HEADER HORMONE/GROWTH FACTOR 24-SEP-04 1W8P
TITLE STRUCTURAL PROPERTIES OF THE B25TYR-NME-B26PHE INSULIN MUTANT.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN A-CHAIN;
COMPND 3 CHAIN: A, C, E, G, I, K;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: INSULIN B-CHAIN;
COMPND 7 CHAIN: B, D, F, H, J, L;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 OTHER_DETAILS: METHYLATED MAIN CHAIN NITROGEN BETWEEN B25 AND B26.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS INSULIN, IGF-1, MUTANTS, HORMONE/GROWTH FACTOR, HORMONE-GROWTH FACTOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.ZAKOWA,O.AU-ALVAREZ,E.J.DODSON,G.G.DODSON,A.M.BRZOZOWSKI
REVDAT 4 13-DEC-23 1W8P 1 LINK
REVDAT 3 28-JUN-17 1W8P 1 REMARK
REVDAT 2 24-FEB-09 1W8P 1 VERSN
REVDAT 1 03-FEB-05 1W8P 0
JRNL AUTH L.ZARKOWA,J.BRYNDA,O.AU-ALVAREZ,E.J.DODSON,G.G.DODSON,
JRNL AUTH 2 J.L.WHITTINGHAM,A.M.BRZOZOWSKI
JRNL TITL TOWARDS THE INSULIN-IGF-I INTERMEDIATE STRUCTURES:
JRNL TITL 2 FUNCTIONAL AND STRUCTURAL PROPERTIES OF THE
JRNL TITL 3 B25TYR-NME-B26PHE INSULIN MUTANT.
JRNL REF BIOCHEMISTRY V. 43 16293 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15610023
JRNL DOI 10.1021/BI048856U
REMARK 2
REMARK 2 RESOLUTION. 2.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 17491
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 956
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) : 2.08
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1253
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE SET COUNT : 69
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2342
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 83
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.03000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.234
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.209
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.144
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.435
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2483 ; 0.018 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3356 ; 1.708 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 285 ; 6.783 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 357 ; 0.125 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1882 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1050 ; 0.248 ; 0.200
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): 98 ; 0.226 ; 0.200
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): 39 ; 0.248 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.099 ; 0.200
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): 1461 ; 1.157 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2331 ; 2.278 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 999 ; 3.043 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 983 ; 5.169 ; 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): NULL ; NULL ; NULL
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 : BABINET MODEL WITH 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 1W8P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1290021059.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 8.00
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 : ENRAF-NONIUS FR591
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17496
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080
REMARK 200 RESOLUTION RANGE LOW (A) : 25.560
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.03000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.12000
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: PDB ENTRY 1EVR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRI-SODIUM CITRATE, 0.02 % W/V
REMARK 280 ZINC ACETATE, 6 % W/V TRIS/HCL PH 8.2, 0.1 % W/V PHENOL., PH 8.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 31.05800
REMARK 290 SMTRY3 2 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: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE PHE 49 TYR CHAIN B, D, F, H, J, L
REMARK 400 ENGINEERED RESIDUE TYR 50 PHE CHAIN B, D, F, H, J, L
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 THR B 30
REMARK 465 LYS D 29
REMARK 465 THR D 30
REMARK 465 THR F 30
REMARK 465 LYS H 29
REMARK 465 THR H 30
REMARK 465 THR J 30
REMARK 465 LYS L 29
REMARK 465 THR L 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 LYS B 29 CG CD CE NZ
