Header list of 1cz2.pdb file
Complete list - b 16 2 Bytes
HEADER LIPID BINDING PROTEIN 01-SEP-99 1CZ2
TITLE SOLUTION STRUCTURE OF WHEAT NS-LTP COMPLEXED WITH PROSTAGLANDIN B2.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NONSPECIFIC LIPID TRANSFER PROTEIN;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRITICUM AESTIVUM;
SOURCE 3 ORGANISM_COMMON: BREAD WHEAT;
SOURCE 4 ORGANISM_TAXID: 4565;
SOURCE 5 ORGAN: SEED
KEYWDS PROTEIN COMPLEX ALPHA HELIX, LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 12
AUTHOR S.TASSIN-MOINDROT,A.CAILLE,J.-P.DOULIEZ,D.MARION,F.VOVELLE
REVDAT 4 16-FEB-22 1CZ2 1 REMARK
REVDAT 3 24-FEB-09 1CZ2 1 VERSN
REVDAT 2 01-APR-03 1CZ2 1 JRNL
REVDAT 1 27-SEP-00 1CZ2 0
JRNL AUTH S.TASSIN-MOINDROT,A.CAILLE,J.P.DOULIEZ,D.MARION,F.VOVELLE
JRNL TITL THE WIDE BINDING PROPERTIES OF A WHEAT NONSPECIFIC LIPID
JRNL TITL 2 TRANSFER PROTEIN. SOLUTION STRUCTURE OF A COMPLEX WITH
JRNL TITL 3 PROSTAGLANDIN B2.
JRNL REF EUR.J.BIOCHEM. V. 267 1117 2000
JRNL REFN ISSN 0014-2956
JRNL PMID 10672021
JRNL DOI 10.1046/J.1432-1327.2000.01109.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CZ2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-SEP-99.
REMARK 100 THE DEPOSITION ID IS D_1000009632.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 12
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 : NULL
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: 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 5 NE2 HIS A 5 CD2 -0.072
REMARK 500 1 HIS A 35 NE2 HIS A 35 CD2 -0.071
REMARK 500 1 HIS A 59 NE2 HIS A 59 CD2 -0.071
REMARK 500 2 HIS A 5 NE2 HIS A 5 CD2 -0.072
REMARK 500 2 HIS A 35 NE2 HIS A 35 CD2 -0.071
REMARK 500 2 HIS A 59 NE2 HIS A 59 CD2 -0.071
REMARK 500 3 HIS A 5 NE2 HIS A 5 CD2 -0.073
REMARK 500 3 HIS A 35 NE2 HIS A 35 CD2 -0.072
REMARK 500 3 HIS A 59 NE2 HIS A 59 CD2 -0.071
REMARK 500 4 HIS A 5 NE2 HIS A 5 CD2 -0.071
REMARK 500 4 HIS A 35 NE2 HIS A 35 CD2 -0.072
REMARK 500 4 HIS A 59 NE2 HIS A 59 CD2 -0.071
REMARK 500 5 HIS A 5 NE2 HIS A 5 CD2 -0.071
REMARK 500 5 HIS A 35 NE2 HIS A 35 CD2 -0.071
REMARK 500 5 HIS A 59 NE2 HIS A 59 CD2 -0.072
REMARK 500 6 HIS A 5 NE2 HIS A 5 CD2 -0.071
REMARK 500 6 HIS A 35 NE2 HIS A 35 CD2 -0.071
REMARK 500 6 HIS A 59 NE2 HIS A 59 CD2 -0.072
REMARK 500 7 HIS A 5 NE2 HIS A 5 CD2 -0.072
REMARK 500 7 HIS A 35 NE2 HIS A 35 CD2 -0.072
REMARK 500 7 HIS A 59 NE2 HIS A 59 CD2 -0.072
REMARK 500 8 HIS A 5 NE2 HIS A 5 CD2 -0.071
REMARK 500 8 HIS A 35 NE2 HIS A 35 CD2 -0.073
REMARK 500 8 HIS A 59 NE2 HIS A 59 CD2 -0.070
REMARK 500 9 HIS A 5 NE2 HIS A 5 CD2 -0.072
REMARK 500 9 HIS A 35 NE2 HIS A 35 CD2 -0.074
REMARK 500 9 HIS A 59 NE2 HIS A 59 CD2 -0.071
REMARK 500 10 HIS A 5 NE2 HIS A 5 CD2 -0.072
REMARK 500 10 HIS A 35 NE2 HIS A 35 CD2 -0.073
REMARK 500 10 HIS A 59 NE2 HIS A 59 CD2 -0.072
REMARK 500 11 HIS A 5 NE2 HIS A 5 CD2 -0.073
REMARK 500 11 HIS A 35 NE2 HIS A 35 CD2 -0.071
REMARK 500 11 HIS A 59 NE2 HIS A 59 CD2 -0.071
REMARK 500 12 HIS A 5 NE2 HIS A 5 CD2 -0.073
REMARK 500 12 HIS A 35 NE2 HIS A 35 CD2 -0.071
REMARK 500 12 HIS A 59 NE2 HIS A 59 CD2 -0.072
