Header list of 1ng7.pdb file
Complete list - b 23 2 Bytes
HEADER VIRAL PROTEIN 16-DEC-02 1NG7
TITLE THE SOLUTION STRUCTURE OF THE SOLUBLE DOMAIN OF POLIOVIRUS 3A PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENOME POLYPROTEIN [CORE PROTEIN P3A];
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: POLIOVIRUS 3A-N;
COMPND 5 SYNONYM: POLIOVIRUS 3A-N;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN POLIOVIRUS 1;
SOURCE 3 ORGANISM_TAXID: 12080;
SOURCE 4 GENE: 3A;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET 21A
KEYWDS HELICAL HAIRPIN, UNFOLDED DOMAIN, SYMMETRIC DIMER, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR D.M.STRAUSS,L.W.GLUSTROM,D.S.WUTTKE
REVDAT 3 23-FEB-22 1NG7 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1NG7 1 VERSN
REVDAT 1 15-JUL-03 1NG7 0
JRNL AUTH D.M.STRAUSS,L.W.GLUSTROM,D.S.WUTTKE
JRNL TITL TOWARDS AN UNDERSTANDING OF THE POLIOVIRUS REPLICATION
JRNL TITL 2 COMPLEX: THE SOLUTION STRUCTURE OF THE SOLUBLE DOMAIN OF THE
JRNL TITL 3 POLIOVIRUS 3A PROTEIN.
JRNL REF J.MOL.BIOL. V. 330 225 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12823963
JRNL DOI 10.1016/S0022-2836(03)00577-1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1A, X-PLOR 3.851
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 866 INTRAMONOMER AND 46
REMARK 3 INTERMONOMER NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS AND 34 TALOS-DERIVED DIHEDRAL ANGLE
REMARK 3 RESTRAINTS.
REMARK 3 THE MONOMER STRUCTURE WAS CALCULATED FIRST AND THEN THE DIMER WAS
REMARK 3 BUILT FROM RANDOM MONOMER STARTING ORIENTATIONS.
REMARK 4
REMARK 4 1NG7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000017847.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 25; 25
REMARK 210 PH : 7.0; 7.0
REMARK 210 IONIC STRENGTH : 20 MM POTASSIUM PHOSPHATE, 50 MM
REMARK 210 NACL; 10 MM TRIS, 50 MM NACL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1-3 MM 3A-N U-95% 13C;U-99% 15N;
REMARK 210 20MM PHOSPHATE BUFFER NA; 100%
REMARK 210 D2O; 1-3 MM 3A-N U-99% 15N; 20MM
REMARK 210 PHOSPHATE BUFFER NA; 95% H2O, 5%
REMARK 210 D2O; 1.5 MM 3A-N NA; 1.5 MM 3A-N
REMARK 210 U-95% 13C;U-99% 15N; 20MM
REMARK 210 PHOSPHATE BUFFER NA; 100% D2O; 2
REMARK 210 MM 3A-N U-99% 15N; 10 MM TRIS
REMARK 210 BUFFER NA; 95% H2O, 5% D2O; 1-3
REMARK 210 MM 3A-N U-95% 13C;U-99% 15N;
REMARK 210 20MM PHOSPHATE BUFFER NA; 95%
REMARK 210 H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 2D
REMARK 210 NOESY; 3D_15N-SEPARATED_NOESY;
REMARK 210 3D_13C-SEPARATED SELECT/FILTER
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.0, ANSIG 3.3
REMARK 210 METHOD USED : DISTANCE GEOMETRY/SIMMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : 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 : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D
REMARK 210 HETERONUCLEAR TECHNIQUES.
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 O ILE A 22 H LEU A 26 1.39
REMARK 500 O ILE B 22 H LEU B 26 1.40
REMARK 500 O GLN A 32 H ASP A 36 1.42
REMARK 500 O GLN B 32 H ASP B 36 1.44
REMARK 500 O PRO B 19 H CYS B 21 1.50
REMARK 500 O PRO A 19 H CYS A 21 1.51
REMARK 500 O SER A 31 H VAL A 34 1.58
REMARK 500 O SER B 31 H VAL B 34 1.58
REMARK 500 O TYR B 37 H LYS B 41 1.58
REMARK 500 O TYR A 37 H LYS A 41 1.59
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 SER A 31 N - CA - CB ANGL. DEV. = -10.3 DEGREES
REMARK 500 1 SER B 31 N - CA - CB ANGL. DEV. = -10.4 DEGREES
REMARK 500 2 SER A 31 N - CA - CB ANGL. DEV. = -10.3 DEGREES
REMARK 500 2 SER B 31 N - CA - CB ANGL. DEV. = -10.3 DEGREES
REMARK 500 3 SER A 31 N - CA - CB ANGL. DEV. = -10.0 DEGREES
REMARK 500 3 SER B 31 N - CA - CB ANGL. DEV. = -10.3 DEGREES
REMARK 500 4 SER A 31 N - CA - CB ANGL. DEV. = -10.3 DEGREES
