Header list of 1dby.pdb file
Complete list - b 16 2 Bytes
HEADER OXIDOREDUCTASE 03-NOV-99 1DBY
TITLE NMR STRUCTURES OF CHLOROPLAST THIOREDOXIN M CH2 FROM THE GREEN ALGA
TITLE 2 CHLAMYDOMONAS REINHARDTII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHLOROPLAST THIOREDOXIN M CH2;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE 3 ORGANISM_TAXID: 3055;
SOURCE 4 ORGANELLE: CHLOROPLAST;
SOURCE 5 GENE: NUCLEAR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET3
KEYWDS THIOREDOXIN M, THIOREDOXIN CH2, CHLOROPLASTIC THIOREDOXIN,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA SOLUTION NMR
NUMMDL 28
AUTHOR J.-M.LANCELIN,L.GUILHAUDIS,I.KRIMM,M.J.BLACKLEDGE,D.MARION
REVDAT 6 16-FEB-22 1DBY 1 REMARK SEQADV
REVDAT 5 24-FEB-09 1DBY 1 VERSN
REVDAT 4 01-APR-03 1DBY 1 JRNL
REVDAT 3 23-MAY-01 1DBY 1 REMARK DBREF SEQADV
REVDAT 2 09-OCT-00 1DBY 1 JRNL
REVDAT 1 08-NOV-99 1DBY 0
JRNL AUTH J.M.LANCELIN,L.GUILHAUDIS,I.KRIMM,M.J.BLACKLEDGE,D.MARION,
JRNL AUTH 2 J.P.JACQUOT
JRNL TITL NMR STRUCTURES OF THIOREDOXIN M FROM THE GREEN ALGA
JRNL TITL 2 CHLAMYDOMONAS REINHARDTII.
JRNL REF PROTEINS V. 41 334 2000
JRNL REFN ISSN 0887-3585
JRNL PMID 11025545
JRNL DOI 10.1002/1097-0134(20001115)41:3<334::AID-PROT60>3.3.CO;2-D
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.-M.LANCELIN,M.STEIN,J.-P.JACQUOT
REMARK 1 TITL SECONDARY STRUCTURE AND PROTEIN FOLDING OF RECOMBINANT
REMARK 1 TITL 2 CHLOROPLASTIC THIOREDOXIN CH2 FROM THE GREEN ALGA
REMARK 1 TITL 3 CHLAMYDOMONAS REINHARDTII AS DETERMINED BY 1H NMR
REMARK 1 REF J.BIOCHEM.(TOKYO) V. 114 421 1993
REMARK 1 REFN ISSN 0021-924X
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.STEIN,J.-P.JACQUOT,E.JEANNETTE,P.DECOTTIGNIES,M.HODGES,
REMARK 1 AUTH 2 J.-M.LANCELIN,V.MITTARD,J.M.SCHMITTER,M.MIGINIAC-MASLOW
REMARK 1 TITL CHLAMYDOMONAS REINHARDTII THIOREDOXINS: STRUCTURE OF THE
REMARK 1 TITL 2 GENES CODING FOR CHLOROPLASTIC M AND CYTOSOLIC H ISOFORMS;
REMARK 1 TITL 3 EXPRESSION IN ESCHERICHIA COLI OF THE RECOMBINANT PROTEINS,
REMARK 1 TITL 4 PURIFICATION AND BIOCHEMICAL PROPERTIES
REMARK 1 REF PLANT MOL.BIOL. V. 28 487 1995
REMARK 1 REFN ISSN 0167-4412
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.-P.JACQUOT,M.STEIN,M.HODGES,M.MIGINIAC-MASLOW
REMARK 1 TITL PCR CLONING OF A NUCLEOTIDIC SEQUENCE CODING FOR THE MATURE
REMARK 1 TITL 2 PART OF CHLAMYDOMONAS REINHARDTII THIOREDOXIN CH2
REMARK 1 REF NUCLEIC ACIDS RES. V. 20 617 1992
REMARK 1 REFN ISSN 0305-1048
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.0, DISCOVER 2.3.0
REMARK 3 AUTHORS : BRUKER SPECTROSPIN AG (XWINNMR), BIOSYM
REMARK 3 TECHNOLOGIES (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON 1372 TOTAL INTERPROTON DISTANCE
REMARK 3 RESTRAINTS, 1348
REMARK 3 ARE DERIVED FROM NOE DATA AND 44 DERIVED FROM SLOW DEUTERIUM
REMARK 3 EXCHANGE
REMARK 3 EXPERIMENTS OF HYDROGEN BONDED AMIDE PROTONS IN REGULAR SECONDARY
REMARK 3 STRUCTURE
REMARK 3 MOTIFS. THE RESTRAINT SET INCLUDES 102 DIHEDRAL RESTRAINTS, 66 PHI,
REMARK 3 34 KHI1, 2
REMARK 3 KHI2. FINAL STRUCTURES ARE REFINED AGAINST THE FULL DESCRIPTION OF
REMARK 3 AMBER4
REMARK 3 FORCE FIELD WITH REDUCED CHARGES FOR FORMALLY CHARGED GROUPS AS
REMARK 3 ARG, LYS, ASP,
REMARK 3 GLU RESIDUES.
