Header list of 3aiy.pdb file
Complete list - 16 20 Bytes
HEADER HORMONE/GROWTH FACTOR 29-DEC-98 3AIY
TITLE R6 HUMAN INSULIN HEXAMER (SYMMETRIC), NMR, REFINED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (INSULIN);
COMPND 3 CHAIN: A, C, E, G, I, K;
COMPND 4 FRAGMENT: ALPHA CHAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: A PHENOL MOLECULE IS NON-COVALENTLY ATTACHED TO EACH
COMPND 7 INSULIN MONOMER;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROTEIN (INSULIN);
COMPND 10 CHAIN: B, D, F, H, J, L;
COMPND 11 FRAGMENT: BETA CHAIN;
COMPND 12 ENGINEERED: YES;
COMPND 13 OTHER_DETAILS: A PHENOL MOLECULE IS NON-COVALENTLY ATTACHED TO EACH
COMPND 14 INSULIN MONOMER
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PROTEIN WAS CHEMICALLY SYNTHESIZED FROM THE
SOURCE 4 SECRETION OF HUMAN (HOMO SAPIENS) PANCREATIC CELLS.;
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 OTHER_DETAILS: THE PROTEIN WAS CHEMICALLY SYNTHESIZED FROM THE
SOURCE 8 SECRETION OF HUMAN (HOMO SAPIENS) PANCREATIC CELLS.
KEYWDS HORMONE, GLUCOSE METABOLISM, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
AUTHOR S.I.O'DONOGHUE,X.CHANG,R.ABSEHER,M.NILGES,J.J.LED
REVDAT 4 16-MAR-22 3AIY 1 REMARK
REVDAT 3 24-FEB-09 3AIY 1 VERSN
REVDAT 2 01-APR-03 3AIY 1 JRNL
REVDAT 1 28-FEB-00 3AIY 0
JRNL AUTH S.I.O'DONOGHUE,X.CHANG,R.ABSEHER,M.NILGES,J.J.LED
JRNL TITL UNRAVELING THE SYMMETRY AMBIGUITY IN A HEXAMER: CALCULATION
JRNL TITL 2 OF THE R6 HUMAN INSULIN STRUCTURE.
JRNL REF J.BIOMOL.NMR V. 16 93 2000
JRNL REFN ISSN 0925-2738
JRNL PMID 10723989
JRNL DOI 10.1023/A:1008323819099
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.I.O'DONOGHUE,M.NILGES
REMARK 1 TITL CALCULATION OF SYMMETRIC OLIGOMER STRUCTURES FROM NMR DATA
REMARK 1 EDIT N.R.KRISHNA, J.BERLINER
REMARK 1 REF STRUCTURE, COMPUTATION AND 1999
REMARK 1 REF 2 DYNAMICS IN PROTEIN NMR (IN:
REMARK 1 REF 3 BIOLOGICAL MAGNETIC
REMARK 1 REF 4 RESONANCE, V. 17)
REMARK 1 PUBL NEW YORK : PLENUM PRESS
REMARK 1 REFN ISSN 0-306-45953-1
REMARK 1 REFERENCE 2
REMARK 1 AUTH X.CHANG,A.M.JORGENSEN,P.BARDRUM,J.J.LED
REMARK 1 TITL SOLUTION STRUCTURES OF THE R6 HUMAN INSULIN HEXAMER
REMARK 1 REF BIOCHEMISTRY V. 36 9409 1997
REMARK 1 REFN ISSN 0006-2960
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:
REMARK 3 REFINEMENT WAS DONE IN A SHELL OF WATER MOLECULES (J.P.LINGE,
REMARK 3 M.NILGES,1998,
REMARK 3 J.BIOMOL.NMR, IN PRESS).
REMARK 4
REMARK 4 3AIY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000007014.
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 : 1 ATM
REMARK 210 SAMPLE CONTENTS : H2O AND D2O
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 : SYMMETRY-ADR METHOD: SIMULATED
REMARK 210 ANNEALING, WATER-SHELL
REMARK 210 REFINEMENT, AND ENERGY
REMARK 210 MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TOTAL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: IONIC_STRENGTH: NULL PRESSURE: NULL SOLVENT SYSTEM: H2O
REMARK 210 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: 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 27.65 -151.46
REMARK 500 ILE A 10 132.54 62.77
REMARK 500 VAL B 2 102.11 -48.46
REMARK 500 ASN B 3 -169.34 -108.58
REMARK 500 GLN B 4 -84.86 59.91
REMARK 500 SER C 9 27.90 -151.30
REMARK 500 ILE C 10 132.79 62.60
REMARK 500 VAL D 2 101.76 -48.46
REMARK 500 ASN D 3 -169.31 -108.45
REMARK 500 GLN D 4 -84.73 59.89
REMARK 500 SER E 9 28.08 -151.78
REMARK 500 ILE E 10 132.75 62.46
REMARK 500 VAL F 2 101.83 -48.61
REMARK 500 ASN F 3 -168.91 -108.28
REMARK 500 GLN F 4 -84.84 59.66
REMARK 500 SER G 9 27.61 -151.78
REMARK 500 ILE G 10 132.44 62.79
REMARK 500 VAL H 2 101.98 -48.40
REMARK 500 ASN H 3 -169.30 -108.68
REMARK 500 GLN H 4 -84.98 59.88
REMARK 500 SER I 9 27.89 -151.66
REMARK 500 ILE I 10 132.75 62.66
REMARK 500 VAL J 2 101.71 -48.43
REMARK 500 ASN J 3 -169.32 -108.37
REMARK 500 GLN J 4 -84.95 59.95
REMARK 500 SER K 9 27.62 -151.75
REMARK 500 ILE K 10 132.56 62.86
REMARK 500 VAL L 2 101.79 -48.40
REMARK 500 ASN L 3 -169.22 -108.42
REMARK 500 GLN L 4 -84.87 59.85