REMARK 470 PRO H 28 C O
REMARK 470 TYR L 25 CG CD1 CD2 CE1 CE2 CZ OH
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 NE2 GLN K 5 OH TYR K 19 2.11
REMARK 500 OE2 GLU F 13 O HOH F 2005 2.12
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 ILE A 2 -43.19 129.02
REMARK 500 ILE G 2 -49.28 72.78
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 GLY G 1 ILE G 2 147.43
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 B1030 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 10 NE2
REMARK 620 2 HOH B2009 O 111.2
REMARK 620 3 HIS F 10 NE2 102.8 113.8
REMARK 620 4 HIS J 10 NE2 112.7 111.0 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1030 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 10 NE2
REMARK 620 2 HOH D2012 O 125.8
REMARK 620 3 HIS H 10 NE2 115.8 102.2
REMARK 620 4 HIS L 10 NE2 90.8 113.2 108.0
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 B1030
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D1030
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH A1022
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH C1022
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH E1022
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH G1022
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH I1022
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH K1022
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A7F RELATED DB: PDB
REMARK 900 INSULIN MUTANT B16 GLU, B24 GLY, DES-B30 , NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1AI0 RELATED DB: PDB
REMARK 900 R6 HUMAN INSULIN HEXAMER (NON-SYMMETRIC), NMR, 10 STRUCTURES
REMARK 900 RELATED ID: 1AIY RELATED DB: PDB
REMARK 900 R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, 10 STRUCTURES
REMARK 900 RELATED ID: 1B9E RELATED DB: PDB
REMARK 900 HUMAN INSULIN MUTANT SERB9GLU
REMARK 900 RELATED ID: 1BEN RELATED DB: PDB
REMARK 900 INSULIN COMPLEXED WITH 4-HYDROXYBENZAMIDE
REMARK 900 RELATED ID: 1EFE RELATED DB: PDB
REMARK 900 AN ACTIVE MINI-PROINSULIN, M2PI
REMARK 900 RELATED ID: 1EV3 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE RHOMBOHEDRAL FORM OF THE M-CRESOL/INSULIN R6
REMARK 900 HEXAMER
REMARK 900 RELATED ID: 1EV6 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE MONOCLINIC FORM OF THE M -CRESOL/INSULIN R6 HEXAMER
REMARK 900 RELATED ID: 1EVR RELATED DB: PDB
REMARK 900 THE STRUCTURE OF THE RESORCINOL/INSULIN R6 HEXAMER
REMARK 900 RELATED ID: 1FU2 RELATED DB: PDB
REMARK 900 FIRST PROTEIN STRUCTURE DETERMINED FROM X- RAY POWDERDIFFRACTION
REMARK 900 DATA
REMARK 900 RELATED ID: 1FUB RELATED DB: PDB
REMARK 900 FIRST PROTEIN STRUCTURE DETERMINED FROM X- RAY POWDERDIFFRACTION
REMARK 900 DATA
REMARK 900 RELATED ID: 1G7A RELATED DB: PDB
REMARK 900 1.2 A STRUCTURE OF T3R3 HUMAN INSULIN AT 100 K
REMARK 900 RELATED ID: 1G7B RELATED DB: PDB
REMARK 900 1.3 A STRUCTURE OF T3R3 HUMAN INSULIN AT 100 K
REMARK 900 RELATED ID: 1GUJ RELATED DB: PDB
REMARK 900 INSULIN AT PH 2: STRUCTURAL ANALYSIS OF THE CONDITIONS PROMOTING
REMARK 900 INSULIN FIBRE FORMATION.
REMARK 900 RELATED ID: 1HIQ RELATED DB: PDB
REMARK 900 INSULIN (HUMAN) MUTANT WITH PHE B 24 REPLACED BY SER (F24S) (NMR,
REMARK 900 REPRESENTATIVE PLUS 9 STRUCTURES)
REMARK 900 RELATED ID: 1HIS RELATED DB: PDB
REMARK 900 INSULIN (HUMAN, DES-PENTAPEPTIDE (B 26 - B 30)) (NMR,
REMARK 900 REPRESENTATIVE PLUS 14 STRUCTURES)
REMARK 900 RELATED ID: 1HIT RELATED DB: PDB
REMARK 900 INSULIN (HUMAN) MUTANT WITH PHE B 24 REPLACED BY GLY (F24G) (NMR,
REMARK 900 REPRESENTATIVE PLUS 8 STRUCTURES)
REMARK 900 RELATED ID: 1HLS RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE HUMAN INSULIN-HIS(B16 )
REMARK 900 RELATED ID: 1HTV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN
REMARK 900 RELATED ID: 1HUI RELATED DB: PDB
REMARK 900 INSULIN MUTANT (B1, B10, B16, B27)GLU, DES -B30, NMR, 25 STRUCTURES
REMARK 900 RELATED ID: 1IOG RELATED DB: PDB
REMARK 900 INSULIN MUTANT A3 GLY,(B1, B10, B16, B27) GLU, DES-B30, NMR, 19
REMARK 900 STRUCTURES
REMARK 900 RELATED ID: 1IOH RELATED DB: PDB
REMARK 900 INSULIN MUTANT A8 HIS,(B1, B10, B16, B27) GLU, DES-B30, NMR, 26
REMARK 900 STRUCTURES
REMARK 900 RELATED ID: 1J73 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN UNSTABLE INSULIN ANALOG WITH NATIVEACTIVITY.
