Header list of 1a7m.pdb file
Complete list - b 16 2 Bytes
HEADER CYTOKINE 16-MAR-98 1A7M
TITLE LEUKAEMIA INHIBITORY FACTOR CHIMERA (MH35-LIF), NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEUKEMIA INHIBITORY FACTOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LIF;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: MURINE-HUMAN CHIMERA
SOURCE MOL_ID: 1;
SOURCE 2 FRAGMENT: RESIDUES 48-81;
SOURCE 3 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 4 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 5 ORGANISM_TAXID: 10090;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: NM522
KEYWDS CYTOKINE, FOUR HELICAL BUNDLE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.G.HINDS,T.MAURER,J.-G.ZHANG,N.A.NICOLA,R.S.NORTON
REVDAT 3 16-FEB-22 1A7M 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1A7M 1 VERSN
REVDAT 1 20-APR-99 1A7M 0
JRNL AUTH M.G.HINDS,T.MAURER,J.G.ZHANG,N.A.NICOLA,R.S.NORTON
JRNL TITL SOLUTION STRUCTURE OF LEUKEMIA INHIBITORY FACTOR.
JRNL REF J.BIOL.CHEM. V. 273 13738 1998
JRNL REFN ISSN 0021-9258
JRNL PMID 9593715
JRNL DOI 10.1074/JBC.273.22.13738
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESTRAINED SIMULATED ANNEALING OF DYANA
REMARK 3 STRUCTURES
REMARK 4
REMARK 4 1A7M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170493.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 4.4
REMARK 210 IONIC STRENGTH : 1 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-NOESY-HSQC; 15N-TOCSY-HSQC;
REMARK 210 13C-NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX 600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA, X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N LABELLED MH35 LEUKAEMIA INHIBITORY
REMARK 210 FACTOR
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 9 CYS A 60 CA CYS A 60 CB -0.082
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 TYR A 84 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 1 ARG A 99 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 1 ARG A 123 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 1 ARG A 132 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 2 CYS A 18 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 2 PHE A 52 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 2 CYS A 131 CA - CB - SG ANGL. DEV. = 8.6 DEGREES
REMARK 500 2 CYS A 163 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 3 ARG A 15 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 3 ARG A 85 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 3 CYS A 131 CA - CB - SG ANGL. DEV. = 10.2 DEGREES
REMARK 500 3 CYS A 134 CA - CB - SG ANGL. DEV. = 10.7 DEGREES
REMARK 500 3 ARG A 138 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 3 ASP A 143 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 5 CYS A 12 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 5 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 5 THR A 65 OG1 - CB - CG2 ANGL. DEV. = -13.9 DEGREES
REMARK 500 5 TYR A 84 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 5 ARG A 85 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 5 ARG A 123 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 5 CYS A 131 CA - CB - SG ANGL. DEV. = 9.0 DEGREES
REMARK 500 5 ARG A 132 NE - CZ - NH2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 5 ARG A 138 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 5 PHE A 156 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 5 TYR A 169 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 5 TYR A 169 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 6 TYR A 84 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 6 ARG A 123 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 6 ARG A 132 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 6 CYS A 163 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 7 TYR A 45 CB - CG - CD1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 8 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 8 PHE A 52 CB - CG - CD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 8 PHE A 52 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 8 ARG A 123 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 8 ARG A 132 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 8 ARG A 138 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 8 CYS A 163 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 9 PHE A 52 CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 9 TYR A 137 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 9 TYR A 137 CB - CG - CD1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 9 CYS A 163 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 10 TYR A 84 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 10 ARG A 85 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 10 CYS A 134 CA - CB - SG ANGL. DEV. = 8.3 DEGREES
REMARK 500 10 TYR A 137 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 10 TYR A 137 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 11 ARG A 85 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 11 ARG A 123 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 11 TYR A 137 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 83 ANGLE DEVIATIONS.