REMARK 4
REMARK 4 1DBY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1000009956.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 311
REMARK 210 PH : 5.8
REMARK 210 IONIC STRENGTH : 100 MM POTASSIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2-3 MM THIOREDOXIN M (OXIDIZED)
REMARK 210 U-15N; 100 MM POTASSIUM
REMARK 210 PHOSPHATE BUFFER PH 5.8; 90% H2O
REMARK 210 10% D20; 2-3 MM THIOREDOXIN M
REMARK 210 (OXIDIZED);100 MM POTASSIUM
REMARK 210 PHOSPHATE BUFFER PH 5.8; 90% H2O
REMARK 210 10% D20; 2-3 MM THIOREDOXIN M
REMARK 210 (OXIDIZED);100 MM POTASSIUM
REMARK 210 PHOSPHATE BUFFER PH 5.8; 100% D20
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D
REMARK 210 -SEPARATED-TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2.3, NMRPIPE 1.7, DISCOVER
REMARK 210 2.3.0, UXNMR 940501.3, GIFA 4.0
REMARK 210 METHOD USED : SIMULATED ANNEALING STARTING
REMARK 210 FROM A RANDOM ARRAY OF ATOMS.
REMARK 210 HIGH TEMPERATURE SIMULATED
REMARK 210 ANNEALING. RESTRAINED MOLECULAR
REMARK 210 DYNAMIC AT ROOM TEMPERATURE.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 28
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY. STRUCTURES
REMARK 210 WITH FAVORABLE NON- BOND ENERGY.
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS. STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY.
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 16
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE WAS DETERMINED USING 2D HOMONUCLEAR IN H20 AND 100%
REMARK 210 D2O AND 3D-
REMARK 210 15N SEPARATED NOESY AND TOCSY DATA.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 8 CYS A 34 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 16 CYS A 34 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 18 ILE A 77 C - N - CA ANGL. DEV. = 18.9 DEGREES
REMARK 500 18 ILE A 77 CB - CA - C ANGL. DEV. = -14.1 DEGREES
REMARK 500 18 ILE A 77 N - CA - CB ANGL. DEV. = -17.8 DEGREES
REMARK 500 18 ILE A 77 N - CA - C ANGL. DEV. = 28.0 DEGREES
REMARK 500 21 LYS A 53 N - CA - C ANGL. DEV. = 16.7 DEGREES
REMARK 500 25 CYS A 34 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 27 LYS A 53 N - CA - C ANGL. DEV. = 16.6 DEGREES
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 VAL A 15 -74.82 -115.46
REMARK 500 1 ASP A 50 -55.10 68.51
REMARK 500 1 ASN A 64 -73.64 -30.07
REMARK 500 1 ARG A 72 -64.23 -149.35
REMARK 500 1 CYS A 86 -58.18 -126.96
REMARK 500 1 LEU A 106 -97.09 -92.09
REMARK 500 2 ASP A 9 -74.08 -62.57
REMARK 500 2 VAL A 15 -72.43 -115.95
REMARK 500 2 TYR A 48 33.19 -97.25
REMARK 500 2 ASP A 50 -58.55 71.90
REMARK 500 2 SER A 73 166.19 94.31
REMARK 500 2 CYS A 86 -66.23 -129.61
