Header list of 1apf.pdb file
Complete list - v 29 2 Bytes
HEADER CARDIAC STIMULANT 30-MAY-95 1APF
TITLE ANTHOPLEURIN-B, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTHOPLEURIN-B;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AP-B, AXII
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ANTHOPLEURA XANTHOGRAMMICA;
SOURCE 3 ORGANISM_COMMON: GIANT GREEN SEA ANEMONE;
SOURCE 4 ORGANISM_TAXID: 6112;
SOURCE 5 ORGAN: WHOLE ANIMAL
KEYWDS TOXIN, SEA ANEMONE, CARDIAC STIMULANT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.A.MONKS,P.K.PALLAGHY,M.J.SCANLON,R.S.NORTON
REVDAT 3 29-NOV-17 1APF 1 REMARK HELIX
REVDAT 2 24-FEB-09 1APF 1 VERSN
REVDAT 1 11-JUL-96 1APF 0
JRNL AUTH S.A.MONKS,P.K.PALLAGHY,M.J.SCANLON,R.S.NORTON
JRNL TITL SOLUTION STRUCTURE OF THE CARDIOSTIMULANT POLYPEPTIDE
JRNL TITL 2 ANTHOPLEURIN-B AND COMPARISON WITH ANTHOPLEURIN-A.
JRNL REF STRUCTURE V. 3 791 1995
JRNL REFN ISSN 0969-2126
JRNL PMID 7582896
JRNL DOI 10.1016/S0969-2126(01)00214-3
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.K.PALLAGHY,M.J.SCANLON,S.A.MONKS,R.S.NORTON
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE IN SOLUTION OF THE POLYPEPTIDE
REMARK 1 TITL 2 CARDIAC STIMULANT ANTHOPLEURIN-A
REMARK 1 REF BIOCHEMISTRY V. 34 3782 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.S.NORTON
REMARK 1 TITL STRUCTURE AND STRUCTURE-FUNCTION RELATIONSHIPS OF SEA
REMARK 1 TITL 2 ANEMONE PROTEINS THAT INTERACT WITH THE SODIUM CHANNEL
REMARK 1 REF TOXICON V. 29 1051 1991
REMARK 1 REFN ISSN 0041-0101
REMARK 1 REFERENCE 3
REMARK 1 AUTH W.R.KEM
REMARK 1 TITL SEA ANEMONE TOXINS: STRUCTURE AND ACTION
REMARK 1 EDIT D.A.HESSINGER, H.M.LENHOFF
REMARK 1 REF THE BIOLOGY OF NEMATOCYSTS 375 1988
REMARK 1 PUBL ACADEMIC PRESS, NEW YORK
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1APF 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_1000171095.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.5
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 : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 34 NE2 HIS A 34 CD2 -0.067
REMARK 500 1 HIS A 39 NE2 HIS A 39 CD2 -0.067
REMARK 500 2 HIS A 34 NE2 HIS A 34 CD2 -0.066
REMARK 500 2 HIS A 39 NE2 HIS A 39 CD2 -0.069
REMARK 500 3 HIS A 34 NE2 HIS A 34 CD2 -0.066
REMARK 500 3 HIS A 39 NE2 HIS A 39 CD2 -0.068
REMARK 500 4 HIS A 34 NE2 HIS A 34 CD2 -0.067
REMARK 500 4 HIS A 39 NE2 HIS A 39 CD2 -0.067
REMARK 500 5 HIS A 39 NE2 HIS A 39 CD2 -0.068
