Header list of 2eu0.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSFERASE 27-OCT-05 2EU0
TITLE THE NMR ENSEMBLE STRUCTURE OF THE ITK SH2 DOMAIN BOUND TO A
TITLE 2 PHOSPHOPEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE ITK/TSK;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH2 DOMAIN;
COMPND 5 SYNONYM: T-CELL-SPECIFIC KINASE, IL-2-INDUCIBLE T-CELL KINASE, KINASE
COMPND 6 EMT, KINASE TLK, ITK;
COMPND 7 EC: 2.7.1.112;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: LYMPHOCYTE CYTOSOLIC PROTEIN 2 PHOSPHOPEPTIDE FRAGMENT;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: PHOSPHOPEPTIDE FRAGMENT, SEQUENCE DATABASE RESIDUES 143-
COMPND 13 148;
COMPND 14 SYNONYM: SH2 DOMAIN-CONTAINING LEUCOCYTE PROTEIN OF 76 KDA, SLP-76
COMPND 15 TYROSINE PHOSPHOPROTEIN, SLP76;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ITK, EMT, TLK, TSK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX(2T);
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN MUS MUSCULUS
SOURCE 14 (MOUSE)
KEYWDS CIS/TRANS ISOMERIZATION, INTERLEUKIN-2 TYROSINE KINASE, ITK, T-CELL
KEYWDS 2 SPECIFIC KINASE, TSK, SRC HOMOLOGY 2, SH2, PROLINE, PHOSPHOTYROSINE
KEYWDS 3 BINDING, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.SUNDD,E.V.PLETNEVA,D.B.FULTON,A.H.ANDREOTTI
REVDAT 5 09-MAR-22 2EU0 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 2EU0 1 VERSN
REVDAT 3 21-MAR-06 2EU0 1 JRNL
REVDAT 2 14-FEB-06 2EU0 1 AUTHOR
REVDAT 1 07-FEB-06 2EU0 0
JRNL AUTH E.V.PLETNEVA,M.SUNDD,D.B.FULTON,A.H.ANDREOTTI
JRNL TITL MOLECULAR DETAILS OF ITK ACTIVATION BY PROLYL ISOMERIZATION
JRNL TITL 2 AND PHOSPHOLIGAND BINDING: THE NMR STRUCTURE OF THE ITK SH2
JRNL TITL 3 DOMAIN BOUND TO A PHOSPHOPEPTIDE.
JRNL REF J.MOL.BIOL. V. 357 550 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16436281
JRNL DOI 10.1016/J.JMB.2005.12.073
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.J.MALLIS,K.N.BRAZIN,D.B.FULTON,A.H.ANDREOTTI
REMARK 1 TITL STRUCTURAL CHARACTERIZATION OF A PROLINE-DRIVEN
REMARK 1 TITL 2 CONFORMATIONAL SWITCH WITHIN THE ITK SH2 DOMAIN
REMARK 1 REF NAT.STRUCT.BIOL. V. 9 900 2002
REMARK 1 REFN ISSN 1072-8368
REMARK 1 PMID 12402030
REMARK 1 DOI 10.1038/NSB864
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, CNS 1.0
REMARK 3 AUTHORS : BRUNGER ET AL (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 2486 INTRAMOLECULAR NOE RESTRAINTS, 31
REMARK 3 INTERMOLECULAR NOE RESTRAINTS, 63 DIHEDRAL ANGLES CALCULATED
REMARK 3 USING HNHA EXPERIMENT AND TALOS AND 27 HYDROGEN BONDS (D20
REMARK 3 EXCHANGE BASED RESTRAINTS)
REMARK 4
REMARK 4 2EU0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000035090.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 125MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM ITK SH2 DOMAIN, 20MM