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 11 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 2 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 2 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 3 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 3 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 3 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 4 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 4 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 4 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 4 TYR A 79 CB - CG - CD1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 5 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 5 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 5 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 6 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 6 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 7 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 7 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 8 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 8 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 8 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 8 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 8 TYR A 79 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 8 TYR A 79 CB - CG - CD1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 8 ARG A 89 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 9 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 9 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 9 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 9 ARG A 89 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 10 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 10 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 10 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 10 ARG A 89 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 11 TYR A 16 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 11 TYR A 16 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 11 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 11 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 11 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 12 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 12 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.4 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 ILE A 54 -74.92 -81.56
REMARK 500 1 ASN A 60 80.50 -66.07
REMARK 500 1 LYS A 72 -61.12 -162.22
REMARK 500 1 THR A 80 -76.81 -74.22
REMARK 500 1 SER A 82 48.92 -92.97
REMARK 500 1 ILE A 85 -99.38 -129.98
REMARK 500 2 ARG A 39 -50.35 -130.41
REMARK 500 2 ILE A 54 -73.00 -80.63
REMARK 500 2 ASN A 60 80.46 -66.08
REMARK 500 2 LYS A 72 -61.32 -161.25
REMARK 500 2 THR A 80 -75.37 -77.41
REMARK 500 2 SER A 82 45.47 -93.85
REMARK 500 2 ILE A 85 -97.98 -129.26
REMARK 500 3 GLN A 37 34.05 -90.43
REMARK 500 3 ALA A 38 54.02 -148.25
REMARK 500 3 ILE A 54 -64.82 -92.70
REMARK 500 3 ASN A 60 64.59 -174.91
REMARK 500 3 LYS A 72 -58.16 -168.99