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 ARG B 22 0.15 SIDE CHAIN
REMARK 500 ARG D 22 0.15 SIDE CHAIN
REMARK 500 ARG F 22 0.15 SIDE CHAIN
REMARK 500 ARG H 22 0.15 SIDE CHAIN
REMARK 500 ARG J 22 0.15 SIDE CHAIN
REMARK 500 ARG L 22 0.15 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZN1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: IN THE CRYSTAL STRUCTURE, 1ZNJ, THESE RESIDUES
REMARK 800 ARE COORDINATED BY A ZINC ATOM. THE ZINC ATOM IS NOT INCLUDED
REMARK 800 SINCE IT COULD NOT BE OBSERVED IN THE NMR SPECTRA.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZN2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: IN THE CRYSTAL STRUCTURE, 1ZNJ, THESE RESIDUES
REMARK 800 ARE COORDINATED BY A ZINC ATOM. THE ZINC ATOM IS NOT INCLUDED
REMARK 800 SINCE IT COULD NOT BE OBSERVED IN THE NMR SPECTRA.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH A 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH C 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH E 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH G 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH I 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPH K 22
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AIY RELATED DB: PDB
REMARK 900 ENSEMBLE OF THE 20 LOWEST ENERGY STRUCTURES
REMARK 900 RELATED ID: 4AIY RELATED DB: PDB
REMARK 900 STRUCTURES IN THE ENSEMBLE CLUSTER INTO TWO DISTINCT SUBSTATES, ONE
REMARK 900 IS DENOTED 'GREEN' IN 4AIY
REMARK 900 RELATED ID: 5AIY RELATED DB: PDB
REMARK 900 STRUCTURES IN THE ENSEMBLE CLUSTER INTO TWO DISTINCT SUBSTATES, ONE
REMARK 900 IS DENOTED 'RED' IN 5AIY
DBREF 3AIY A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 3AIY B 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 3AIY C 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 3AIY D 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 3AIY E 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 3AIY F 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 3AIY G 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 3AIY H 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 3AIY I 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 3AIY J 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 3AIY K 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 3AIY 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 IPH A 22 13
HET IPH C 22 13
HET IPH E 22 13
HET IPH G 22 13
HET IPH I 22 13
HET IPH K 22 13
HETNAM IPH PHENOL
FORMUL 13 IPH 6(C6 H6 O)
HELIX 1 1 VAL A 3 CYS A 6 1 4
HELIX 2 2 LEU A 13 TYR A 19 1 7
HELIX 3 3 GLY B 8 CYS B 19 1 12
HELIX 4 4 VAL C 3 SER C 9 1 7
HELIX 5 5 LEU C 13 TYR C 19 1 7
HELIX 6 6 GLY D 8 CYS D 19 1 12
HELIX 7 7 VAL E 3 SER E 9 1 7
HELIX 8 8 LEU E 13 TYR E 19 1 7
HELIX 9 9 GLY F 8 CYS F 19 1 12
HELIX 10 10 VAL G 3 CYS G 6 1 4
HELIX 11 11 LEU G 13 TYR G 19 1 7
HELIX 12 12 GLY H 8 CYS H 19 1 12
HELIX 13 13 VAL I 3 SER I 9 1 7
HELIX 14 14 LEU I 13 TYR I 19 1 7
HELIX 15 15 GLY J 8 CYS J 19 1 12
HELIX 16 16 VAL K 3 CYS K 6 1 4
HELIX 17 17 LEU K 13 TYR K 19 1 7
HELIX 18 18 GLY L 8 CYS L 19 1 12
SHEET 1 A 2 PHE B 24 TYR B 26 0
SHEET 2 A 2 PHE D 24 TYR D 26 -1 N PHE D 24 O TYR B 26
SHEET 1 B 2 PHE F 24 TYR F 26 0
SHEET 2 B 2 PHE H 24 TYR H 26 -1 N PHE H 24 O TYR F 26
SHEET 1 C 2 PHE J 24 TYR J 26 0
SHEET 2 C 2 PHE L 24 TYR L 26 -1 N PHE L 24 O TYR J 26
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
SITE 1 ZN1 3 HIS B 10 HIS F 10 HIS J 10
SITE 1 ZN2 3 HIS D 10 HIS H 10 HIS L 10
SITE 1 AC1 7 ILE A 10 CYS A 11 LEU A 16 LEU B 11
SITE 2 AC1 7 ALA B 14 LEU F 6 LEU H 17
SITE 1 AC2 7 ILE C 10 CYS C 11 LEU C 16 LEU D 11
SITE 2 AC2 7 ALA D 14 LEU J 17 LEU L 6
SITE 1 AC3 7 ILE E 10 CYS E 11 LEU E 16 LEU F 11
SITE 2 AC3 7 ALA F 14 LEU J 6 LEU L 17
SITE 1 AC4 7 LEU B 17 LEU D 6 ILE G 10 CYS G 11
SITE 2 AC4 7 LEU G 16 LEU H 11 ALA H 14
SITE 1 AC5 7 LEU B 6 LEU D 17 ILE I 10 CYS I 11
SITE 2 AC5 7 LEU I 16 LEU J 11 ALA J 14
SITE 1 AC6 7 LEU F 17 LEU H 6 ILE K 10 CYS K 11
SITE 2 AC6 7 LEU K 16 LEU L 11 ALA L 14
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
Complete list - 16 20 Bytes