Header list of 1c89.pdb file
Complete list - b 16 2 Bytes
HEADER ANTIFREEZE PROTEIN 04-MAY-00 1C89
TITLE NMR STRUCTURE OF INTRAMOLECULAR DIMER ANTIFREEZE PROTEIN RD3, 40 SA
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIFREEZE PROTEIN TYPE III;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RD3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PACHYCARA BRACHYCEPHALUM;
SOURCE 3 ORGANISM_TAXID: 36221;
SOURCE 4 VARIANT: RD3;
SOURCE 5 TISSUE: BLOOD PLASMA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM105;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PKK223-3UC;
SOURCE 12 OTHER_DETAILS: SYNTHETIC GENE
KEYWDS ANTIFREEZE, THERMAL HYSTERESIS PROTEIN, ICE BINDING PROTEIN,
KEYWDS 2 ANTIFREEZE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR K.MIURA,S.TSUDA
REVDAT 3 16-FEB-22 1C89 1 REMARK
REVDAT 2 24-FEB-09 1C89 1 VERSN
REVDAT 1 28-FEB-01 1C89 0
JRNL AUTH K.MIURA,S.OHGIYA,T.HOSHINO,N.NEMOTO,T.SUETAKE,A.MIURA,
JRNL AUTH 2 L.SPYRACOPOULOS,H.KONDO,S.TSUDA
JRNL TITL NMR ANALYSIS OF TYPE III ANTIFREEZE PROTEIN INTRAMOLECULAR
JRNL TITL 2 DIMER. STRUCTURAL BASIS FOR ENHANCED ACTIVITY.
JRNL REF J.BIOL.CHEM. V. 276 1304 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11010977
JRNL DOI 10.1074/JBC.M007902200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.MIURA,S.OHGIYA,T.HOSHINO,N.NEMOTO,M.ODAIRA,K.NITTA,S.TSUDA
REMARK 1 TITL DETERMINATION OF THE SOLUTION STRUCTURE OF THE N-DOMAIN PLUS
REMARK 1 TITL 2 LINKER OF ANTARCTIC EEL POUT ANTIFREEZE PROTEIN RD3
REMARK 1 REF J.BIOCHEM.(TOKYO) V. 126 387 1999
REMARK 1 REFN ISSN 0021-924X
REMARK 1 REFERENCE 2
REMARK 1 AUTH Z.JIA,C.I.DELUCA,H.CHAO,P.L.DAVIES
REMARK 1 TITL STRUCTURAL BASIS FOR THE BINDING OF A GLOBULAR ANTIFREEZE
REMARK 1 TITL 2 PROTEIN TO ICE
REMARK 1 REF NATURE V. 384 285 1996
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/384285A0
REMARK 1 REFERENCE 3
REMARK 1 AUTH F.D.SONNICHSEN,C.I.DELUCA,P.L.DAVIES,B.D.SYKES
REMARK 1 TITL REFINED SOLUTION STRUCTURE OF TYPE III ANTIFREEZE PROTEIN:
REMARK 1 TITL 2 HYDROPHOBIC GROUPS MAY BE INVOLVED IN THE ENERGETICS OF THE
REMARK 1 TITL 3 PROTEIN-ICE INTERACTION
REMARK 1 REF STRUCTURE V. 4 1325 1996
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 4
REMARK 1 AUTH X.WANG,A.L.DEVRIES,C.H.CHENG
REMARK 1 TITL ANTIFREEZE PEPTIDE HETEROGENEITY IN AN ANTARCTIC EEL POUT
REMARK 1 TITL 2 INCLUDES AN UNUSUALLY LARGE MAJOR VARIANT COMPRISED OF TWO 7
REMARK 1 TITL 3 KDA TYPE III AFPS LINKED IN TANDEM
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V.1247 163 1995
REMARK 1 REFN ISSN 0006-3002
REMARK 1 DOI 10.1016/0167-4838(94)00205-U
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1C89 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-00.
