8 CYS C 6 SER C 9 ILE C 10 CYS C 11
SITE 2 AC3 8 HOH C 51 HIS D 5 HIS D 10 LEU D 11
SITE 1 AC4 2 HIS D 10 CL D 32
SITE 1 AC5 2 HIS D 10 ZN D 31
CRYST1 78.225 78.225 36.712 90.00 90.00 120.00 H 3 18
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 0.012784 0.007381 0.000000 0.00000
SCALE2 0.000000 0.014761 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027239 0.00000
(ATOM LINES ARE NOT SHOWN.)
END