Header list of 1ai0.pdb file
Complete list - b 16 2 Bytes
HEADER HORMONE 30-APR-97 1AI0
TITLE R6 HUMAN INSULIN HEXAMER (NON-SYMMETRIC), NMR, 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: R6 INSULIN HEXAMER;
COMPND 3 CHAIN: A, C, E, G, I, K;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: R6 INSULIN HEXAMER;
COMPND 6 CHAIN: B, D, F, H, J, L
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: PANCREAS;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_COMMON: HUMAN;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 ORGAN: PANCREAS
KEYWDS HORMONE, GLUCOSE METABOLISM
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR X.CHANG,A.M.M.JORGENSEN,P.BARDRUM,J.J.LED
REVDAT 4 16-FEB-22 1AI0 1 REMARK LINK
REVDAT 3 09-JUN-09 1AI0 1 REVDAT
REVDAT 2 24-FEB-09 1AI0 1 VERSN
REVDAT 1 12-NOV-97 1AI0 0
JRNL AUTH X.CHANG,A.M.JORGENSEN,P.BARDRUM,J.J.LED
JRNL TITL SOLUTION STRUCTURES OF THE R6 HUMAN INSULIN HEXAMER.
JRNL REF BIOCHEMISTRY V. 36 9409 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9235985
JRNL DOI 10.1021/BI9631069
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AI0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170840.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 8.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D DQF-COSY; NOESY AND TOCSY; 2D
REMARK 210 13C-1H HSQC; HSQC-TOCSY; 3D
REMARK 210 TOCSY-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AM500; UNITY INOVA PLUS
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING AND ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TOTAL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: SOLVENT SYSTEM: H2O AND D2O
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 ZN ZN H 31 H1 HOH H 32 1.46
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 1 GLU A 4 55.01 -107.48
REMARK 500 1 GLN A 5 -36.83 -176.37
REMARK 500 1 ILE A 10 107.52 -44.61
REMARK 500 1 ASN B 3 -38.60 173.32
REMARK 500 1 GLU B 21 49.50 78.86
REMARK 500 1 ARG B 22 -54.81 -124.21
REMARK 500 1 GLU C 4 53.11 -105.98
REMARK 500 1 GLN C 5 -36.44 -174.34
REMARK 500 1 ILE C 10 108.05 -44.29
REMARK 500 1 ASN D 3 -38.82 170.92
REMARK 500 1 GLU D 21 50.81 79.55
REMARK 500 1 ARG D 22 -51.90 -126.15
REMARK 500 1 GLU E 4 53.22 -108.04
REMARK 500 1 GLN E 5 -34.89 -174.78
REMARK 500 1 SER E 9 117.97 -169.19
REMARK 500 1 ILE E 10 106.94 -42.25
REMARK 500 1 ASN F 3 -41.07 174.32
REMARK 500 1 GLU F 21 49.51 79.65
REMARK 500 1 GLU G 4 52.45 -105.70
REMARK 500 1 GLN G 5 -34.72 -173.05
REMARK 500 1 SER G 9 119.43 -168.75
REMARK 500 1 ILE G 10 106.86 -42.82
REMARK 500 1 ASN H 3 -37.26 170.72
REMARK 500 1 GLU H 21 50.68 80.93
REMARK 500 1 ARG H 22 -56.81 -124.26
REMARK 500 1 GLU I 4 49.40 -108.09
REMARK 500 1 GLN I 5 -34.14 -170.12
REMARK 500 1 SER I 9 119.29 -167.52
REMARK 500 1 ILE I 10 107.74 -43.73
REMARK 500 1 ASN J 3 -38.75 171.80
REMARK 500 1 GLU J 21 45.17 167.44
REMARK 500 1 GLU K 4 51.96 -103.95
REMARK 500 1 GLN K 5 -37.97 -172.28
REMARK 500 1 SER K 9 119.85 -165.27
REMARK 500 1 ILE K 10 107.06 -42.99
REMARK 500 1 ASN L 3 -40.24 172.86
REMARK 500 1 GLU L 21 48.08 80.38
REMARK 500 1 ARG L 22 -53.86 -121.36
REMARK 500 2 GLN A 5 -39.29 -156.34
REMARK 500 2 ILE A 10 104.79 -46.81
REMARK 500 2 TYR A 19 55.74 -99.94
REMARK 500 2 ASN B 3 -40.76 179.96
