HEADER HORMONE 06-MAY-12 4F1B
TITLE HUMAN INSULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN A CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 90-110;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: INSULIN B CHAIN;
COMPND 7 CHAIN: B, D;
COMPND 8 FRAGMENT: UNP RESIDUES 25-54
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606
KEYWDS PANCREATIC HORMONE, HORMONE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.P.FAVERO-RETTO,L.C.PALMIERI,L.M.T.R.LIMA
REVDAT 4 15-NOV-17 4F1B 1 REMARK
REVDAT 3 18-DEC-13 4F1B 1 JRNL
REVDAT 2 12-JUN-13 4F1B 1 JRNL
REVDAT 1 08-MAY-13 4F1B 0
JRNL AUTH M.P.FAVERO-RETTO,L.C.PALMIERI,T.A.SOUZA,F.C.ALMEIDA,L.M.LIMA
JRNL TITL STRUCTURAL META-ANALYSIS OF REGULAR HUMAN INSULIN IN
JRNL TITL 2 PHARMACEUTICAL FORMULATIONS.
JRNL REF EUR J PHARM BIOPHARM V. 85 1112 2013
JRNL REFN ISSN 0939-6411
JRNL PMID 23692694
JRNL DOI 10.1016/J.EJPB.2013.05.005
REMARK 2
REMARK 2 RESOLUTION. 1.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 3 NUMBER OF REFLECTIONS : 10239
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 + TEST SET) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 496
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.59
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.63
REMARK 3 REFLECTION IN BIN (WORKING SET) : 802
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.76
REMARK 3 BIN R VALUE (WORKING SET) : 0.3260
REMARK 3 BIN FREE R VALUE SET COUNT : 42
REMARK 3 BIN FREE R VALUE : 0.4600
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 808
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 107
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : 0.05000
REMARK 3 B33 (A**2) : -0.07000
REMARK 3 B12 (A**2) : 0.02000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.239
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.120
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.074
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.701
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 878 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 563 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1197 ; 1.862 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): 1375 ; 1.250 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 107 ; 7.206 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 42 ;32.332 ;24.048
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 138 ;12.594 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 3 ;13.831 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 131 ; 0.174 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 991 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 193 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 531 ; 1.900 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 216 ; 0.656 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 860 ; 2.868 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 347 ; 4.517 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 337 ; 6.237 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 1441 ; 1.997 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4F1B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-12.
REMARK 100 THE DEPOSITION ID IS D_1000072329.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LNLS
REMARK 200 BEAMLINE : W01B-MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.45860
REMARK 200 MONOCHROMATOR : DOUBLE FLAT CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10239
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.591
REMARK 200 RESOLUTION RANGE LOW (A) : 40.995
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.35400
REMARK 200 R SYM FOR SHELL (I) : 0.35400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 UL 0.1 M SODIUM PHOSPHATE, PH 5.5,
REMARK 280 10% W/V PEG6000 + 2 UL 100 U/ML HUMAN INSULIN (NOVOLIN R, LOT #
REMARK 280 TS 62987), CRYOPROTECTANT: MOTHER LIQUOR + 10% GLYCEROL, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 40.99500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.66847
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 11.25000
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 40.99500
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 23.66847
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 11.25000
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 40.99500
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 23.66847
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 11.25000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 47.33695
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 22.50000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 47.33695
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 22.50000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 47.33695
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 22.50000
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: 21000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -387.0 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 101 LIES ON A SPECIAL POSITION.
REMARK 375 ZN ZN D 101 LIES ON A SPECIAL POSITION.
REMARK 375 CL CL D 102 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 230 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 231 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 SER A 9 -149.81 -87.85
REMARK 500 SER C 9 -120.01 -128.83
REMARK 500 SER C 9 -127.67 -123.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS B 29 THR B 30 146.06
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 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 102
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3I3Z RELATED DB: PDB
REMARK 900 RELATED ID: 4EWW RELATED DB: PDB
REMARK 900 RELATED ID: 4EWX RELATED DB: PDB
REMARK 900 RELATED ID: 4EWZ RELATED DB: PDB
REMARK 900 RELATED ID: 4EX0 RELATED DB: PDB
REMARK 900 RELATED ID: 4EX1 RELATED DB: PDB
REMARK 900 RELATED ID: 4EXX RELATED DB: PDB
REMARK 900 RELATED ID: 4EY1 RELATED DB: PDB
REMARK 900 RELATED ID: 4EY9 RELATED DB: PDB
REMARK 900 RELATED ID: 4EYD RELATED DB: PDB
REMARK 900 RELATED ID: 4EYN RELATED DB: PDB
REMARK 900 RELATED ID: 4EYP RELATED DB: PDB
REMARK 900 RELATED ID: 4F0N RELATED DB: PDB
REMARK 900 RELATED ID: 4F0O RELATED DB: PDB
REMARK 900 RELATED ID: 4F1A RELATED DB: PDB
REMARK 900 RELATED ID: 4F1C RELATED DB: PDB
REMARK 900 RELATED ID: 4F1D RELATED DB: PDB
REMARK 900 RELATED ID: 4F1F RELATED DB: PDB
REMARK 900 RELATED ID: 4F1G RELATED DB: PDB
DBREF 4F1B A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 4F1B B 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 4F1B C 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 4F1B 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 101 1
HET CL B 102 1
HET ZN D 101 1
HET CL D 102 1
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 CL 2(CL 1-)
FORMUL 9 HOH *107(H2 O)
HELIX 1 1 GLY A 1 CYS A 7 1 7
HELIX 2 2 LEU A 13 GLU A 17 1 5
HELIX 3 3 ASN A 18 CYS A 20 5 3
HELIX 4 4 GLY B 8 GLY B 20 1 13
HELIX 5 5 GLU B 21 GLY B 23 5 3
HELIX 6 6 ILE C 2 SER C 9 1 8
HELIX 7 7 SER C 12 GLU C 17 1 6
HELIX 8 8 ASN C 18 CYS C 20 5 3
HELIX 9 9 GLY D 8 GLY D 20 1 13
HELIX 10 10 GLU D 21 GLY D 23 5 3
SHEET 1 A 2 CYS A 11 SER A 12 0
SHEET 2 A 2 ASN B 3 GLN B 4 -1 O GLN B 4 N CYS A 11
SHEET 1 B 2 PHE B 24 TYR B 26 0
SHEET 2 B 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 2.08
SSBOND 2 CYS A 7 CYS B 7 1555 1555 2.01
SSBOND 3 CYS A 20 CYS B 19 1555 1555 1.99
SSBOND 4 CYS C 6 CYS C 11 1555 1555 2.04
SSBOND 5 CYS C 7 CYS D 7 1555 1555 2.06
SSBOND 6 CYS C 20 CYS D 19 1555 1555 2.05
LINK NE2 HIS B 10 ZN ZN B 101 1555 1555 2.00
LINK NE2 HIS D 10 ZN ZN D 101 1555 1555 2.04
SITE 1 AC1 2 HIS B 10 CL B 102
SITE 1 AC2 1 ZN B 101
SITE 1 AC3 2 HIS D 10 CL D 102
SITE 1 AC4 3 HIS D 10 ZN D 101 HOH D 233
CRYST1 81.990 81.990 33.750 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 0.012197 0.007042 0.000000 0.00000
SCALE2 0.000000 0.014083 0.000000 0.00000
SCALE3 0.000000 0.000000 0.029629 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
