Header list of 1eio.pdb file
Complete list - 16 20 Bytes
HEADER LIPID BINDING PROTEIN 27-FEB-00 1EIO
TITLE ILEAL LIPID BINDING PROTEIN IN COMPLEX WITH GLYCOCHOLATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ILEAL LIPID BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET3D
KEYWDS BILE ACID BINDING, PROTEIN-LIGAND INTERACTION, LIPID-BINDING PROTEIN,
KEYWDS 2 LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 5
AUTHOR C.LUECKE,F.ZHANG,J.A.HAMILTON,J.C.SACCHETTINI,H.RUETERJANS
REVDAT 3 16-FEB-22 1EIO 1 KEYWDS REMARK SEQADV
REVDAT 2 24-FEB-09 1EIO 1 VERSN
REVDAT 1 31-MAY-00 1EIO 0
JRNL AUTH C.LUECKE,F.ZHANG,J.A.HAMILTON,J.C.SACCHETTINI,H.RUETERJANS
JRNL TITL SOLUTION STRUCTURE OF ILEAL LIPID BINDING PROTEIN IN COMPLEX
JRNL TITL 2 WITH GLYCOCHOLATE.
JRNL REF EUR.J.BIOCHEM. V. 267 2929 2000
JRNL REFN ISSN 0014-2956
JRNL PMID 10806391
JRNL DOI 10.1046/J.1432-1327.2000.01307.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.LUECKE,F.ZHANG,H.RUETERJANS,J.A.HAMILTON,J.C.SACCHETTINI
REMARK 1 TITL FLEXIBILITY IS A LIKELY DETERMINANT OF BINDING IN THE CASE
REMARK 1 TITL 2 OF ILEAL LIPID BINDING PROTEIN
REMARK 1 REF STRUCTURE V. 4 785 1996
REMARK 1 REFN ISSN 0969-2126
REMARK 1 DOI 10.1016/S0969-2126(96)00086-X
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.LUECKE,D.FUSHMAN,C.LUDWIG,J.A.HAMILTON,J.C.SACCHETTINI,
REMARK 1 AUTH 2 H.RUETERJANS
REMARK 1 TITL A COMPARATIVE STUDY OF THE BACKBONE DYNAMICS OF TWO CLOSELY
REMARK 1 TITL 2 RELATED LIPID BINDING PROTEINS: BOVINE HEART FATTY ACID
REMARK 1 TITL 3 BINDING PROTEIN AND PORCINE ILEAL LIPID BINDING PROTEIN
REMARK 1 REF MOL.CELL.BIOCHEM. V. 192 109 1999
REMARK 1 REFN ISSN 0300-8177
REMARK 1 DOI 10.1023/A:1006834708786
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 1.3, SYBYL 6.4
REMARK 3 AUTHORS : BRUKER (XWINNMR), TRIPOS (SYBYL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE LIGAND WAS DOCKED INTO THE PROTEIN
REMARK 3 STRUCTURE BY SIMULATED ANNEALING
REMARK 4
REMARK 4 1EIO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010614.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 20MM KH2PO4
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3-4MM ILBP/GLYCOCHOLATE COMPLEX
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D 1H/13C-NOESY; 2D
REMARK 210 TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA 2.1, FELIX 95.0, DIANA
REMARK 210 2.8
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 8
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 5
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGIES AFTER DOCKING OF LIGAND
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: 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 OD2 ASP A 26 HE2 HIS A 57 1.36
REMARK 500 HZ1 LYS A 89 OE2 GLU A 102 1.38
REMARK 500 OE1 GLU A 7 HZ3 LYS A 35 1.39
REMARK 500 OE2 GLU A 72 HZ2 LYS A 78 1.41
REMARK 500 OD1 ASP A 26 HZ2 LYS A 30 1.41
REMARK 500 OD1 ASP A 70 HZ2 LYS A 80 1.42
REMARK 500 HE2 HIS A 99 OE2 GLU A 110 1.43
REMARK 500 OE2 GLU A 86 HE2 HIS A 98 1.43
REMARK 500 OD1 ASP A 15 HZ1 LYS A 19 1.43
REMARK 500 OD2 ASP A 70 HZ1 LYS A 78 1.44
REMARK 500 OE2 GLU A 16 HZ2 LYS A 19 1.46
REMARK 500 OE1 GLU A 68 HZ1 LYS A 80 1.46
REMARK 500 HZ1 LYS A 67 OE2 GLU A 68 1.46
REMARK 500 OD2 ASP A 29 HZ1 LYS A 30 1.46
REMARK 500 HZ1 LYS A 41 OD1 ASP A 43 1.47