REMARK 210 PHOSPHOPEPTIDE, 50MM KH2PO4,
REMARK 210 75MM NACL, 2MM DTT, 0.02% NAN3,
REMARK 210 PH 7.4; U-15N LABELED, 1MM ITK
REMARK 210 SH2 DOMAIN, 20MM PHOSPHOPEPTIDE,
REMARK 210 50MM KH2PO4, 75MM NACL, 2MM DTT,
REMARK 210 0.02% NAN3, PH 7.4; U-15N, 13-C
REMARK 210 LABELED, 1MM ITK SH2 DOMAIN,
REMARK 210 20MM PHOSPHOPEPTIDE, 50MM KH2PO4,
REMARK 210 75MM NACL, 2MM DTT, 0.02% NAN3,
REMARK 210 PH 7.4; 5MM PHOSPHOPEPTIDE, 50MM
REMARK 210 KH2PO4, 75MM NACL, 2MM DTT, 0.02%
REMARK 210 NAN3, PH 7.4; 1MM ITK SH2
REMARK 210 DOMAIN, 20MM PHOSPHOPEPTIDE,
REMARK 210 50MM KH2PO4, 75MM NACL, 2MM DTT,
REMARK 210 0.02% NAN3, PH 7.4
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; 3D_13C-
REMARK 210 SEPARATED_NOESY; 3D_13C_
REMARK 210 SEPARATED_AROMATIC_NOESY; HNCACB;
REMARK 210 CBCA(CO)NH; HCCH_TOCSY; CCONH;
REMARK 210 13C EDITED_13C/15_N FILTERED
REMARK 210 NOESY; 15N_EDITED_13C/15N_
REMARK 210 FILTERED NOESY; 2D TOCSY; D2O
REMARK 210 EXCHANGE EXPERIMENT
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 4.1.3
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING WAS USED FOR REFINEMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 HD1 TRP A 11 HB3 PRO A 108 1.17
REMARK 500 O TYR A 45 H ILE A 66 1.26
REMARK 500 H PHE A 34 O TYR A 107 1.32
REMARK 500 O TRP A 11 H VAL A 36 1.34
REMARK 500 H TYR A 76 O PHE A 84 1.35
REMARK 500 O GLY A 32 H TYR A 107 1.38
REMARK 500 O ARG A 18 H GLU A 22 1.39
REMARK 500 O MET A 35 H SER A 48 1.39
REMARK 500 O TYR A 76 H PHE A 84 1.42
REMARK 500 O LEU A 101 H ARG A 104 1.45
REMARK 500 O PRO A 73 H ARG A 75 1.47
REMARK 500 H ARG A 37 O THR A 46 1.48
REMARK 500 HG1 THR A 69 O LYS A 74 1.48
REMARK 500 H LYS A 67 O TYR A 77 1.48
REMARK 500 O LYS A 67 H TYR A 77 1.51
REMARK 500 O LYS A 20 H LEU A 24 1.51
REMARK 500 O ALA A 33 H PHE A 50 1.52
REMARK 500 O ILE A 87 H ILE A 91 1.52
REMARK 500 O GLN A 92 H TYR A 96 1.52
REMARK 500 H VAL A 47 O TYR A 64 1.53
REMARK 500 O GLU A 22 H LEU A 26 1.53
REMARK 500 O ARG A 37 H THR A 46 1.54
REMARK 500 O PRO A 88 H GLN A 92 1.55
REMARK 500 O SER A 86 H LEU A 90 1.55
REMARK 500 O LEU A 89 H TYR A 93 1.56
REMARK 500 O VAL A 47 H TYR A 64 1.56
REMARK 500 O ALA A 21 H LEU A 25 1.56
REMARK 500 H VAL A 49 O LYS A 62 1.56
REMARK 500 O VAL A 49 H LYS A 62 1.58
REMARK 500 O LEU A 90 H HIS A 94 1.58
REMARK 500 O ASN A 4 H GLU A 7 1.58
REMARK 500 HD2 TYR A 77 O ALA A 79 1.60
REMARK 500 O HIS A 94 HB2 ARG A 104 1.60
REMARK 500 HG1 THR A 51 OG1 THR A 103 1.60
REMARK 500 OG SER A 39 O1P PTR B 121 2.10
REMARK 500 OG1 THR A 44 O ILE A 66 2.12
REMARK 500 O THR A 41 N GLY A 43 2.14
REMARK 500 OG1 THR A 69 O LYS A 74 2.16
REMARK 500 O GLU A 10 O PRO A 108 2.16
REMARK 500 OG1 THR A 51 OG1 THR A 103 2.16
REMARK 500 O MET A 35 N SER A 48 2.16