REMARK 500 6 HIS A 39 NE2 HIS A 39 CD2 -0.071
REMARK 500 7 HIS A 39 NE2 HIS A 39 CD2 -0.069
REMARK 500 8 HIS A 39 NE2 HIS A 39 CD2 -0.067
REMARK 500 9 HIS A 34 NE2 HIS A 34 CD2 -0.067
REMARK 500 9 HIS A 39 NE2 HIS A 39 CD2 -0.068
REMARK 500 10 HIS A 34 NE2 HIS A 34 CD2 -0.066
REMARK 500 10 HIS A 39 NE2 HIS A 39 CD2 -0.069
REMARK 500 11 HIS A 34 NE2 HIS A 34 CD2 -0.066
REMARK 500 11 HIS A 39 NE2 HIS A 39 CD2 -0.066
REMARK 500 12 HIS A 39 NE2 HIS A 39 CD2 -0.067
REMARK 500 13 HIS A 39 NE2 HIS A 39 CD2 -0.067
REMARK 500 14 HIS A 34 NE2 HIS A 34 CD2 -0.066
REMARK 500 14 HIS A 39 NE2 HIS A 39 CD2 -0.068
REMARK 500 15 HIS A 39 NE2 HIS A 39 CD2 -0.067
REMARK 500 16 HIS A 34 NE2 HIS A 34 CD2 -0.067
REMARK 500 16 HIS A 39 NE2 HIS A 39 CD2 -0.068
REMARK 500 17 HIS A 39 NE2 HIS A 39 CD2 -0.068
REMARK 500 18 HIS A 39 NE2 HIS A 39 CD2 -0.070
REMARK 500 19 HIS A 34 NE2 HIS A 34 CD2 -0.067
REMARK 500 19 HIS A 39 NE2 HIS A 39 CD2 -0.071
REMARK 500 20 HIS A 39 NE2 HIS A 39 CD2 -0.069
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 CYS A 36 CA - CB - SG ANGL. DEV. = 9.1 DEGREES
REMARK 500 3 TRP A 23 CA - CB - CG ANGL. DEV. = -11.8 DEGREES
REMARK 500 3 CYS A 36 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 4 CYS A 36 CA - CB - SG ANGL. DEV. = 9.2 DEGREES
REMARK 500 5 CYS A 36 CA - CB - SG ANGL. DEV. = 9.6 DEGREES
REMARK 500 6 TRP A 23 CA - CB - CG ANGL. DEV. = -11.8 DEGREES
REMARK 500 6 CYS A 36 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 7 TRP A 23 CA - CB - CG ANGL. DEV. = -11.4 DEGREES
REMARK 500 7 CYS A 36 CA - CB - SG ANGL. DEV. = 8.1 DEGREES
REMARK 500 8 CYS A 36 CA - CB - SG ANGL. DEV. = 8.9 DEGREES
REMARK 500 9 TRP A 23 CA - CB - CG ANGL. DEV. = -12.5 DEGREES
REMARK 500 10 CYS A 36 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 11 CYS A 36 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 12 CYS A 36 CA - CB - SG ANGL. DEV. = 9.7 DEGREES
REMARK 500 14 CYS A 36 CA - CB - SG ANGL. DEV. = 9.1 DEGREES
REMARK 500 15 CYS A 36 CA - CB - SG ANGL. DEV. = 8.0 DEGREES
REMARK 500 16 ASP A 9 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 16 CYS A 36 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 17 TRP A 23 CA - CB - CG ANGL. DEV. = -11.6 DEGREES
REMARK 500 17 CYS A 36 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 18 CYS A 36 CA - CB - SG ANGL. DEV. = 8.7 DEGREES
REMARK 500 20 CYS A 36 CA - CB - SG ANGL. DEV. = 8.4 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 CYS A 6 -167.03 -127.73