REMARK 100 THE DEPOSITION ID IS D_1000001458.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 277
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; 15N-1H HSQC; 13C-1H HSQC
REMARK 210 15N-TOCSYHSQC; 15N-NOESYHSQC;
REMARK 210 15N-HNHA; HNCA; HNCACB; CBCA(CO)
REMARK 210 NH; C(CO)NH; HC(CO)NH; HCCH-
REMARK 210 TOCSY; MOTHER-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851
REMARK 210 METHOD USED : SA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40
REMARK 210 CONFORMERS, SELECTION CRITERIA : AVERAGE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 40
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C/15N-LABELED RD3
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: 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 O ILE A 11 H VAL A 49 1.45
REMARK 500 O PRO A 82 HG1 THR A 85 1.54
REMARK 500 O GLU A 36 H ASN A 39 1.57
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 PRO A 12 -162.05 -75.32
REMARK 500 1 VAL A 41 151.70 -46.57
REMARK 500 1 LYS A 61 -103.12 -62.81
REMARK 500 1 GLU A 64 163.76 169.31
REMARK 500 1 THR A 68 -73.40 -106.25
REMARK 500 1 PRO A 70 -90.69 -72.26
REMARK 500 1 ILE A 83 158.56 -42.01
REMARK 500 1 ASN A 84 75.76 41.92
REMARK 500 1 ALA A 86 85.95 -54.59
REMARK 500 1 LEU A 121 -148.38 -59.06
REMARK 500 1 ASP A 122 88.23 -43.99
REMARK 500 1 LYS A 131 -131.99 -81.98
REMARK 500 1 TYR A 133 -167.75 -68.37
REMARK 500 2 PRO A 12 -159.95 -73.53
REMARK 500 2 ASN A 14 71.96 44.37
REMARK 500 2 ALA A 16 89.17 -64.66
REMARK 500 2 GLU A 36 56.79 -92.83
REMARK 500 2 PRO A 50 -168.59 -72.23
REMARK 500 2 LYS A 61 -130.85 -65.64
REMARK 500 2 TYR A 63 -94.55 -53.62
REMARK 500 2 GLU A 64 -159.97 -121.81
REMARK 500 2 THR A 68 -140.09 -85.23
REMARK 500 2 PRO A 70 -94.40 -72.19
REMARK 500 2 ILE A 83 152.13 -45.22
REMARK 500 2 ASN A 84 71.02 50.98
REMARK 500 2 ALA A 86 98.82 -52.07
REMARK 500 2 LEU A 121 -149.41 -58.99
REMARK 500 2 ASP A 122 85.05 -44.71
REMARK 500 2 ASN A 132 45.53 -94.08
REMARK 500 3 PRO A 12 -159.61 -73.60
REMARK 500 3 GLU A 36 32.63 -94.82
REMARK 500 3 VAL A 41 151.54 -46.24
REMARK 500 3 LYS A 61 -135.65 -70.53
REMARK 500 3 TYR A 63 -102.01 -53.69
REMARK 500 3 GLU A 64 -148.60 -130.10
REMARK 500 3 ASP A 65 36.61 -86.40
REMARK 500 3 THR A 67 -155.99 -82.37
REMARK 500 3 THR A 68 -127.60 -97.52
REMARK 500 3 PRO A 70 -150.13 -71.89