REMARK 500 O ASN A 4 N LEU A 6 2.17
REMARK 500 O TRP A 11 N VAL A 36 2.18
REMARK 500 O ALA A 33 N PHE A 50 2.19
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 ASN A 5 -39.30 -20.37
REMARK 500 1 GLU A 10 30.77 -77.08
REMARK 500 1 TRP A 11 -10.33 -149.14
REMARK 500 1 LYS A 14 -157.47 -44.34
REMARK 500 1 SER A 15 7.98 -65.31
REMARK 500 1 SER A 17 160.02 -38.47
REMARK 500 1 THR A 41 58.50 -100.89
REMARK 500 1 PRO A 42 66.63 -35.21
REMARK 500 1 ILE A 55 167.93 -34.50
REMARK 500 1 ASN A 58 165.66 101.09
REMARK 500 1 LYS A 74 63.49 -56.44
REMARK 500 1 ARG A 75 -60.24 -101.86
REMARK 500 1 ALA A 79 161.83 175.69
REMARK 500 1 LYS A 81 -20.44 165.29
REMARK 500 1 HIS A 94 2.31 -62.02
REMARK 500 1 GLN A 95 -37.16 -141.60
REMARK 500 1 VAL A 102 111.17 -5.17
REMARK 500 1 THR A 103 37.13 24.03
REMARK 500 1 ARG A 104 175.81 43.57
REMARK 500 1 ARG A 106 -73.83 -123.06
REMARK 500 1 CYS A 110 87.21 -44.84
REMARK 500 1 GLU B 122 76.02 11.53
REMARK 500 1 PRO B 123 88.74 -36.91
REMARK 500 2 ASN A 5 26.13 31.80
REMARK 500 2 GLU A 10 28.60 -77.45
REMARK 500 2 TRP A 11 -17.70 -152.59
REMARK 500 2 LYS A 14 -155.32 -45.01
REMARK 500 2 SER A 15 1.43 -55.12
REMARK 500 2 SER A 17 157.59 101.39
REMARK 500 2 ARG A 40 -24.40 -37.70
REMARK 500 2 THR A 41 59.22 -100.37
REMARK 500 2 PRO A 42 69.08 -33.96
REMARK 500 2 ILE A 54 -24.27 -37.72
REMARK 500 2 THR A 69 -158.12 -136.55
REMARK 500 2 ASP A 71 111.70 66.98
REMARK 500 2 VAL A 78 52.75 -113.19
REMARK 500 2 ALA A 79 161.22 176.14
REMARK 500 2 LYS A 81 -30.05 161.04
REMARK 500 2 GLN A 95 -40.98 -146.55
REMARK 500 2 LEU A 101 -164.80 -105.38
REMARK 500 2 THR A 103 33.19 28.34
REMARK 500 2 ARG A 104 168.03 45.33
REMARK 500 2 ARG A 106 -79.50 -123.13
REMARK 500 2 VAL A 109 50.97 -95.34
REMARK 500 2 CYS A 110 69.46 -51.34
REMARK 500 2 GLU B 122 -84.35 -26.93
REMARK 500 3 ASN A 5 -22.05 80.03
REMARK 500 3 TRP A 11 -15.25 -149.19
REMARK 500 3 LYS A 14 -158.93 -45.38
REMARK 500 3 SER A 15 16.19 -68.08
REMARK 500
REMARK 500 THIS ENTRY HAS 499 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE B 118
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 B 125
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LUI RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE ITK SH2 DOMAIN, PRO287CIS, 20 LOW ENERGY
REMARK 900 STRUCTURES
REMARK 900 RELATED ID: 1LUK RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE ITK SH2 DOMAIN, PRO287CIS, ENERGY MINIMIZED
REMARK 900 AVERAGE STRUCTURE
REMARK 900 RELATED ID: 1LUM RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE ITK SH2 DOMAIN, PRO287TRANS, 20 LOW ENERGY
REMARK 900 STRUCTURES
REMARK 900 RELATED ID: 1LUN RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE ITK SH2 DOMAIN, PRO287TRANS, ENERGY MINIMIZED
REMARK 900 AVERAGE STRUCTURE
