HEADER HORMONE/GROWTH FACTOR 19-APR-00 1EV3
TITLE STRUCTURE OF THE RHOMBOHEDRAL FORM OF THE M-CRESOL/INSULIN R6 HEXAMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: RESIDUES 87-107;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: INSULIN;
COMPND 8 CHAIN: B, D;
COMPND 9 FRAGMENT: RESIDUES 25-54;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HOMO SAPIENS
SOURCE 4 (HUMAN);
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HOMO SAPIENS
SOURCE 8 (HUMAN)
KEYWDS R6 HEXAMER, 18-A, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.D.SMITH,E.CISZAK,L.A.MAGRUM,W.A.PANGBORN,R.H.BLESSING
REVDAT 5 13-JUL-11 1EV3 1 VERSN
REVDAT 4 24-FEB-09 1EV3 1 VERSN
REVDAT 3 12-APR-05 1EV3 1 REMARK SCALE1 SCALE2 SCALE3
REVDAT 2 24-JAN-01 1EV3 1 REMARK
REVDAT 1 04-DEC-00 1EV3 0
JRNL AUTH G.D.SMITH,E.CISZAK,L.A.MAGRUM,W.A.PANGBORN,R.H.BLESSING
JRNL TITL R6 HEXAMERIC INSULIN COMPLEXED WITH M-CRESOL OR RESORCINOL.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 56 1541 2000
JRNL REFN ISSN 0907-4449
JRNL PMID 11092919
JRNL DOI 10.1107/S0907444900012749
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.D.SMITH,G.G.DODSON
REMARK 1 TITL STRUCTURE OF A RHOMBOHEDRAL R6 INSULIN/PHENOL COMPLEX
REMARK 1 REF PROTEINS V. 14 401 1992
REMARK 1 REFN ISSN 0887-3585
REMARK 1 REFERENCE 2
REMARK 1 AUTH U.DEREWENDA,Z.DEREWENDA,E.J.DODSON,G.G.DODSON,C.D.REYNOLDS,
REMARK 1 AUTH 2 G.D.SMITH,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 DOI 10.1038/338594A0
REMARK 2
REMARK 2 RESOLUTION. 1.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.72
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) (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 8552
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) : 0.200
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.300
REMARK 3 FREE R VALUE TEST SET COUNT : 885
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.78
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.89
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1173
REMARK 3 BIN R VALUE (WORKING SET) : 0.3360
REMARK 3 BIN FREE R VALUE : 0.3710
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 136
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.320
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 755
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 88
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.96000
REMARK 3 B22 (A**2) : -0.96000
REMARK 3 B33 (A**2) : 1.92000
REMARK 3 B12 (A**2) : 0.73000
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) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.19
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) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.37
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.90
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) : 1.780 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.720 ; 2.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.360 ; 2.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.410 ; 3.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 56.69
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 1EV3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-00.
REMARK 100 THE RCSB ID CODE IS RCSB010918.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JAN-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC CONFOCAL MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9334
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 19.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 60.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.17300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: CNS 1.0
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30 MG INSULIN, 3.0 ML OF 0.02 M HCL,
REMARK 280 0.3 ML OF 0.15 M ZINC ACETATE, 1.5 ML OF 0.2 M SODIUM CITRATE,
REMARK 280 1.2 ML OF 2.5% M-CRESOL IN ACETONE, 0.36 GM SODIUM CHLORIDE, PH
REMARK 280 8.5, SLOW COOLING, 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 39.43300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.76665
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 13.15500
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 39.43300
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 22.76665
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 13.15500
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 39.43300
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 22.76665
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 13.15500
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 45.53331
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 26.31000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 45.53331
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 26.31000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 45.53331
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 26.31000
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 20660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -308.0 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 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
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 ZN ZN D 31 LIES ON A SPECIAL POSITION.
REMARK 375 CL CL B 32 LIES ON A SPECIAL POSITION.
REMARK 375 CL CL D 32 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 33 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 33 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 55 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LYS B 29
REMARK 465 THR B 30
REMARK 465 LYS D 29
REMARK 465 THR D 30
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 4 CG CD OE1 OE2
REMARK 470 TYR A 14 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 21 CG CD OE1 OE2
REMARK 470 PHE D 1 CG CD1 CD2 CE1 CE2 CZ
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 35 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH A 38 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH B 53 DISTANCE = 5.03 ANGSTROMS
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 B 31 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 10 NE2
REMARK 620 2 CL B 32 CL 106.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 31 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 10 NE2
REMARK 620 2 CL D 32 CL 107.6
REMARK 620 N 1
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 ZN D 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 32
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 32
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CRS A 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CRS C 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CRS C 23
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EV6 RELATED DB: PDB
DBREF 1EV3 A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1EV3 B 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1EV3 C 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1EV3 D 1 30 UNP P01308 INS_HUMAN 25 54
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 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 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 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 THR
HET ZN B 31 1
HET ZN D 31 1
HET CL B 32 1
HET CL D 32 1
HET CRS A 22 8
HET CRS C 22 8
HET CRS C 23 8
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM CRS M-CRESOL
FORMUL 5 ZN 2(ZN 2+)
FORMUL 7 CL 2(CL 1-)
FORMUL 9 CRS 3(C7 H8 O)
FORMUL 12 HOH *88(H2 O)
HELIX 1 1 GLY A 1 CYS A 7 1 7
HELIX 2 2 SER A 12 GLU A 17 1 6
HELIX 3 3 PHE B 1 GLY B 20 1 20
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 GLU C 17 1 6
HELIX 7 7 PHE D 1 GLY D 20 1 20
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 2.02
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 2.02
SSBOND 6 CYS C 20 CYS D 19 1555 1555 2.04
LINK ZN ZN B 31 NE2 HIS B 10 1555 1555 1.97
LINK ZN ZN B 31 CL CL B 32 1555 1555 2.25
LINK ZN ZN D 31 NE2 HIS D 10 1555 1555 2.00
LINK ZN ZN D 31 CL CL D 32 1555 1555 2.39
LINK ZN ZN B 31 NE2 HIS B 10 1555 2555 1.97
LINK ZN ZN B 31 NE2 HIS B 10 1555 3555 1.97
LINK ZN ZN B 31 CL CL B 32 1555 2555 2.25
LINK ZN ZN B 31 CL CL B 32 1555 3555 2.25
LINK ZN ZN D 31 NE2 HIS D 10 1555 3555 2.00
LINK ZN ZN D 31 CL CL D 32 1555 2555 2.39
LINK ZN ZN D 31 CL CL D 32 1555 3555 2.39
LINK ZN ZN D 31 NE2 HIS D 10 1555 2555 2.00
SITE 1 AC1 2 HIS B 10 CL B 32
SITE 1 AC2 2 HIS D 10 CL D 32
SITE 1 AC3 2 HIS B 10 ZN B 31
SITE 1 AC4 2 HIS D 10 ZN D 31
SITE 1 AC5 6 CYS A 6 ILE A 10 CYS A 11 LEU A 16
SITE 2 AC5 6 HIS B 5 LEU B 11
SITE 1 AC6 8 LEU B 17 CYS C 6 SER C 9 ILE C 10
SITE 2 AC6 8 CYS C 11 HIS D 5 LEU D 11 ALA D 14
SITE 1 AC7 3 VAL B 18 LEU C 13 VAL D 18
CRYST1 78.866 78.866 39.465 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 0.012680 0.007321 0.000000 0.00000
SCALE2 0.000000 0.014641 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025339 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