REMARK 500 2 PRO B 28 -88.35 -76.42
REMARK 500 2 LYS B 29 -153.97 59.29
REMARK 500 2 GLU C 4 48.27 -102.86
REMARK 500 2 GLN C 5 -36.04 -166.44
REMARK 500 2 ILE C 10 101.14 -48.76
REMARK 500 2 TYR C 19 57.58 -101.39
REMARK 500 2 ASN D 3 -42.90 179.25
REMARK 500 2 PRO D 28 -87.30 -77.32
REMARK 500
REMARK 500 THIS ENTRY HAS 326 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 2 ARG B 22 0.16 SIDE CHAIN
REMARK 500 2 ARG D 22 0.16 SIDE CHAIN
REMARK 500 2 ARG F 22 0.15 SIDE CHAIN
REMARK 500 2 ARG H 22 0.17 SIDE CHAIN
REMARK 500 2 ARG J 22 0.16 SIDE CHAIN
REMARK 500 2 ARG L 22 0.16 SIDE CHAIN
REMARK 500 3 ARG B 22 0.28 SIDE CHAIN
REMARK 500 3 ARG D 22 0.29 SIDE CHAIN
REMARK 500 3 ARG F 22 0.27 SIDE CHAIN
REMARK 500 3 ARG H 22 0.29 SIDE CHAIN
REMARK 500 3 ARG J 22 0.29 SIDE CHAIN
REMARK 500 3 ARG L 22 0.28 SIDE CHAIN
REMARK 500 5 ARG B 22 0.28 SIDE CHAIN
REMARK 500 5 ARG D 22 0.26 SIDE CHAIN
REMARK 500 5 ARG F 22 0.29 SIDE CHAIN
REMARK 500 5 ARG H 22 0.28 SIDE CHAIN
REMARK 500 5 ARG J 22 0.28 SIDE CHAIN
REMARK 500 5 ARG L 22 0.28 SIDE CHAIN
REMARK 500 6 ARG B 22 0.22 SIDE CHAIN
REMARK 500 6 ARG D 22 0.21 SIDE CHAIN
REMARK 500 6 ARG F 22 0.20 SIDE CHAIN
REMARK 500 6 ARG H 22 0.21 SIDE CHAIN
REMARK 500 6 ARG J 22 0.22 SIDE CHAIN
REMARK 500 6 ARG L 22 0.20 SIDE CHAIN
REMARK 500 7 ARG B 22 0.17 SIDE CHAIN
REMARK 500 7 ARG D 22 0.16 SIDE CHAIN
REMARK 500 7 ARG F 22 0.17 SIDE CHAIN
REMARK 500 7 ARG H 22 0.19 SIDE CHAIN
REMARK 500 7 ARG J 22 0.18 SIDE CHAIN
REMARK 500 7 ARG L 22 0.14 SIDE CHAIN
REMARK 500 8 ARG B 22 0.16 SIDE CHAIN
REMARK 500 8 ARG D 22 0.19 SIDE CHAIN
REMARK 500 8 ARG F 22 0.16 SIDE CHAIN
REMARK 500 8 ARG H 22 0.16 SIDE CHAIN
REMARK 500 8 ARG J 22 0.13 SIDE CHAIN
REMARK 500 8 ARG L 22 0.17 SIDE CHAIN
REMARK 500 9 ARG B 22 0.31 SIDE CHAIN
REMARK 500 9 ARG D 22 0.31 SIDE CHAIN
REMARK 500 9 ARG F 22 0.32 SIDE CHAIN
REMARK 500 9 ARG H 22 0.31 SIDE CHAIN
REMARK 500 9 ARG J 22 0.31 SIDE CHAIN
REMARK 500 9 ARG L 22 0.32 SIDE CHAIN
REMARK 500 10 ARG B 22 0.10 SIDE CHAIN
REMARK 500 10 ARG D 22 0.09 SIDE CHAIN
REMARK 500 10 ARG H 22 0.10 SIDE CHAIN
REMARK 500 10 ARG J 22 0.11 SIDE CHAIN
REMARK 500 10 ARG L 22 0.13 SIDE CHAIN
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 B 31 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 10 NE2
REMARK 620 2 HIS F 10 NE2 117.5
REMARK 620 3 HIS J 10 NE2 114.9 112.4
REMARK 620 4 HOH J 31 O 106.6 102.5 100.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 31 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 10 NE2
REMARK 620 2 HIS H 10 NE2 115.8
REMARK 620 3 HOH H 32 O 107.8 108.9
REMARK 620 4 HIS L 10 NE2 109.2 105.9 109.2
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 B 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH B 32
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH D 32
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH E 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH G 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH J 32
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH L 32