REMARK 900 RELATED ID: 1JCA RELATED DB: PDB
REMARK 900 NON-STANDARD DESIGN OF UNSTABLE INSULIN ANALOGUES WITHENHANCED
REMARK 900 ACTIVITY
REMARK 900 RELATED ID: 1JCO RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE MONOMERIC [THR(B27 )->PRO,PRO(B28)->THR]
REMARK 900 INSULIN MUTANT (PT INSULIN)
REMARK 900 RELATED ID: 1K3M RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN INSULIN MUTANT ILE- A2-ALA, HIS-B10-ASP, PRO-
REMARK 900 B28-LYS, LYS- B29-PRO, 15 STRUCTURES
REMARK 900 RELATED ID: 1KMF RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN INSULIN MUTANT ILE- A2-ALLO-ILE, HIS-B10-ASP,
REMARK 900 PRO-B28-LYS, LYS-B29-PRO, 15 STRUCTURES
REMARK 900 RELATED ID: 1LKQ RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN INSULIN MUTANT ILE- A2-GLY, VAL-A3-GLY, HIS-
REMARK 900 B10-ASP, PRO- B28-LYS, LYS-B29-PRO, 20 STRUCTURES
REMARK 900 RELATED ID: 1LNP RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN INSULIN MUTANT HIS- B10-ASP, PRO-B28-LYS,
REMARK 900 LYS-B29-PRO, 20 STRUCTURES
REMARK 900 RELATED ID: 1LPH RELATED DB: PDB
REMARK 900 LYS(B28)PRO(B29)-HUMAN INSULIN
REMARK 900 RELATED ID: 1MHI RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: INSULIN; CHAIN: A, B; ENGINEERED: YES MUTATION:
REMARK 900 S(B 9)D;
REMARK 900 RELATED ID: 1MHJ RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: INSULIN; CHAIN: A, B; ENGINEERED: YES MUTATION:
REMARK 900 DES-[PHE(B 25)];
REMARK 900 RELATED ID: 1MSO RELATED DB: PDB
REMARK 900 T6 HUMAN INSULIN AT 1.0 A RESOLUTION
REMARK 900 RELATED ID: 1OS3 RELATED DB: PDB
REMARK 900 DEHYDRATED T6 HUMAN INSULIN AT 100 K
REMARK 900 RELATED ID: 1OS4 RELATED DB: PDB
REMARK 900 DEHYDRATED T6 HUMAN INSULIN AT 295 K
REMARK 900 RELATED ID: 1Q4V RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ALLO-ILEA2-INSULIN, AN INACTIVE CHIRALANALOGUE:
REMARK 900 IMPLICATIONS FOR THE MECHANISM OF RECEPTOR
REMARK 900 RELATED ID: 1QIY RELATED DB: PDB
REMARK 900 HUMAN INSULIN HEXAMERS WITH CHAIN B HIS MUTATED TO TYR COMPLEXED
REMARK 900 WITH PHENOL
REMARK 900 RELATED ID: 1QIZ RELATED DB: PDB
REMARK 900 HUMAN INSULIN HEXAMERS WITH CHAIN B HIS MUTATED TO TYR COMPLEXED
REMARK 900 WITH RESORCINOL
REMARK 900 RELATED ID: 1QJ0 RELATED DB: PDB
REMARK 900 HUMAN INSULIN HEXAMERS WITH CHAIN B HIS MUTATED TO TYR
REMARK 900 RELATED ID: 1SF1 RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN INSULIN UNDER AMYLOIDOGENICCONDITION, 15
REMARK 900 STRUCTURES
REMARK 900 RELATED ID: 1SJT RELATED DB: PDB
REMARK 900 MINI-PROINSULIN, TWO CHAIN INSULIN ANALOG MUTANT: DES B30, HIS(B 10)
REMARK 900 ASP, PRO(B 28)ASP, NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1SJU RELATED DB: PDB