REMARK 500 1 ASP A 9 79.41 -69.41
REMARK 500 1 PRO A 11 27.70 -70.79
REMARK 500 1 PRO A 13 -145.70 -73.05
REMARK 500 1 ASN A 16 -64.38 28.95
REMARK 500 1 LEU A 18 29.39 -152.10
REMARK 500 1 SER A 19 43.11 -88.70
REMARK 500 1 HIS A 34 29.82 -146.04
REMARK 500 1 ASN A 35 152.03 64.10
REMARK 500 1 CYS A 36 -45.77 -130.16
REMARK 500 1 PRO A 41 -174.66 -66.12
REMARK 500 1 ILE A 43 33.33 -95.06
REMARK 500 1 CYS A 47 -169.74 -127.40
REMARK 500 2 ASP A 7 -45.31 -25.39
REMARK 500 2 SER A 8 48.91 -83.28
REMARK 500 2 ASP A 9 -71.82 -103.48
REMARK 500 2 ASN A 16 79.26 53.18
REMARK 500 2 PHE A 24 49.58 -88.87
REMARK 500 2 SER A 31 107.42 -51.73
REMARK 500 2 HIS A 34 33.82 -147.03
REMARK 500 2 ASN A 35 143.29 60.44
REMARK 500 3 PRO A 11 42.88 -80.10
REMARK 500 3 PHE A 24 40.58 -88.91
REMARK 500 3 SER A 31 104.62 -58.41
REMARK 500 3 ASN A 35 156.73 59.59
REMARK 500 3 CYS A 36 -52.18 -125.66
REMARK 500 3 ALA A 38 30.96 -81.82
REMARK 500 3 ILE A 43 30.10 -88.84
REMARK 500 4 SER A 8 32.47 -97.46
REMARK 500 4 PRO A 11 26.72 -76.48
REMARK 500 4 ARG A 14 -140.35 60.01
REMARK 500 4 ASN A 16 54.38 -156.98
REMARK 500 4 LEU A 18 74.08 -118.49
REMARK 500 4 SER A 19 47.80 -98.71
REMARK 500 4 PHE A 24 49.81 -89.00
REMARK 500 4 SER A 31 105.65 -53.13
REMARK 500 4 HIS A 34 36.59 -146.98
REMARK 500 4 ASN A 35 137.93 63.30
REMARK 500 4 ALA A 38 34.21 -97.99
REMARK 500 5 ASP A 7 -74.92 -80.47
REMARK 500 5 PRO A 11 40.09 -79.81
REMARK 500 5 ARG A 14 33.67 -67.82
REMARK 500 5 ASN A 16 -84.42 -119.58
REMARK 500 5 THR A 17 48.81 -150.52
REMARK 500 5 LEU A 18 149.64 66.67
REMARK 500 5 SER A 27 31.90 -86.65
REMARK 500 5 SER A 31 109.57 -49.64
REMARK 500 5 HIS A 34 34.18 -143.62
REMARK 500 5 ASN A 35 146.16 61.76
REMARK 500 5 PRO A 41 -171.89 -66.25
REMARK 500
REMARK 500 THIS ENTRY HAS 166 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 12 0.31 SIDE CHAIN
REMARK 500 1 ARG A 14 0.32 SIDE CHAIN
REMARK 500 2 ARG A 12 0.31 SIDE CHAIN
REMARK 500 2 ARG A 14 0.28 SIDE CHAIN
REMARK 500 3 ARG A 12 0.32 SIDE CHAIN
REMARK 500 3 ARG A 14 0.31 SIDE CHAIN
REMARK 500 4 ARG A 12 0.24 SIDE CHAIN
REMARK 500 4 ARG A 14 0.27 SIDE CHAIN
REMARK 500 5 ARG A 12 0.24 SIDE CHAIN
REMARK 500 5 ARG A 14 0.31 SIDE CHAIN
REMARK 500 6 ARG A 12 0.31 SIDE CHAIN
REMARK 500 6 ARG A 14 0.29 SIDE CHAIN
REMARK 500 7 ARG A 12 0.24 SIDE CHAIN
REMARK 500 7 ARG A 14 0.31 SIDE CHAIN
REMARK 500 8 ARG A 12 0.30 SIDE CHAIN