REMARK 500 3 GLN A 79 -169.36 -110.39
REMARK 500 3 ASN A 84 72.80 63.16
REMARK 500 3 ALA A 86 83.63 -55.06
REMARK 500 3 GLU A 96 98.82 -69.40
REMARK 500 3 LEU A 121 -144.54 -59.34
REMARK 500 3 ASP A 122 87.02 -44.29
REMARK 500 4 PRO A 12 -159.78 -73.43
REMARK 500 4 ASN A 14 74.92 44.19
REMARK 500 4 MET A 30 85.60 -68.23
REMARK 500 4 GLU A 36 30.43 -94.47
REMARK 500 4 PRO A 50 -169.36 -70.86
REMARK 500
REMARK 500 THIS ENTRY HAS 625 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 ARG A 47 0.32 SIDE CHAIN
REMARK 500 1 ARG A 117 0.29 SIDE CHAIN
REMARK 500 2 ARG A 47 0.31 SIDE CHAIN
REMARK 500 2 ARG A 117 0.17 SIDE CHAIN
REMARK 500 3 ARG A 47 0.32 SIDE CHAIN
REMARK 500 3 ARG A 117 0.21 SIDE CHAIN
REMARK 500 4 ARG A 47 0.26 SIDE CHAIN
REMARK 500 4 ARG A 117 0.17 SIDE CHAIN
REMARK 500 5 ARG A 47 0.31 SIDE CHAIN
REMARK 500 5 ARG A 117 0.31 SIDE CHAIN
REMARK 500 6 ARG A 47 0.13 SIDE CHAIN
REMARK 500 6 ARG A 117 0.23 SIDE CHAIN
REMARK 500 7 ARG A 47 0.24 SIDE CHAIN
REMARK 500 7 ARG A 117 0.26 SIDE CHAIN
REMARK 500 8 ARG A 47 0.13 SIDE CHAIN
REMARK 500 8 ARG A 117 0.23 SIDE CHAIN
REMARK 500 9 ARG A 47 0.20 SIDE CHAIN
REMARK 500 9 ARG A 117 0.28 SIDE CHAIN
REMARK 500 10 ARG A 47 0.31 SIDE CHAIN
REMARK 500 10 ARG A 117 0.19 SIDE CHAIN
REMARK 500 11 ARG A 47 0.21 SIDE CHAIN
REMARK 500 11 ARG A 117 0.30 SIDE CHAIN
REMARK 500 12 ARG A 47 0.08 SIDE CHAIN
REMARK 500 12 ARG A 117 0.19 SIDE CHAIN
REMARK 500 13 ARG A 47 0.21 SIDE CHAIN
REMARK 500 13 ARG A 117 0.31 SIDE CHAIN
REMARK 500 14 ARG A 47 0.11 SIDE CHAIN
REMARK 500 14 ARG A 117 0.32 SIDE CHAIN
REMARK 500 15 ARG A 47 0.29 SIDE CHAIN
REMARK 500 15 ARG A 117 0.26 SIDE CHAIN
REMARK 500 16 ARG A 47 0.24 SIDE CHAIN
REMARK 500 16 ARG A 117 0.24 SIDE CHAIN
REMARK 500 17 ARG A 117 0.18 SIDE CHAIN
REMARK 500 18 ARG A 47 0.32 SIDE CHAIN
REMARK 500 18 ARG A 117 0.31 SIDE CHAIN
REMARK 500 19 ARG A 47 0.32 SIDE CHAIN
REMARK 500 19 ARG A 117 0.18 SIDE CHAIN
REMARK 500 20 ARG A 47 0.26 SIDE CHAIN
REMARK 500 20 ARG A 117 0.21 SIDE CHAIN
REMARK 500 21 ARG A 47 0.23 SIDE CHAIN
REMARK 500 21 ARG A 117 0.28 SIDE CHAIN
REMARK 500 22 ARG A 47 0.20 SIDE CHAIN
REMARK 500 22 ARG A 117 0.13 SIDE CHAIN
REMARK 500 23 ARG A 47 0.12 SIDE CHAIN
REMARK 500 23 ARG A 117 0.32 SIDE CHAIN
REMARK 500 24 ARG A 47 0.28 SIDE CHAIN
REMARK 500 24 ARG A 117 0.27 SIDE CHAIN