REMARK 900 RELATED ID: 2ETZ RELATED DB: PDB
REMARK 900 THE NMR MINIMIZED AVERAGE STRUCTURE OF THE ITK SH2 DOMAIN BOUND TO
REMARK 900 A PHOSPHOPEPTIDE
DBREF 2EU0 A 4 110 UNP Q03526 ITK_MOUSE 238 344
DBREF 2EU0 B 119 124 UNP Q60787 LCP2_MOUSE 143 148
SEQADV 2EU0 GLY A 111 UNP Q03526 CLONING ARTIFACT
SEQADV 2EU0 PTR B 121 UNP Q60787 TYR 145 MODIFIED RESIDUE
SEQRES 1 A 109 ACE ASN ASN LEU GLU THR TYR GLU TRP TYR ASN LYS SER
SEQRES 2 A 109 ILE SER ARG ASP LYS ALA GLU LYS LEU LEU LEU ASP THR
SEQRES 3 A 109 GLY LYS GLU GLY ALA PHE MET VAL ARG ASP SER ARG THR
SEQRES 4 A 109 PRO GLY THR TYR THR VAL SER VAL PHE THR LYS ALA ILE
SEQRES 5 A 109 ILE SER GLU ASN PRO CYS ILE LYS HIS TYR HIS ILE LYS
SEQRES 6 A 109 GLU THR ASN ASP SER PRO LYS ARG TYR TYR VAL ALA GLU
SEQRES 7 A 109 LYS TYR VAL PHE ASP SER ILE PRO LEU LEU ILE GLN TYR
SEQRES 8 A 109 HIS GLN TYR ASN GLY GLY GLY LEU VAL THR ARG LEU ARG
SEQRES 9 A 109 TYR PRO VAL CYS GLY
SEQRES 1 B 8 ACE ALA ASP PTR GLU PRO PRO NH2
MODRES 2EU0 PTR B 121 TYR O-PHOSPHOTYROSINE
HET ACE A 3 6
HET ACE B 118 6
HET PTR B 121 24
HET NH2 B 125 1
HETNAM ACE ACETYL GROUP
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM NH2 AMINO GROUP
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 ACE 2(C2 H4 O)
FORMUL 2 PTR C9 H12 N O6 P
FORMUL 2 NH2 H2 N
HELIX 1 1 ASN A 4 TYR A 9 5 6
HELIX 2 2 SER A 17 GLY A 29 1 13
HELIX 3 3 SER A 86 ASN A 97 1 12
SHEET 1 A 4 CYS A 60 ILE A 66 0
SHEET 2 A 4 TYR A 45 THR A 51 -1 N TYR A 45 O ILE A 66
SHEET 3 A 4 ALA A 33 ASP A 38 -1 N ARG A 37 O THR A 46
SHEET 4 A 4 TYR A 107 PRO A 108 1 O TYR A 107 N PHE A 34
SHEET 1 B 2 TYR A 76 TYR A 77 0
SHEET 2 B 2 VAL A 83 PHE A 84 -1 O PHE A 84 N TYR A 76
LINK C ACE A 3 N ASN A 4 1555 1555 1.33
LINK C ACE B 118 N ALA B 119 1555 1555 1.33
LINK C ASP B 120 N PTR B 121 1555 1555 1.33
LINK C PTR B 121 N GLU B 122 1555 1555 1.33
LINK C PRO B 124 N NH2 B 125 1555 1555 1.33
CISPEP 1 SER A 72 PRO A 73 1 -0.02
CISPEP 2 SER A 72 PRO A 73 2 0.65
CISPEP 3 SER A 72 PRO A 73 3 0.32
CISPEP 4 SER A 72 PRO A 73 4 -0.05
CISPEP 5 SER A 72 PRO A 73 5 1.03
CISPEP 6 SER A 72 PRO A 73 6 -0.14
CISPEP 7 SER A 72 PRO A 73 7 -0.25
CISPEP 8 SER A 72 PRO A 73 8 0.99
CISPEP 9 SER A 72 PRO A 73 9 0.27
CISPEP 10 SER A 72 PRO A 73 10 0.00
CISPEP 11 SER A 72 PRO A 73 11 -0.51
CISPEP 12 SER A 72 PRO A 73 12 0.22
CISPEP 13 SER A 72 PRO A 73 13 -0.40
CISPEP 14 SER A 72 PRO A 73 14 0.44
CISPEP 15 SER A 72 PRO A 73 15 0.21
CISPEP 16 SER A 72 PRO A 73 16 1.14
CISPEP 17 SER A 72 PRO A 73 17 0.42
CISPEP 18 SER A 72 PRO A 73 18 0.18
CISPEP 19 SER A 72 PRO A 73 19 0.42
CISPEP 20 SER A 72 PRO A 73 20 -0.11
SITE 1 AC2 2 PTR B 121 PRO B 123
SITE 1 AC3 3 ALA A 79 GLU A 80 PRO B 124
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 - r 9 2 Bytes