REMARK 500 OE2 GLU A 9 HZ3 LYS A 124 1.48
REMARK 500 OD2 ASP A 105 HZ3 LYS A 107 1.48
REMARK 500 OD1 ASP A 105 HZ2 LYS A 124 1.49
REMARK 500 OE1 GLU A 11 HH TYR A 119 1.51
REMARK 500 OE2 GLU A 11 HH11 ARG A 121 1.52
REMARK 500 OD2 ASP A 15 HH22 ARG A 32 1.56
REMARK 500 HZ2 LYS A 5 OE2 GLU A 39 1.57
REMARK 500 HZ2 LYS A 77 O2 GCH A 128 1.57
REMARK 500 O LEU A 21 HZ3 LYS A 77 1.57
REMARK 500 OE1 GLU A 16 HH12 ARG A 20 1.58
REMARK 500 OE1 GLU A 9 HZ2 LYS A 107 1.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 HIS A 57 CG HIS A 57 CD2 0.077
REMARK 500 1 HIS A 98 CG HIS A 98 CD2 0.076
REMARK 500 1 HIS A 99 CG HIS A 99 CD2 0.074
REMARK 500 1 ALA A 127 C ALA A 127 OXT 0.119
REMARK 500 2 HIS A 57 CG HIS A 57 CD2 0.069
REMARK 500 2 HIS A 98 CG HIS A 98 CD2 0.073
REMARK 500 2 HIS A 99 CG HIS A 99 CD2 0.068
REMARK 500 2 ALA A 127 C ALA A 127 OXT 0.125
REMARK 500 3 HIS A 57 CG HIS A 57 CD2 0.072
REMARK 500 3 HIS A 98 CG HIS A 98 CD2 0.068
REMARK 500 3 HIS A 99 CG HIS A 99 CD2 0.071
REMARK 500 3 ALA A 127 C ALA A 127 OXT 0.121
REMARK 500 4 HIS A 57 CG HIS A 57 CD2 0.071
REMARK 500 4 HIS A 98 CG HIS A 98 CD2 0.075
REMARK 500 4 HIS A 99 CG HIS A 99 CD2 0.075
REMARK 500 4 ALA A 127 C ALA A 127 OXT 0.116
REMARK 500 5 HIS A 57 CG HIS A 57 CD2 0.070
REMARK 500 5 HIS A 98 CG HIS A 98 CD2 0.067
REMARK 500 5 HIS A 99 CG HIS A 99 CD2 0.062
REMARK 500 5 ALA A 127 C ALA A 127 OXT 0.126
REMARK 500
REMARK 500 REMARK: NULL
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 1 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 ARG A 121 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 TYR A 119 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 2 ARG A 121 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 3 ARG A 121 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 4 TYR A 119 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 4 TYR A 119 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 4 ARG A 121 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 5 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 5 TYR A 119 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 5 ARG A 121 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES
REMARK 500 5 ARG A 121 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 5 ARG A 121 NE - CZ - NH2 ANGL. DEV. = -4.2 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 LYS A 12 19.69 -154.76
REMARK 500 1 ASN A 13 18.43 -157.23
REMARK 500 1 ALA A 22 50.67 73.49
REMARK 500 1 ASP A 26 48.73 -80.36
REMARK 500 1 ALA A 27 -34.50 -158.10
REMARK 500 1 ASN A 33 36.29 83.51
REMARK 500 1 THR A 73 -45.84 84.91
REMARK 500 1 ASN A 96 35.52 72.87
REMARK 500 1 TYR A 97 119.79 -167.09
REMARK 500 1 ALA A 101 88.05 -152.20
REMARK 500 1 ASP A 105 14.02 57.79
REMARK 500 1 LEU A 126 23.62 -154.78
REMARK 500 2 ASN A 13 24.19 -150.13
REMARK 500 2 ALA A 22 39.78 84.98
REMARK 500 2 ASP A 26 -44.61 -132.80
REMARK 500 2 LYS A 30 31.44 -96.82
REMARK 500 2 ALA A 31 -1.54 -152.49
REMARK 500 2 HIS A 57 52.74 -141.42
REMARK 500 2 THR A 73 24.49 -173.71
REMARK 500 2 VAL A 104 -119.63 -124.24
REMARK 500 2 ASP A 105 40.75 -78.56
REMARK 500 2 TYR A 119 86.37 -152.68
REMARK 500 3 ASN A 33 29.80 88.98
REMARK 500 3 THR A 73 -147.75 84.59
REMARK 500 3 GLU A 86 -148.80 -101.16
REMARK 500 3 ASN A 96 38.55 -161.34