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 2 -162.07 -73.83
REMARK 500 1 ALA A 10 -82.63 -140.17
REMARK 500 1 CYS A 12 -22.67 -28.18
REMARK 500 1 CYS A 18 -164.52 41.68
REMARK 500 1 ASN A 21 -121.12 -141.42
REMARK 500 1 LEU A 22 -54.89 -167.38
REMARK 500 1 MET A 23 -69.36 -19.50
REMARK 500 1 GLN A 25 -72.24 -85.65
REMARK 500 1 PHE A 41 -59.01 -28.92
REMARK 500 1 SER A 43 -31.33 -37.64
REMARK 500 1 TYR A 44 -71.53 -84.61
REMARK 500 1 PHE A 52 -71.19 -145.92
REMARK 500 1 PRO A 53 3.85 -59.50
REMARK 500 1 PRO A 62 52.48 -62.47
REMARK 500 1 ASN A 63 -66.45 -140.56
REMARK 500 1 VAL A 64 -42.68 -139.41
REMARK 500 1 THR A 65 -142.93 51.69
REMARK 500 1 ASP A 66 45.06 -108.10
REMARK 500 1 PHE A 70 112.73 -19.95
REMARK 500 1 SER A 91 -39.70 -39.89
REMARK 500 1 CYS A 134 -76.32 -69.56
REMARK 500 1 LYS A 136 53.28 -147.09
REMARK 500 1 TYR A 137 -46.85 71.55
REMARK 500 1 VAL A 139 -58.66 -148.32
REMARK 500 1 ASP A 143 134.71 65.22
REMARK 500 1 PRO A 146 71.47 -65.02
REMARK 500 1 VAL A 147 63.91 -113.58
REMARK 500 1 ASP A 149 135.42 174.18
REMARK 500 1 SER A 151 48.74 -91.55
REMARK 500 1 GLU A 154 -91.86 -89.65
REMARK 500 1 LEU A 161 -35.23 -36.13
REMARK 500 1 LEU A 165 -61.20 -90.73
REMARK 500 1 TYR A 169 -47.97 -29.50
REMARK 500 2 LEU A 3 79.20 -114.23
REMARK 500 2 VAL A 8 52.93 -110.11
REMARK 500 2 CYS A 12 45.52 32.00
REMARK 500 2 ALA A 13 -73.78 -128.52
REMARK 500 2 ILE A 14 38.96 -99.90
REMARK 500 2 ARG A 15 -91.10 -100.91
REMARK 500 2 CYS A 18 -159.06 82.32
REMARK 500 2 ASN A 21 -98.19 -126.81
REMARK 500 2 LEU A 22 -68.64 67.70
REMARK 500 2 MET A 23 -69.51 -20.15
REMARK 500 2 GLN A 25 -69.86 -94.53
REMARK 500 2 TYR A 44 -68.47 -91.85
REMARK 500 2 GLU A 50 164.88 -37.82
REMARK 500 2 PHE A 52 -67.60 -138.91
REMARK 500 2 PRO A 53 -26.15 -35.39
REMARK 500 2 THR A 65 -153.61 -100.03
REMARK 500 2 ASP A 66 41.12 -102.07
REMARK 500
REMARK 500 THIS ENTRY HAS 637 RAMACHANDRAN OUTLIERS.
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 SER A 1 PRO A 2 3 147.81
REMARK 500 PRO A 68 PRO A 69 9 -147.92
REMARK 500 SER A 1 PRO A 2 11 144.33
REMARK 500 SER A 1 PRO A 2 12 144.78
REMARK 500 SER A 1 PRO A 2 18 145.64
REMARK 500 PRO A 68 PRO A 69 20 -146.74
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1A7M A 1 180 UNP P09056 LIF_MOUSE 24 203
SEQADV 1A7M LEU A 56 UNP P09056 VAL 79 CONFLICT
SEQADV 1A7M ASP A 57 UNP P09056 GLU 80 CONFLICT
SEQADV 1A7M GLY A 61 UNP P09056 ALA 84 CONFLICT
SEQADV 1A7M VAL A 64 UNP P09056 MET 87 CONFLICT