REMARK 500 8 ARG A 14 0.28 SIDE CHAIN
REMARK 500 9 ARG A 12 0.23 SIDE CHAIN
REMARK 500 9 ARG A 14 0.32 SIDE CHAIN
REMARK 500 10 ARG A 12 0.26 SIDE CHAIN
REMARK 500 10 ARG A 14 0.31 SIDE CHAIN
REMARK 500 11 ARG A 12 0.09 SIDE CHAIN
REMARK 500 11 ARG A 14 0.32 SIDE CHAIN
REMARK 500 12 ARG A 12 0.32 SIDE CHAIN
REMARK 500 12 ARG A 14 0.30 SIDE CHAIN
REMARK 500 13 ARG A 12 0.32 SIDE CHAIN
REMARK 500 13 ARG A 14 0.31 SIDE CHAIN
REMARK 500 14 ARG A 12 0.22 SIDE CHAIN
REMARK 500 14 ARG A 14 0.31 SIDE CHAIN
REMARK 500 15 ARG A 12 0.32 SIDE CHAIN
REMARK 500 15 ARG A 14 0.28 SIDE CHAIN
REMARK 500 16 ARG A 12 0.28 SIDE CHAIN
REMARK 500 16 ARG A 14 0.31 SIDE CHAIN
REMARK 500 17 ARG A 12 0.22 SIDE CHAIN
REMARK 500 17 ARG A 14 0.25 SIDE CHAIN
REMARK 500 18 ARG A 12 0.32 SIDE CHAIN
REMARK 500 18 ARG A 14 0.31 SIDE CHAIN
REMARK 500 19 ARG A 12 0.28 SIDE CHAIN
REMARK 500 19 ARG A 14 0.31 SIDE CHAIN
REMARK 500 20 ARG A 12 0.25 SIDE CHAIN
REMARK 500 20 ARG A 14 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1APF A 1 49 UNP P01531 TXAB_ANTXA 1 49
SEQRES 1 A 49 GLY VAL PRO CYS LEU CYS ASP SER ASP GLY PRO ARG PRO
SEQRES 2 A 49 ARG GLY ASN THR LEU SER GLY ILE LEU TRP PHE TYR PRO
SEQRES 3 A 49 SER GLY CYS PRO SER GLY TRP HIS ASN CYS LYS ALA HIS
SEQRES 4 A 49 GLY PRO ASN ILE GLY TRP CYS CYS LYS LYS
SHEET 1 A 4 VAL A 2 CYS A 4 0
SHEET 2 A 4 GLY A 20 TRP A 23 -1 N LEU A 22 O VAL A 2
SHEET 3 A 4 TRP A 45 LYS A 48 -1 N TRP A 45 O TRP A 23
SHEET 4 A 4 HIS A 34 LYS A 37 -1 N HIS A 34 O LYS A 48
SSBOND 1 CYS A 4 CYS A 46 1555 1555 2.03
SSBOND 2 CYS A 6 CYS A 36 1555 1555 2.02
SSBOND 3 CYS A 29 CYS A 47 1555 1555 2.02
CISPEP 1 GLY A 40 PRO A 41 1 -1.87
CISPEP 2 GLY A 40 PRO A 41 2 -5.18
CISPEP 3 GLY A 40 PRO A 41 3 -2.41
CISPEP 4 GLY A 40 PRO A 41 4 2.50
CISPEP 5 GLY A 40 PRO A 41 5 -4.60
CISPEP 6 GLY A 40 PRO A 41 6 1.10
CISPEP 7 GLY A 40 PRO A 41 7 -2.40
CISPEP 8 GLY A 40 PRO A 41 8 0.87
CISPEP 9 GLY A 40 PRO A 41 9 -4.18
CISPEP 10 GLY A 40 PRO A 41 10 1.66
CISPEP 11 GLY A 40 PRO A 41 11 -5.50
CISPEP 12 GLY A 40 PRO A 41 12 -5.06
CISPEP 13 GLY A 40 PRO A 41 13 -4.06
CISPEP 14 GLY A 40 PRO A 41 14 -1.55
CISPEP 15 GLY A 40 PRO A 41 15 -1.40
CISPEP 16 GLY A 40 PRO A 41 16 -0.68
CISPEP 17 GLY A 40 PRO A 41 17 1.50
CISPEP 18 GLY A 40 PRO A 41 18 -1.67
CISPEP 19 GLY A 40 PRO A 41 19 -5.50
CISPEP 20 GLY A 40 PRO A 41 20 1.45
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 - v 29 2 Bytes