REMARK 500 25 ARG A 47 0.32 SIDE CHAIN
REMARK 500 25 ARG A 117 0.10 SIDE CHAIN
REMARK 500 26 ARG A 47 0.25 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 78 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ICE BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ICE BINDING SITE
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1C8A RELATED DB: PDB
REMARK 900 MINIMIZED AVERAGE STRUCTURE
DBREF 1C89 A 1 134 UNP P35753 ANP3_RHIDE 1 134
SEQRES 1 A 134 ASN LYS ALA SER VAL VAL ALA ASN GLN LEU ILE PRO ILE
SEQRES 2 A 134 ASN THR ALA LEU THR LEU ILE MET MET LYS ALA GLU VAL
SEQRES 3 A 134 VAL THR PRO MET GLY ILE PRO ALA GLU GLU ILE PRO ASN
SEQRES 4 A 134 LEU VAL GLY MET GLN VAL ASN ARG ALA VAL PRO LEU GLY
SEQRES 5 A 134 THR THR LEU MET PRO ASP MET VAL LYS ASN TYR GLU ASP
SEQRES 6 A 134 GLY THR THR SER PRO GLY LEU LYS SER VAL VAL ALA ASN
SEQRES 7 A 134 GLN LEU ILE PRO ILE ASN THR ALA LEU THR LEU VAL MET
SEQRES 8 A 134 MET LYS ALA GLU GLU VAL SER PRO LYS GLY ILE PRO SER
SEQRES 9 A 134 GLU GLU ILE SER LYS LEU VAL GLY MET GLN VAL ASN ARG
SEQRES 10 A 134 ALA VAL TYR LEU ASP GLN THR LEU MET PRO ASP MET VAL
SEQRES 11 A 134 LYS ASN TYR GLU
HELIX 1 1 GLU A 36 VAL A 41 1 6
HELIX 2 2 GLU A 106 VAL A 111 1 6
SHEET 1 A 3 MET A 22 GLU A 25 0
SHEET 2 A 3 SER A 4 ALA A 7 -1 N SER A 4 O GLU A 25
SHEET 3 A 3 THR A 53 THR A 54 -1 O THR A 53 N ALA A 7
SHEET 1 B 3 LYS A 93 GLU A 96 0
SHEET 2 B 3 LYS A 73 ALA A 77 -1 N SER A 74 O GLU A 95
SHEET 3 B 3 GLN A 123 THR A 124 -1 O GLN A 123 N ALA A 77
CISPEP 1 THR A 28 PRO A 29 1 -0.22
CISPEP 2 SER A 98 PRO A 99 1 -0.21
CISPEP 3 THR A 28 PRO A 29 2 -0.16
CISPEP 4 SER A 98 PRO A 99 2 -0.35
CISPEP 5 THR A 28 PRO A 29 3 -0.10
CISPEP 6 SER A 98 PRO A 99 3 -0.29
CISPEP 7 THR A 28 PRO A 29 4 0.01
CISPEP 8 SER A 98 PRO A 99 4 -0.46
CISPEP 9 THR A 28 PRO A 29 5 -0.08
CISPEP 10 SER A 98 PRO A 99 5 -0.33
CISPEP 11 THR A 28 PRO A 29 6 -0.18
CISPEP 12 SER A 98 PRO A 99 6 -0.44
CISPEP 13 THR A 28 PRO A 29 7 -0.30
CISPEP 14 SER A 98 PRO A 99 7 -0.31
CISPEP 15 THR A 28 PRO A 29 8 -0.02
CISPEP 16 SER A 98 PRO A 99 8 -0.34
CISPEP 17 THR A 28 PRO A 29 9 -0.22
CISPEP 18 SER A 98 PRO A 99 9 -0.21
CISPEP 19 THR A 28 PRO A 29 10 -0.22
CISPEP 20 SER A 98 PRO A 99 10 -0.14
CISPEP 21 THR A 28 PRO A 29 11 -0.26
CISPEP 22 SER A 98 PRO A 99 11 -0.20
CISPEP 23 THR A 28 PRO A 29 12 -0.12