SEQADV 1A7M PRO A 69 UNP P09056 SER 92 CONFLICT
SEQADV 1A7M ALA A 72 UNP P09056 GLY 95 CONFLICT
SEQADV 1A7M ALA A 78 UNP P09056 THR 101 CONFLICT
SEQADV 1A7M SER A 107 UNP P09056 THR 130 CONFLICT
SEQADV 1A7M HIS A 112 UNP P09056 GLN 135 CONFLICT
SEQADV 1A7M SER A 113 UNP P09056 VAL 136 CONFLICT
SEQADV 1A7M VAL A 155 UNP P09056 ALA 178 CONFLICT
SEQADV 1A7M LYS A 158 UNP P09056 ARG 181 CONFLICT
SEQRES 1 A 180 SER PRO LEU PRO ILE THR PRO VAL ASN ALA THR CYS ALA
SEQRES 2 A 180 ILE ARG HIS PRO CYS HIS GLY ASN LEU MET ASN GLN ILE
SEQRES 3 A 180 LYS ASN GLN LEU ALA GLN LEU ASN GLY SER ALA ASN ALA
SEQRES 4 A 180 LEU PHE ILE SER TYR TYR THR ALA GLN GLY GLU PRO PHE
SEQRES 5 A 180 PRO ASN ASN LEU ASP LYS LEU CYS GLY PRO ASN VAL THR
SEQRES 6 A 180 ASP PHE PRO PRO PHE HIS ALA ASN GLY THR GLU LYS ALA
SEQRES 7 A 180 LYS LEU VAL GLU LEU TYR ARG MET VAL ALA TYR LEU SER
SEQRES 8 A 180 ALA SER LEU THR ASN ILE THR ARG ASP GLN LYS VAL LEU
SEQRES 9 A 180 ASN PRO SER ALA VAL SER LEU HIS SER LYS LEU ASN ALA
SEQRES 10 A 180 THR ILE ASP VAL MET ARG GLY LEU LEU SER ASN VAL LEU
SEQRES 11 A 180 CYS ARG LEU CYS ASN LYS TYR ARG VAL GLY HIS VAL ASP
SEQRES 12 A 180 VAL PRO PRO VAL PRO ASP HIS SER ASP LYS GLU VAL PHE
SEQRES 13 A 180 GLN LYS LYS LYS LEU GLY CYS GLN LEU LEU GLY THR TYR
SEQRES 14 A 180 LYS GLN VAL ILE SER VAL VAL VAL GLN ALA PHE
HELIX 1 1 CYS A 12 ILE A 14 5 3
HELIX 2 2 LEU A 22 GLN A 48 1 27
HELIX 3 3 LEU A 56 LEU A 59 1 4
HELIX 4 4 GLU A 76 LEU A 104 1 29
HELIX 5 5 ALA A 108 LYS A 136 1 29
HELIX 6 6 GLU A 154 LYS A 160 1 7
HELIX 7 7 CYS A 163 VAL A 176 1 14
SSBOND 1 CYS A 12 CYS A 134 1555 1555 2.03
SSBOND 2 CYS A 18 CYS A 131 1555 1555 2.02
SSBOND 3 CYS A 60 CYS A 163 1555 1555 2.02
CISPEP 1 GLU A 50 PRO A 51 1 -6.75
CISPEP 2 GLU A 50 PRO A 51 2 -5.11
CISPEP 3 GLU A 50 PRO A 51 3 -5.21
CISPEP 4 GLU A 50 PRO A 51 4 -5.62
CISPEP 5 GLU A 50 PRO A 51 5 -5.84
CISPEP 6 GLU A 50 PRO A 51 6 2.81
CISPEP 7 GLU A 50 PRO A 51 7 -2.73
CISPEP 8 GLU A 50 PRO A 51 8 -5.66
CISPEP 9 GLU A 50 PRO A 51 9 -5.73
CISPEP 10 GLU A 50 PRO A 51 10 -5.87
CISPEP 11 GLU A 50 PRO A 51 11 3.25
CISPEP 12 GLU A 50 PRO A 51 12 -5.55
CISPEP 13 GLU A 50 PRO A 51 13 -5.71
CISPEP 14 GLU A 50 PRO A 51 14 -3.99
CISPEP 15 GLU A 50 PRO A 51 15 -5.22
CISPEP 16 GLU A 50 PRO A 51 16 -5.68
CISPEP 17 GLU A 50 PRO A 51 17 -6.17
CISPEP 18 GLU A 50 PRO A 51 18 -5.79
CISPEP 19 GLU A 50 PRO A 51 19 -1.34
CISPEP 20 GLU A 50 PRO A 51 20 -5.92
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