DBREF 1AI0 A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1AI0 B 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1AI0 C 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1AI0 D 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1AI0 E 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1AI0 F 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1AI0 G 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1AI0 H 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1AI0 I 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1AI0 J 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 1AI0 K 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1AI0 L 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
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 PHE TYR
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 PHE TYR
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 PHE TYR
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 PHE TYR
SEQRES 3 L 30 THR PRO LYS THR
HET ZN B 31 1
HET IPH B 32 13
HET IPH D 32 13
HET IPH E 22 13
HET IPH G 22 13
HET ZN H 31 1
HET IPH J 32 13
HET IPH L 32 13
HETNAM ZN ZINC ION
HETNAM IPH PHENOL
FORMUL 13 ZN 2(ZN 2+)
FORMUL 14 IPH 6(C6 H6 O)
FORMUL 21 HOH *2(H2 O)
HELIX 1 1 LEU A 13 TYR A 19 1 7
HELIX 2 2 GLN B 4 CYS B 19 1 16
HELIX 3 3 LEU C 13 TYR C 19 1 7
HELIX 4 4 GLN D 4 CYS D 19 1 16
HELIX 5 5 LEU E 13 TYR E 19 1 7
HELIX 6 6 GLN F 4 CYS F 19 1 16
HELIX 7 7 LEU G 13 TYR G 19 1 7
HELIX 8 8 GLN H 4 CYS H 19 1 16
HELIX 9 9 LEU I 13 TYR I 19 1 7
HELIX 10 10 GLN J 4 CYS J 19 1 16
HELIX 11 11 LEU K 13 TYR K 19 1 7
HELIX 12 12 GLN L 4 CYS L 19 1 16
SHEET 1 A 2 PHE B 24 TYR B 26 0
SHEET 2 A 2 PHE D 24 TYR D 26 -1 N TYR D 26 O PHE B 24
SHEET 1 B 2 PHE F 24 TYR F 26 0
SHEET 2 B 2 PHE H 24 TYR H 26 -1 N TYR H 26 O PHE F 24
SHEET 1 C 2 PHE J 24 TYR J 26 0
SHEET 2 C 2 PHE L 24 TYR L 26 -1 N TYR L 26 O PHE J 24
SSBOND 1 CYS A 6 CYS A 11 1555 1555 2.02
SSBOND 2 CYS A 7 CYS B 7 1555 1555 2.02
SSBOND 3 CYS A 20 CYS B 19 1555 1555 2.02
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 2.02
SSBOND 7 CYS E 6 CYS E 11 1555 1555 2.02
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 2.02
SSBOND 11 CYS G 7 CYS H 7 1555 1555 2.02
SSBOND 12 CYS G 20 CYS H 19 1555 1555 2.02
SSBOND 13 CYS I 6 CYS I 11 1555 1555 2.02
SSBOND 14 CYS I 7 CYS J 7 1555 1555 2.02
SSBOND 15 CYS I 20 CYS J 19 1555 1555 2.02
SSBOND 16 CYS K 6 CYS K 11 1555 1555 2.02
SSBOND 17 CYS K 7 CYS L 7 1555 1555 2.02
SSBOND 18 CYS K 20 CYS L 19 1555 1555 2.02
LINK NE2 HIS B 10 ZN ZN B 31 1555 1555 2.45
LINK ZN ZN B 31 NE2 HIS F 10 1555 1555 2.42
LINK ZN ZN B 31 NE2 HIS J 10 1555 1555 2.36
LINK ZN ZN B 31 O HOH J 31 1555 1555 2.14
LINK NE2 HIS D 10 ZN ZN H 31 1555 1555 2.45
LINK NE2 HIS H 10 ZN ZN H 31 1555 1555 2.12
LINK ZN ZN H 31 O HOH H 32 1555 1555 2.22
LINK ZN ZN H 31 NE2 HIS L 10 1555 1555 2.27
SITE 1 AC1 4 LEU B 6 HIS B 10 LEU F 6 HIS F 10
SITE 1 AC2 7 GLN A 5 CYS A 6 ILE A 10 CYS A 11
SITE 2 AC2 7 SER A 12 HIS B 10 HIS F 5
SITE 1 AC3 7 ILE C 2 GLN C 5 CYS C 6 ILE C 10
SITE 2 AC3 7 CYS C 11 LEU C 16 HIS D 10
SITE 1 AC4 6 GLN E 5 CYS E 6 ILE E 10 CYS F 7
SITE 2 AC4 6 HIS F 10 HIS J 5
SITE 1 AC5 7 LEU B 17 VAL D 2 HIS D 5 LEU D 6
SITE 2 AC5 7 CYS G 6 ILE G 10 CYS G 11
SITE 1 AC6 3 LEU D 6 HIS D 10 LEU H 6
SITE 1 AC7 4 VAL B 2 HIS B 5 LEU D 17 GLN I 5
SITE 1 AC8 6 LEU F 17 HIS H 5 LEU H 6 GLN K 5
SITE 2 AC8 6 CYS K 6 ILE K 10
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - b 16 2 Bytes