CISPEP 24 SER A 98 PRO A 99 12 -0.10
CISPEP 25 THR A 28 PRO A 29 13 -0.29
CISPEP 26 SER A 98 PRO A 99 13 -0.26
CISPEP 27 THR A 28 PRO A 29 14 -0.22
CISPEP 28 SER A 98 PRO A 99 14 -0.59
CISPEP 29 THR A 28 PRO A 29 15 -0.16
CISPEP 30 SER A 98 PRO A 99 15 -0.17
CISPEP 31 THR A 28 PRO A 29 16 -0.10
CISPEP 32 SER A 98 PRO A 99 16 -0.32
CISPEP 33 THR A 28 PRO A 29 17 -0.25
CISPEP 34 SER A 98 PRO A 99 17 -0.40
CISPEP 35 THR A 28 PRO A 29 18 -0.01
CISPEP 36 SER A 98 PRO A 99 18 -0.34
CISPEP 37 THR A 28 PRO A 29 19 -0.13
CISPEP 38 SER A 98 PRO A 99 19 -0.26
CISPEP 39 THR A 28 PRO A 29 20 -0.17
CISPEP 40 SER A 98 PRO A 99 20 -0.17
CISPEP 41 THR A 28 PRO A 29 21 -0.23
CISPEP 42 SER A 98 PRO A 99 21 -0.29
CISPEP 43 THR A 28 PRO A 29 22 0.03
CISPEP 44 SER A 98 PRO A 99 22 -0.07
CISPEP 45 THR A 28 PRO A 29 23 -0.12
CISPEP 46 SER A 98 PRO A 99 23 -0.40
CISPEP 47 THR A 28 PRO A 29 24 -0.19
CISPEP 48 SER A 98 PRO A 99 24 -0.18
CISPEP 49 THR A 28 PRO A 29 25 -0.10
CISPEP 50 SER A 98 PRO A 99 25 -0.14
CISPEP 51 THR A 28 PRO A 29 26 -0.07
CISPEP 52 SER A 98 PRO A 99 26 -0.04
CISPEP 53 THR A 28 PRO A 29 27 -0.41
CISPEP 54 SER A 98 PRO A 99 27 -0.41
CISPEP 55 THR A 28 PRO A 29 28 -0.17
CISPEP 56 SER A 98 PRO A 99 28 -0.40
CISPEP 57 THR A 28 PRO A 29 29 -0.35
CISPEP 58 SER A 98 PRO A 99 29 -0.26
CISPEP 59 THR A 28 PRO A 29 30 -0.03
CISPEP 60 SER A 98 PRO A 99 30 -0.38
CISPEP 61 THR A 28 PRO A 29 31 -0.21
CISPEP 62 SER A 98 PRO A 99 31 -0.42
CISPEP 63 THR A 28 PRO A 29 32 -0.08
CISPEP 64 SER A 98 PRO A 99 32 -0.35
CISPEP 65 THR A 28 PRO A 29 33 -0.14
CISPEP 66 SER A 98 PRO A 99 33 -0.14
CISPEP 67 THR A 28 PRO A 29 34 -0.16
CISPEP 68 SER A 98 PRO A 99 34 -0.17
CISPEP 69 THR A 28 PRO A 29 35 -0.30
CISPEP 70 SER A 98 PRO A 99 35 -0.20
CISPEP 71 THR A 28 PRO A 29 36 -0.19
CISPEP 72 SER A 98 PRO A 99 36 -0.23
CISPEP 73 THR A 28 PRO A 29 37 -0.17
CISPEP 74 SER A 98 PRO A 99 37 -0.38
CISPEP 75 THR A 28 PRO A 29 38 -0.25
CISPEP 76 SER A 98 PRO A 99 38 -0.37
CISPEP 77 THR A 28 PRO A 29 39 -0.15
CISPEP 78 SER A 98 PRO A 99 39 -0.24
CISPEP 79 THR A 28 PRO A 29 40 -0.21
CISPEP 80 SER A 98 PRO A 99 40 -0.31
SITE 1 IC1 6 GLN A 9 ASN A 14 THR A 15 ALA A 16
SITE 2 IC1 6 THR A 18 GLN A 44
SITE 1 IC2 6 GLN A 79 ASN A 84 THR A 85 ALA A 86
SITE 2 IC2 6 THR A 88 GLN A 114
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