REMARK 500 3 ALA A 3 92.07 -62.84
REMARK 500 3 ASP A 9 -72.22 -57.34
REMARK 500 3 VAL A 15 -51.64 -126.60
REMARK 500 3 ASP A 50 -53.71 73.82
REMARK 500 3 ASN A 64 -71.66 -51.83
REMARK 500 3 SER A 73 172.82 101.60
REMARK 500 3 LYS A 81 33.94 -145.42
REMARK 500 4 LYS A 12 -70.44 -42.62
REMARK 500 4 VAL A 15 -65.50 -104.17
REMARK 500 4 GLU A 17 41.39 -79.49
REMARK 500 4 SER A 19 -71.65 -97.18
REMARK 500 4 ARG A 72 -58.39 -154.25
REMARK 500 4 LYS A 81 42.62 -146.42
REMARK 500 4 CYS A 86 -70.29 -88.38
REMARK 500 4 LEU A 106 -95.44 -118.11
REMARK 500 5 GLU A 2 -67.26 72.08
REMARK 500 5 VAL A 15 -66.26 -98.61
REMARK 500 5 GLU A 17 40.55 -78.87
REMARK 500 5 SER A 19 -66.14 -131.58
REMARK 500 5 ASP A 50 -61.81 72.77
REMARK 500 5 SER A 62 52.28 -119.84
REMARK 500 5 CYS A 86 -80.28 -148.83
REMARK 500 5 ALA A 92 -46.57 71.53
REMARK 500 5 LEU A 106 -107.10 -95.44
REMARK 500 6 ASP A 9 -74.14 -66.09
REMARK 500 6 GLU A 17 45.53 -79.39
REMARK 500 6 SER A 19 -68.62 -104.98
REMARK 500 6 SER A 62 51.29 -117.33
REMARK 500 6 LYS A 81 -161.00 -162.28
REMARK 500 6 CYS A 86 -69.15 -103.59
REMARK 500 6 TYR A 105 -77.00 -105.46
REMARK 500 6 LEU A 106 -58.91 67.62
REMARK 500 7 VAL A 15 -64.56 -109.95
REMARK 500 7 LEU A 16 -71.05 -69.23
REMARK 500 7 SER A 18 -129.60 -90.80
REMARK 500 7 SER A 19 -78.04 -161.54
REMARK 500 7 ALA A 28 142.07 -171.53
REMARK 500 7 TRP A 30 -29.96 137.85
REMARK 500
REMARK 500 THIS ENTRY HAS 209 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 1 TYR A 48 0.16 SIDE CHAIN
REMARK 500 2 ARG A 35 0.13 SIDE CHAIN
REMARK 500 3 PHE A 26 0.11 SIDE CHAIN
REMARK 500 3 TYR A 48 0.07 SIDE CHAIN
REMARK 500 3 TYR A 69 0.10 SIDE CHAIN
REMARK 500 4 TYR A 105 0.11 SIDE CHAIN
REMARK 500 5 TYR A 48 0.10 SIDE CHAIN
REMARK 500 5 TYR A 69 0.11 SIDE CHAIN
REMARK 500 6 TYR A 105 0.11 SIDE CHAIN
REMARK 500 7 TYR A 48 0.07 SIDE CHAIN
REMARK 500 8 TYR A 69 0.10 SIDE CHAIN
REMARK 500 8 TYR A 105 0.09 SIDE CHAIN
REMARK 500 9 TYR A 105 0.09 SIDE CHAIN
REMARK 500 10 TYR A 69 0.09 SIDE CHAIN
REMARK 500 11 TYR A 48 0.13 SIDE CHAIN
REMARK 500 12 TYR A 105 0.09 SIDE CHAIN
REMARK 500 14 TYR A 48 0.10 SIDE CHAIN
REMARK 500 14 TYR A 69 0.08 SIDE CHAIN
REMARK 500 15 TYR A 48 0.07 SIDE CHAIN
REMARK 500 15 TYR A 69 0.10 SIDE CHAIN
REMARK 500 16 TYR A 105 0.14 SIDE CHAIN
REMARK 500 17 TYR A 48 0.09 SIDE CHAIN
REMARK 500 17 TYR A 69 0.09 SIDE CHAIN
REMARK 500 19 TYR A 48 0.15 SIDE CHAIN
REMARK 500 19 TYR A 69 0.09 SIDE CHAIN
REMARK 500 20 TYR A 69 0.12 SIDE CHAIN
REMARK 500 20 TYR A 105 0.10 SIDE CHAIN
REMARK 500 21 TYR A 69 0.07 SIDE CHAIN
REMARK 500 22 TYR A 69 0.09 SIDE CHAIN
REMARK 500 23 TYR A 48 0.13 SIDE CHAIN