REMARK 500 3 LEU A 77 156.74 -28.97
REMARK 500 3 THR A 80 -72.15 -89.42
REMARK 500 3 SER A 82 53.62 -94.64
REMARK 500 3 ASP A 86 58.33 -119.17
REMARK 500 3 CYS A 87 173.40 66.00
REMARK 500 4 ASP A 2 87.52 38.00
REMARK 500 4 CYS A 3 78.79 -63.13
REMARK 500 4 GLN A 37 38.88 -81.91
REMARK 500 4 ALA A 38 58.88 -159.61
REMARK 500 4 SER A 42 -55.01 175.54
REMARK 500 4 ILE A 54 -72.88 -81.25
REMARK 500 4 ASN A 60 65.36 -179.17
REMARK 500 4 ASN A 76 47.36 -142.15
REMARK 500 4 LEU A 77 165.48 57.35
REMARK 500 4 TYR A 79 -75.15 -127.86
REMARK 500 4 THR A 80 -77.86 -152.43
REMARK 500 4 ILE A 81 96.01 167.23
REMARK 500 4 SER A 82 31.39 -71.19
REMARK 500 4 ILE A 85 -87.66 -128.34
REMARK 500 4 SER A 88 82.96 60.40
REMARK 500 5 ASP A 2 62.38 110.63
REMARK 500 5 CYS A 3 44.68 36.95
REMARK 500 5 ALA A 38 57.92 -115.93
REMARK 500 5 ILE A 54 -89.77 -82.51
REMARK 500 5 ILE A 58 86.90 -64.72
REMARK 500 5 ASN A 60 62.15 179.84
REMARK 500 5 PRO A 71 -164.16 -72.06
REMARK 500 5 LYS A 72 -71.59 64.85
REMARK 500 5 ILE A 81 160.90 68.40
REMARK 500 5 LEU A 83 74.51 -106.19
REMARK 500 5 ASN A 84 22.85 82.76
REMARK 500 5 ILE A 85 -128.52 -135.56
REMARK 500
REMARK 500 THIS ENTRY HAS 112 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 3 TYR A 16 0.12 SIDE CHAIN
REMARK 500 3 TYR A 79 0.10 SIDE CHAIN
REMARK 500 4 TYR A 16 0.09 SIDE CHAIN
REMARK 500 5 TYR A 16 0.11 SIDE CHAIN
REMARK 500 5 TYR A 79 0.12 SIDE CHAIN
REMARK 500 6 TYR A 79 0.12 SIDE CHAIN
REMARK 500 7 TYR A 79 0.14 SIDE CHAIN
REMARK 500 11 TYR A 79 0.11 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 E2P A 91
DBREF 1CZ2 A 1 90 UNP P24296 NLTP1_WHEAT 1 90
SEQRES 1 A 90 ILE ASP CYS GLY HIS VAL ASP SER LEU VAL ARG PRO CYS
SEQRES 2 A 90 LEU SER TYR VAL GLN GLY GLY PRO GLY PRO SER GLY GLN
SEQRES 3 A 90 CYS CYS ASP GLY VAL LYS ASN LEU HIS ASN GLN ALA ARG
SEQRES 4 A 90 SER GLN SER ASP ARG GLN SER ALA CYS ASN CYS LEU LYS
SEQRES 5 A 90 GLY ILE ALA ARG GLY ILE HIS ASN LEU ASN GLU ASP ASN
SEQRES 6 A 90 ALA ARG SER ILE PRO PRO LYS CYS GLY VAL ASN LEU PRO
SEQRES 7 A 90 TYR THR ILE SER LEU ASN ILE ASP CYS SER ARG VAL
HET E2P A 91 53
HETNAM E2P PROSTAGLANDIN B2
FORMUL 2 E2P C20 H30 O4
HELIX 1 1 GLY A 4 GLY A 20 1 17
HELIX 2 2 SER A 24 ALA A 38 1 15
HELIX 3 3 SER A 40 ILE A 54 1 15
HELIX 4 4 ASN A 62 SER A 68 1 7
HELIX 5 5 ILE A 69 GLY A 74 1 6
SSBOND 1 CYS A 3 CYS A 50 1555 1555 2.03
SSBOND 2 CYS A 13 CYS A 27 1555 1555 2.03
SSBOND 3 CYS A 28 CYS A 73 1555 1555 2.03
SSBOND 4 CYS A 48 CYS A 87 1555 1555 2.03
CISPEP 1 GLY A 22 PRO A 23 1 5.15
CISPEP 2 GLY A 22 PRO A 23 2 4.89
CISPEP 3 GLY A 22 PRO A 23 3 0.53
CISPEP 4 GLY A 22 PRO A 23 4 3.80
CISPEP 5 GLY A 22 PRO A 23 5 -0.59
CISPEP 6 GLY A 22 PRO A 23 6 3.15
CISPEP 7 GLY A 22 PRO A 23 7 -0.08
CISPEP 8 GLY A 22 PRO A 23 8 2.94
CISPEP 9 GLY A 22 PRO A 23 9 4.65
CISPEP 10 GLY A 22 PRO A 23 10 4.67
CISPEP 11 GLY A 22 PRO A 23 11 0.40
CISPEP 12 GLY A 22 PRO A 23 12 -0.17
SITE 1 AC1 10 VAL A 10 CYS A 13 VAL A 17 ALA A 38
SITE 2 AC1 10 CYS A 50 LEU A 51 PRO A 78 TYR A 79
SITE 3 AC1 10 THR A 80 ILE A 81
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