REMARK 900 MINI-PROINSULIN, SINGLE CHAIN INSULIN ANALOG MUTANT: DES B30, HIS(B
REMARK 900 10)ASP, PRO(B 28)ASP AND PEPTIDE BOND BETWEEN LYS B 29 AND GLY A 1,
REMARK 900 NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1T1K RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN INSULIN MUTANT HIS- B10-ASP, VAL-B12-ALA,
REMARK 900 PRO-B28-LYS, LYS- B29-PRO, 15 STRUCTURES
REMARK 900 RELATED ID: 1T1P RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN INSULIN MUTANT HIS- B10-ASP, VAL-B12-THR,
REMARK 900 PRO-B28-LYS, LYS- B29-PRO, 15 STRUCTURES
REMARK 900 RELATED ID: 1T1Q RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN INSULIN MUTANT HIS- B10-ASP, VAL-B12-ABA,
REMARK 900 PRO-B28-LYS, LYS- B29-PRO, 15 STRUCTURES
REMARK 900 RELATED ID: 1TRZ RELATED DB: PDB
REMARK 900 INSULIN (T3R3) COMPLEX WITH TWO ZINC IONS
REMARK 900 RELATED ID: 1TYL RELATED DB: PDB
REMARK 900 INSULIN (T3R3) (PH 6.4, 0.75 M NACL) COMPLEXED WITH TWO ZINC IONS
REMARK 900 AND TYLENOL ( 4'-HYDROXYACETANILIDE)
REMARK 900 RELATED ID: 1TYM RELATED DB: PDB
REMARK 900 INSULIN (T3R3) (PH 5.6, 1.0 M NACL) COMPLEXED WITH TWO ZINC IONS
REMARK 900 AND TYLENOL ( 4'-HYDROXYACETANILIDE)
REMARK 900 RELATED ID: 1UZ9 RELATED DB: PDB
REMARK 900 CRYSTALLOGRAPHIC AND SOLUTION STUDIES OF N- LITHOCHOLYL INSULIN: A
REMARK 900 NEW GENERATION OF PROLONGED-ACTING INSULINS.
REMARK 900 RELATED ID: 1VKT RELATED DB: PDB
REMARK 900 HUMAN INSULIN TWO DISULFIDE MODEL, NMR, 10 STRUCTURES
REMARK 900 RELATED ID: 1XDA RELATED DB: PDB
REMARK 900 STRUCTURE OF INSULIN
REMARK 900 RELATED ID: 1XGL RELATED DB: PDB
REMARK 900 HUMAN INSULIN DISULFIDE ISOMER, NMR, 10 STRUCTURES
REMARK 900 RELATED ID: 1ZEG RELATED DB: PDB
REMARK 900 STRUCTURE OF B28 ASP INSULIN IN COMPLEX WITH PHENOL
REMARK 900 RELATED ID: 1ZEH RELATED DB: PDB
REMARK 900 STRUCTURE OF INSULIN
REMARK 900 RELATED ID: 1ZNJ RELATED DB: PDB
REMARK 900 INSULIN, MONOCLINIC CRYSTAL FORM
REMARK 900 RELATED ID: 2AIY RELATED DB: PDB
REMARK 900 R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 2HIU RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HUMAN INSULIN IN 20% ACETIC ACID, ZINC-FREE, 10
REMARK 900 STRUCTURES
REMARK 900 RELATED ID: 3AIY RELATED DB: PDB
REMARK 900 R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, REFINED AVERAGE STRUCTURE
REMARK 900 RELATED ID: 4AIY RELATED DB: PDB
REMARK 900 R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, ' GREEN' SUBSTATE,
REMARK 900 AVERAGE STRUCTURE
REMARK 900 RELATED ID: 5AIY RELATED DB: PDB
REMARK 900 R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, ' RED' SUBSTATE, AVERAGE
REMARK 900 STRUCTURE