REMARK 500 23 TYR A 69 0.11 SIDE CHAIN
REMARK 500 24 TYR A 48 0.09 SIDE CHAIN
REMARK 500 24 TYR A 69 0.07 SIDE CHAIN
REMARK 500 24 TYR A 105 0.09 SIDE CHAIN
REMARK 500 25 TYR A 69 0.11 SIDE CHAIN
REMARK 500 26 TYR A 48 0.17 SIDE CHAIN
REMARK 500 26 TYR A 69 0.08 SIDE CHAIN
REMARK 500 27 TYR A 69 0.12 SIDE CHAIN
REMARK 500 28 TYR A 48 0.09 SIDE CHAIN
REMARK 500 28 TYR A 69 0.09 SIDE CHAIN
REMARK 500 28 TYR A 105 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TOF RELATED DB: PDB
DBREF 1DBY A 1 107 UNP P23400 TRXM_CHLRE 1 107
SEQADV 1DBY MET A 1 UNP P23400 CLONING ARTIFACT
SEQRES 1 A 107 MET GLU ALA GLY ALA VAL ASN ASP ASP THR PHE LYS ASN
SEQRES 2 A 107 VAL VAL LEU GLU SER SER VAL PRO VAL LEU VAL ASP PHE
SEQRES 3 A 107 TRP ALA PRO TRP CYS GLY PRO CYS ARG ILE ILE ALA PRO
SEQRES 4 A 107 VAL VAL ASP GLU ILE ALA GLY GLU TYR LYS ASP LYS LEU
SEQRES 5 A 107 LYS CYS VAL LYS LEU ASN THR ASP GLU SER PRO ASN VAL
SEQRES 6 A 107 ALA SER GLU TYR GLY ILE ARG SER ILE PRO THR ILE MET
SEQRES 7 A 107 VAL PHE LYS GLY GLY LYS LYS CYS GLU THR ILE ILE GLY
SEQRES 8 A 107 ALA VAL PRO LYS ALA THR ILE VAL GLN THR VAL GLU LYS
SEQRES 9 A 107 TYR LEU ASN
HELIX 1 1 ASN A 7 VAL A 15 1 9
HELIX 2 2 CYS A 31 TYR A 48 1 18
HELIX 3 3 SER A 62 GLY A 70 1 9
HELIX 4 4 PRO A 94 LEU A 106 1 13
SHEET 1 A 5 GLY A 4 VAL A 6 0
SHEET 2 A 5 LYS A 53 ASN A 58 1 O CYS A 54 N GLY A 4
SHEET 3 A 5 VAL A 22 TRP A 27 1 O LEU A 23 N VAL A 55
SHEET 4 A 5 THR A 76 PHE A 80 -1 O THR A 76 N PHE A 26
SHEET 5 A 5 LYS A 85 ILE A 90 -1 N CYS A 86 O VAL A 79
SSBOND 1 CYS A 31 CYS A 34 1555 1555 2.08
CISPEP 1 ILE A 74 PRO A 75 1 3.24
CISPEP 2 ILE A 74 PRO A 75 2 1.32
CISPEP 3 ILE A 74 PRO A 75 3 2.21
CISPEP 4 ILE A 74 PRO A 75 4 1.56
CISPEP 5 ILE A 74 PRO A 75 5 1.82
CISPEP 6 ILE A 74 PRO A 75 6 3.16
CISPEP 7 ILE A 74 PRO A 75 7 2.56
CISPEP 8 ILE A 74 PRO A 75 8 2.44
CISPEP 9 ILE A 74 PRO A 75 9 1.61
CISPEP 10 ILE A 74 PRO A 75 10 1.88
CISPEP 11 ILE A 74 PRO A 75 11 2.35
CISPEP 12 ILE A 74 PRO A 75 12 3.05
CISPEP 13 ILE A 74 PRO A 75 13 1.57
CISPEP 14 ILE A 74 PRO A 75 14 1.54
CISPEP 15 ILE A 74 PRO A 75 15 0.50
CISPEP 16 ILE A 74 PRO A 75 16 3.91
CISPEP 17 ILE A 74 PRO A 75 17 1.25
CISPEP 18 ILE A 74 PRO A 75 18 2.09
CISPEP 19 ILE A 74 PRO A 75 19 3.99
CISPEP 20 ILE A 74 PRO A 75 20 2.20
CISPEP 21 ILE A 74 PRO A 75 21 4.46
CISPEP 22 ILE A 74 PRO A 75 22 1.05
CISPEP 23 ILE A 74 PRO A 75 23 2.14
CISPEP 24 ILE A 74 PRO A 75 24 1.05
CISPEP 25 ILE A 74 PRO A 75 25 1.52
CISPEP 26 ILE A 74 PRO A 75 26 2.51
CISPEP 27 ILE A 74 PRO A 75 27 2.43
CISPEP 28 ILE A 74 PRO A 75 28 3.00
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