REMARK 500 3 VAL A 104 -115.80 -121.82
REMARK 500 3 ASP A 105 46.86 -79.96
REMARK 500 4 LYS A 12 43.41 -80.56
REMARK 500 4 ASN A 13 -81.79 -164.21
REMARK 500 4 TYR A 14 -55.32 71.10
REMARK 500 4 ALA A 22 39.28 81.16
REMARK 500 4 ASP A 26 -46.62 -139.06
REMARK 500 4 ARG A 32 29.05 -76.36
REMARK 500 4 ASN A 33 32.99 -157.89
REMARK 500 4 THR A 73 -23.50 -173.17
REMARK 500 4 LYS A 78 72.19 49.35
REMARK 500 4 LYS A 89 101.84 -173.65
REMARK 500 4 ASP A 105 78.33 -65.68
REMARK 500 4 LEU A 126 49.69 -101.57
REMARK 500 5 LYS A 12 -38.99 -141.16
REMARK 500 5 ALA A 22 46.86 74.56
REMARK 500 5 ASP A 43 51.84 -145.50
REMARK 500 5 GLN A 45 -19.99 96.62
REMARK 500 5 GLU A 72 64.18 -155.94
REMARK 500 5 GLU A 86 -149.90 -147.42
REMARK 500 5 PRO A 95 40.86 -71.37
REMARK 500 5 ASN A 96 -20.25 161.18
REMARK 500 5 ASP A 105 17.36 58.98
REMARK 500 5 LEU A 126 44.62 -83.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN A 52 TYR A 53 1 -142.75
REMARK 500 PHE A 79 LYS A 80 1 148.34
REMARK 500 GLU A 68 CYS A 69 2 148.96
REMARK 500 GLU A 72 THR A 73 2 136.48
REMARK 500 ILE A 74 GLY A 75 2 149.83
REMARK 500 PHE A 79 LYS A 80 2 145.43
REMARK 500 VAL A 83 GLN A 84 2 -146.69
REMARK 500 GLY A 106 LYS A 107 2 146.16
REMARK 500 ILE A 71 GLU A 72 4 149.96
REMARK 500 GLY A 88 LYS A 89 4 -133.05
REMARK 500 ARG A 32 ASN A 33 5 -65.43
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 53 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GCH A 128
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EAL RELATED DB: PDB
REMARK 900 APO-STRUCTURE OF ILBP
DBREF 1EIO A 1 127 UNP P10289 ILBP_PIG 1 127
SEQADV 1EIO SER A 118 UNP P10289 THR 118 CONFLICT
SEQRES 1 A 127 ALA PHE THR GLY LYS TYR GLU ILE GLU SER GLU LYS ASN
SEQRES 2 A 127 TYR ASP GLU PHE MET LYS ARG LEU ALA LEU PRO SER ASP
SEQRES 3 A 127 ALA ILE ASP LYS ALA ARG ASN LEU LYS ILE ILE SER GLU
SEQRES 4 A 127 VAL LYS GLN ASP GLY GLN ASN PHE THR TRP SER GLN GLN
SEQRES 5 A 127 TYR PRO GLY GLY HIS SER ILE THR ASN THR PHE THR ILE
SEQRES 6 A 127 GLY LYS GLU CYS ASP ILE GLU THR ILE GLY GLY LYS LYS
SEQRES 7 A 127 PHE LYS ALA THR VAL GLN MET GLU GLY GLY LYS VAL VAL
SEQRES 8 A 127 VAL ASN SER PRO ASN TYR HIS HIS THR ALA GLU ILE VAL
SEQRES 9 A 127 ASP GLY LYS LEU VAL GLU VAL SER THR VAL GLY GLY VAL
SEQRES 10 A 127 SER TYR GLU ARG VAL SER LYS LYS LEU ALA
HET GCH A 128 76
HETNAM GCH GLYCOCHOLIC ACID
HETSYN GCH N-CHOLYLGLYCINE
FORMUL 2 GCH C26 H43 N O6
HELIX 1 1 ASN A 13 ALA A 22 1 10
HELIX 2 2 PRO A 24 ASP A 29 1 6
SHEET 1 A10 HIS A 57 THR A 64 0
SHEET 2 A10 ASN A 46 TYR A 53 -1 N PHE A 47 O PHE A 63
SHEET 3 A10 ILE A 37 GLN A 42 -1 O ILE A 37 N GLN A 52
SHEET 4 A10 GLY A 4 GLU A 11 -1 N GLY A 4 O VAL A 40
SHEET 5 A10 VAL A 117 ALA A 127 -1 O VAL A 122 N GLU A 9
SHEET 6 A10 LYS A 107 VAL A 114 -1 N LEU A 108 O SER A 123
SHEET 7 A10 TYR A 97 VAL A 104 -1 O HIS A 98 N THR A 113
SHEET 8 A10 VAL A 90 SER A 94 -1 N VAL A 90 O ALA A 101
SHEET 9 A10 LYS A 78 MET A 85 -1 O THR A 82 N ASN A 93
SHEET 10 A10 LYS A 67 GLU A 72 -1 O LYS A 67 N VAL A 83
CISPEP 1 ALA A 1 PHE A 2 1 -6.70
CISPEP 2 GLY A 4 LYS A 5 2 -29.66
SITE 1 AC1 10 ARG A 20 LEU A 21 ASN A 61 LYS A 77
SITE 2 AC1 10 PHE A 79 VAL A 92 TYR A 97 HIS A 99
SITE 3 AC1 10 GLU A 110 VAL 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 - 16 20 Bytes