DBREF 1W8P A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1W8P B 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1W8P C 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1W8P D 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1W8P E 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1W8P F 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1W8P G 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1W8P H 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1W8P I 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1W8P J 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1W8P K 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1W8P L 1 30 UNP P01308 INS_HUMAN 25 54
SEQADV 1W8P TYR B 25 UNP P01308 PHE 49 ENGINEERED MUTATION
SEQADV 1W8P PHE B 26 UNP P01308 TYR 50 ENGINEERED MUTATION
SEQADV 1W8P TYR D 25 UNP P01308 PHE 49 ENGINEERED MUTATION
SEQADV 1W8P PHE D 26 UNP P01308 TYR 50 ENGINEERED MUTATION
SEQADV 1W8P TYR F 25 UNP P01308 PHE 49 ENGINEERED MUTATION
SEQADV 1W8P PHE F 26 UNP P01308 TYR 50 ENGINEERED MUTATION
SEQADV 1W8P TYR H 25 UNP P01308 PHE 49 ENGINEERED MUTATION
SEQADV 1W8P PHE H 26 UNP P01308 TYR 50 ENGINEERED MUTATION
SEQADV 1W8P TYR J 25 UNP P01308 PHE 49 ENGINEERED MUTATION
SEQADV 1W8P PHE J 26 UNP P01308 TYR 50 ENGINEERED MUTATION
SEQADV 1W8P TYR L 25 UNP P01308 PHE 49 ENGINEERED MUTATION
SEQADV 1W8P PHE L 26 UNP P01308 TYR 50 ENGINEERED MUTATION
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 TYR PHE
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 TYR PHE
SEQRES 3 D 30 THR PRO LYS 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 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 F 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE TYR PHE
SEQRES 3 F 30 THR PRO LYS 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 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 H 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE TYR PHE
SEQRES 3 H 30 THR PRO LYS 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 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 J 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE TYR PHE
SEQRES 3 J 30 THR PRO LYS 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 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 L 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE TYR PHE
SEQRES 3 L 30 THR PRO LYS THR
HET IPH A1022 7
HET ZN B1030 1
HET IPH C1022 7
HET ZN D1030 1
HET IPH E1022 7
HET IPH G1022 7
HET IPH I1022 7
HET IPH K1022 7
HETNAM IPH PHENOL
HETNAM ZN ZINC ION
FORMUL 13 IPH 6(C6 H6 O)
FORMUL 14 ZN 2(ZN 2+)
FORMUL 21 HOH *83(H2 O)
HELIX 1 1 ILE A 2 SER A 9 1 8
HELIX 2 2 SER A 12 ASN A 18 1 7
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 SER C 9 1 9
