HEADER HORMONE 09-DEC-11 3V1G
TITLE FORESTALLING INSULIN FIBRILLATION BY INSERTION OF A CHIRAL CLAMP
TITLE 2 MECHANISM-BASED APPLICATION OF PROTEIN ENGINEERING TO GLOBAL HEALTH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN;
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: INSULIN;
COMPND 7 CHAIN: B, D;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606
KEYWDS ZINC-BINDING SITE, LONG-ACTING INSULIN ANALOG, RECEPTOR BINDING
KEYWDS 2 PROTEIN ENGINEERING, INSULIN FIBRILLATION, HORMONE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.L.WAN,Q.X.HUA,N.P.WICKRAMASINGHE,K.HUANG,A.T.PETKOVA,S.Q.HU,
AUTHOR 2 N.B.PHILLIPS,I.J.YEH,J.WHITTAKE,F.ISMAIL-BEIGI,P.G.KATSOYYANNIS,
AUTHOR 3 R.TYCKO,M.A.WEISS
REVDAT 3 13-SEP-23 3V1G 1 REMARK SEQADV LINK
REVDAT 2 27-SEP-17 3V1G 1 REMARK
REVDAT 1 12-DEC-12 3V1G 0
JRNL AUTH Z.L.WAN,Q.X.HUA,N.P.WICKRAMASINGHE,K.HUANG,A.T.PETKOVA,
JRNL AUTH 2 S.Q.HU,N.B.PHILLIPS,I.J.YEH,J.WHITTAKE,F.ISMAIL-BEIGI,
JRNL AUTH 3 P.G.KATSOYYANNIS,R.TYCKO,M.A.WEISS
JRNL TITL FORESTALLING INSULIN FIBRILLATION BY INSERTION OF A CHIRAL
JRNL TITL 2 CLAMP MECHANISM-BASED APPLICATION OF PROTEIN ENGINEERING TO
JRNL TITL 3 GLOBAL HEALTH
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Z.L.WAN,K.HUANG,B.XU,S.Q.HU,S.WANG,Y.C.CHU,P.G.KATSOYANNIS,
REMARK 1 AUTH 2 M.A.WEISS
REMARK 1 TITL DIABETES-ASSOCIATED MUTATIONS IN HUMAN INSULIN: CRYSTAL
REMARK 1 TITL 2 STRUCTURE AND PHOTO-CROSS-LINKING STUDIES OF A-CHAIN VARIANT
REMARK 1 TITL 3 INSULIN WAKAYAMA
REMARK 1 REF BIOCHEMISTRY V.(13) 5000 2005
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH Z.L.WAN,B.XU,Y.C.CHU,P.G.KATSOYANNIS,M.A.WEISS
REMARK 1 TITL CRYSTAL STRUCTURE OF ALLO-ILE(A2)-INSULIN, AN INACTIVE
REMARK 1 TITL 2 CHIRAL ANALOGUE: IMPLICATIONS FOR THE MECHANISM OF RECEPTOR
REMARK 1 TITL 3 BINDING
REMARK 1 REF BIOCHEMISTRY V.(44) 12770 2003
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH Z.L WAN,B.XU,Y.C.CHU,B.LI,S.H.NAKAGAWA,Y.QU,S.Q.HU,
REMARK 1 AUTH 2 P.G.KATSOYANNIS,M.A.WEISS
REMARK 1 TITL ENHANCING THE ACTIVITY OF INSULIN AT THE RECEPTOR INTERFACE:
REMARK 1 TITL 2 CRYSTAL STRUCTURE AND PHOTO-CROSS-LINKING OF A8 ANALOGUES
REMARK 1 REF BIOCHEMISTRY V.(51) 16119 2004
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH E.N.BAKER,T.L.BLUNDELL,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 5
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 6
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 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.54
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) (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 4212
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) : 0.229
REMARK 3 FREE R VALUE : 0.323
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 448
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE : 0.3910
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 56
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.052
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 : 10
REMARK 3 SOLVENT ATOMS : 81
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.06000
REMARK 3 B22 (A**2) : -4.06000
REMARK 3 B33 (A**2) : 8.13000
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) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.15
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 5.410
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 3V1G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-DEC-11.
REMARK 100 THE DEPOSITION ID IS D_1000069474.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JAN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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) : 1.5418
REMARK 200 MONOCHROMATOR : MONOCHROMATOR MIRROR
REMARK 200 OPTICS : OPTICS MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER AXIOM 200
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PROTEUM PLUS
REMARK 200 DATA SCALING SOFTWARE : PROTEUM PLUS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 4321
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 39.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.03600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.23200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
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 (%): 36.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
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 8.0, VAPOR
REMARK 280 DIFFUSION, 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 39.54050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.82872
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 12.46733
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 39.54050
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 22.82872
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 12.46733
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 39.54050
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 22.82872
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 12.46733
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 45.65744
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 24.93467
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 45.65744
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 24.93467
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 45.65744
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 24.93467
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: 19020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -294.0 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 79.08100
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 39.54050
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 68.48615
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 D 32 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 LYS B 29 -54.31 -151.43
REMARK 500 PRO D 28 -85.68 -87.62
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 DGL B 21
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGL D 21
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH C 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
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
REMARK 900 RELATED ID: 3V19 RELATED DB: PDB
DBREF 3V1G A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 3V1G B 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 3V1G C 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 3V1G D 1 30 UNP P01308 INS_HUMAN 25 54
SEQADV 3V1G DGL B 21 UNP P01308 GLU 45 ENGINEERED MUTATION
SEQADV 3V1G DGL D 21 UNP P01308 GLU 45 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 DGL 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 DGL ARG GLY PHE PHE TYR
SEQRES 3 D 30 THR PRO LYS THR
HET DGL B 21 9
HET DGL D 21 9
HET ZN B 31 1
HET IPH C 200 7
HET ZN D 31 1
HET CL D 32 1
HETNAM DGL D-GLUTAMIC ACID
HETNAM ZN ZINC ION
HETNAM IPH PHENOL
HETNAM CL CHLORIDE ION
FORMUL 2 DGL 2(C5 H9 N O4)
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 IPH C6 H6 O
FORMUL 8 CL CL 1-
FORMUL 9 HOH *81(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 ASN A 18 CYS A 20 5 3
HELIX 4 4 GLY B 8 GLY B 20 1 13
HELIX 5 5 DGL B 21 GLY B 23 5 3
HELIX 6 6 ILE C 2 CYS C 7 1 6
HELIX 7 7 SER C 12 ASN C 18 1 7
HELIX 8 8 ASN D 3 GLY D 20 1 18
HELIX 9 9 DGL 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 TYR D 26 N PHE B 24
SSBOND 1 CYS A 6 CYS A 11 1555 1555 2.03
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 2.04
SSBOND 5 CYS C 7 CYS D 7 1555 1555 2.03
SSBOND 6 CYS C 20 CYS D 19 1555 1555 2.03
LINK C GLY B 20 N DGL B 21 1555 1555 1.33
LINK C DGL B 21 N ARG B 22 1555 1555 1.33
LINK C GLY D 20 N DGL D 21 1555 1555 1.33
LINK C DGL D 21 N ARG D 22 1555 1555 1.33
LINK NE2 HIS B 10 ZN ZN B 31 1555 1555 2.07
LINK NE2 HIS D 10 ZN ZN D 31 1555 1555 2.06
SITE 1 AC1 9 CYS B 19 GLY B 20 ARG B 22 GLY B 23
SITE 2 AC1 9 HOH B 76 PRO D 28 LYS D 29 THR D 30
SITE 3 AC1 9 HOH D 68
SITE 1 AC2 8 PRO B 28 CYS D 19 GLY D 20 ARG D 22
SITE 2 AC2 8 GLY D 23 HOH D 43 HOH D 47 HOH D 49
SITE 1 AC3 1 HIS B 10
SITE 1 AC4 6 CYS C 6 SER C 9 ILE C 10 CYS C 11
SITE 2 AC4 6 HIS D 5 LEU D 11
SITE 1 AC5 2 HIS D 10 CL D 32
SITE 1 AC6 2 HIS D 10 ZN D 31
CRYST1 79.081 79.081 37.402 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 0.012645 0.007301 0.000000 0.00000
SCALE2 0.000000 0.014601 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026737 0.00000
(ATOM LINES ARE NOT SHOWN.)
END