HELIX 6 6 SER C 12 ASN C 18 1 7
HELIX 7 7 PHE D 1 GLY D 20 1 20
HELIX 8 8 GLU D 21 GLY D 23 5 3
HELIX 9 9 GLY E 1 CYS E 7 1 7
HELIX 10 10 SER E 12 ASN E 18 1 7
HELIX 11 11 PHE F 1 GLY F 20 1 20
HELIX 12 12 GLU F 21 GLY F 23 5 3
HELIX 13 13 ILE G 2 THR G 8 1 7
HELIX 14 14 SER G 12 GLU G 17 1 6
HELIX 15 15 PHE H 1 GLY H 20 1 20
HELIX 16 16 GLU H 21 GLY H 23 5 3
HELIX 17 17 GLY I 1 CYS I 7 1 7
HELIX 18 18 SER I 12 GLU I 17 1 6
HELIX 19 19 PHE J 1 GLY J 20 1 20
HELIX 20 20 GLU J 21 GLY J 23 5 3
HELIX 21 21 GLY K 1 CYS K 7 1 7
HELIX 22 22 SER K 12 GLU K 17 1 6
HELIX 23 23 PHE L 1 GLY L 20 1 20
HELIX 24 24 GLU L 21 GLY L 23 5 3
SHEET 1 BA 2 PHE B 24 TYR B 25 0
SHEET 2 BA 2 TYR D 25 PHE D 26 -1 O PHE D 26 N PHE B 24
SHEET 1 JA 2 PHE J 24 TYR J 25 0
SHEET 2 JA 2 TYR L 25 PHE L 26 -1 O PHE L 26 N PHE J 24
SSBOND 1 CYS A 6 CYS A 11 1555 1555 1.98
SSBOND 2 CYS A 7 CYS B 7 1555 1555 2.01
SSBOND 3 CYS A 20 CYS B 19 1555 1555 2.05
SSBOND 4 CYS C 6 CYS C 11 1555 1555 1.98
SSBOND 5 CYS C 7 CYS D 7 1555 1555 2.00
SSBOND 6 CYS C 20 CYS D 19 1555 1555 2.03
SSBOND 7 CYS E 6 CYS E 11 1555 1555 2.01
SSBOND 8 CYS E 7 CYS F 7 1555 1555 2.02
SSBOND 9 CYS E 20 CYS F 19 1555 1555 2.02
SSBOND 10 CYS G 6 CYS G 11 1555 1555 1.99
SSBOND 11 CYS G 7 CYS H 7 1555 1555 2.03
SSBOND 12 CYS G 20 CYS H 19 1555 1555 2.03
SSBOND 13 CYS I 6 CYS I 11 1555 1555 1.96
SSBOND 14 CYS I 7 CYS J 7 1555 1555 2.04
SSBOND 15 CYS I 20 CYS J 19 1555 1555 2.02
SSBOND 16 CYS K 6 CYS K 11 1555 1555 1.98
SSBOND 17 CYS K 7 CYS L 7 1555 1555 2.02
SSBOND 18 CYS K 20 CYS L 19 1555 1555 2.04
LINK NE2 HIS B 10 ZN ZN B1030 1555 1555 2.00
LINK ZN ZN B1030 O HOH B2009 1555 1555 2.20
LINK ZN ZN B1030 NE2 HIS F 10 1555 1555 2.05
LINK ZN ZN B1030 NE2 HIS J 10 1555 1555 2.08
LINK NE2 HIS D 10 ZN ZN D1030 1555 1555 2.22
LINK ZN ZN D1030 O HOH D2012 1555 1555 2.19
LINK ZN ZN D1030 NE2 HIS H 10 1555 1555 2.06
LINK ZN ZN D1030 NE2 HIS L 10 1555 1555 2.02
CISPEP 1 CYS A 20 ASN A 21 0 16.95
SITE 1 AC1 4 HIS B 10 HOH B2009 HIS F 10 HIS J 10
SITE 1 AC2 4 HIS D 10 HOH D2012 HIS H 10 HIS L 10
SITE 1 AC3 4 CYS A 6 SER A 9 ILE A 10 CYS A 11
SITE 1 AC4 3 CYS C 6 ILE C 10 CYS C 11
SITE 1 AC5 3 CYS E 6 CYS E 11 LEU F 11
SITE 1 AC6 6 VAL D 2 HIS D 5 CYS G 6 ILE G 10
SITE 2 AC6 6 CYS G 11 LEU H 11
SITE 1 AC7 4 CYS I 6 ILE I 10 CYS I 11 LEU J 11
SITE 1 AC8 6 HIS H 5 CYS K 6 SER K 9 ILE K 10
SITE 2 AC8 6 CYS K 11 LEU L 11
CRYST1 59.903 62.116 47.796 90.00 110.58 90.00 P 1 21 1 12
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 0.016694 0.000000 0.006268 0.00000
SCALE2 0.000000 0.016099 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022349 0.00000
(ATOM LINES ARE NOT SHOWN.)
END