REMARK 500 4 SER B 31 N - CA - CB ANGL. DEV. = -10.4 DEGREES
REMARK 500 5 SER A 31 N - CA - CB ANGL. DEV. = -10.4 DEGREES
REMARK 500 5 SER B 31 N - CA - CB ANGL. DEV. = -10.0 DEGREES
REMARK 500 6 SER A 31 N - CA - CB ANGL. DEV. = -10.3 DEGREES
REMARK 500 6 SER B 31 N - CA - CB ANGL. DEV. = -10.4 DEGREES
REMARK 500 7 SER A 31 N - CA - CB ANGL. DEV. = -10.3 DEGREES
REMARK 500 7 SER B 31 N - CA - CB ANGL. DEV. = -10.3 DEGREES
REMARK 500 8 SER A 31 N - CA - CB ANGL. DEV. = -10.4 DEGREES
REMARK 500 8 SER B 31 N - CA - CB ANGL. DEV. = -10.2 DEGREES
REMARK 500 9 SER A 31 N - CA - CB ANGL. DEV. = -10.1 DEGREES
REMARK 500 9 SER B 31 N - CA - CB ANGL. DEV. = -9.2 DEGREES
REMARK 500 10 SER A 31 N - CA - CB ANGL. DEV. = -10.2 DEGREES
REMARK 500 10 SER B 31 N - CA - CB ANGL. DEV. = -10.5 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 LEU A 4 -151.45 -165.99
REMARK 500 1 GLN A 5 45.49 -87.16
REMARK 500 1 TYR A 6 110.20 -37.16
REMARK 500 1 ASP A 8 95.56 47.53
REMARK 500 1 LYS A 10 23.03 -143.44
REMARK 500 1 ILE A 11 -136.64 -124.99
REMARK 500 1 ASP A 12 -51.34 -164.29
REMARK 500 1 ILE A 13 -179.92 59.24
REMARK 500 1 SER A 16 -122.80 -60.99
REMARK 500 1 GLU A 20 54.85 -55.37
REMARK 500 1 ASP A 30 92.41 45.35
REMARK 500 1 SER A 31 66.34 -166.41
REMARK 500 1 ILE A 44 15.08 84.05
REMARK 500 1 VAL A 45 110.52 -31.86
REMARK 500 1 ASN A 46 110.66 179.39
REMARK 500 1 SER A 49 -67.61 -104.63
REMARK 500 1 GLN A 50 37.46 -149.81
REMARK 500 1 GLN A 52 55.89 -154.12
REMARK 500 1 GLU A 54 74.14 48.03
REMARK 500 1 ARG A 55 -159.37 -72.89
REMARK 500 1 ILE A 57 -178.09 -53.73
REMARK 500 1 TYR B 6 86.41 43.84
REMARK 500 1 LYS B 7 -161.77 -167.74
REMARK 500 1 LYS B 10 41.23 -147.07
REMARK 500 1 ILE B 11 -136.99 -123.20
REMARK 500 1 ASP B 12 -80.78 171.09
REMARK 500 1 LYS B 14 -79.85 177.60
REMARK 500 1 SER B 16 -124.12 -61.97
REMARK 500 1 GLU B 20 54.72 -55.89
REMARK 500 1 ASP B 30 92.86 46.37
REMARK 500 1 SER B 31 66.89 -165.61
REMARK 500 1 ILE B 44 13.75 82.98
REMARK 500 1 VAL B 45 101.98 -29.20
REMARK 500 1 ASN B 46 -54.48 179.18
REMARK 500 1 SER B 49 -73.73 -118.48
REMARK 500 1 ARG B 55 78.19 -109.59
REMARK 500 2 TYR A 6 -172.00 47.02
REMARK 500 2 ASP A 8 -170.48 59.61
REMARK 500 2 ILE A 11 -121.93 -126.21
REMARK 500 2 ASP A 12 -126.45 40.37
REMARK 500 2 SER A 16 -122.92 -61.44
REMARK 500 2 GLU A 20 54.93 -54.87
REMARK 500 2 ASP A 30 92.34 45.02
REMARK 500 2 SER A 31 66.36 -166.27
REMARK 500 2 ILE A 44 13.64 83.16
REMARK 500 2 VAL A 45 103.97 -27.64
REMARK 500 2 GLN A 50 103.02 67.47
REMARK 500 2 GLN A 52 41.69 -87.77
REMARK 500 2 THR A 53 102.97 -44.91
REMARK 500 2 ILE A 57 91.00 59.43
REMARK 500
REMARK 500 THIS ENTRY HAS 379 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 59 0.31 SIDE CHAIN
REMARK 500 1 ARG B 35 0.08 SIDE CHAIN
REMARK 500 1 ARG B 55 0.30 SIDE CHAIN
REMARK 500 1 ARG B 59 0.25 SIDE CHAIN
REMARK 500 2 ARG A 35 0.08 SIDE CHAIN
REMARK 500 2 ARG A 55 0.18 SIDE CHAIN
REMARK 500 2 ARG A 59 0.29 SIDE CHAIN
REMARK 500 2 ARG B 35 0.08 SIDE CHAIN
REMARK 500 2 ARG B 55 0.31 SIDE CHAIN
REMARK 500 2 ARG B 59 0.19 SIDE CHAIN
REMARK 500 3 ARG A 35 0.17 SIDE CHAIN
REMARK 500 3 ARG A 55 0.24 SIDE CHAIN
REMARK 500 3 ARG A 59 0.31 SIDE CHAIN
REMARK 500 3 ARG B 35 0.17 SIDE CHAIN
REMARK 500 3 ARG B 55 0.17 SIDE CHAIN
REMARK 500 3 ARG B 59 0.10 SIDE CHAIN
REMARK 500 4 ARG A 35 0.16 SIDE CHAIN
REMARK 500 4 ARG A 55 0.32 SIDE CHAIN
REMARK 500 4 ARG A 59 0.24 SIDE CHAIN
REMARK 500 4 ARG B 35 0.17 SIDE CHAIN
REMARK 500 4 ARG B 55 0.26 SIDE CHAIN
REMARK 500 4 ARG B 59 0.30 SIDE CHAIN
REMARK 500 5 ARG A 35 0.14 SIDE CHAIN
REMARK 500 5 ARG A 55 0.19 SIDE CHAIN
REMARK 500 5 ARG A 59 0.20 SIDE CHAIN
REMARK 500 5 ARG B 35 0.12 SIDE CHAIN
REMARK 500 5 ARG B 55 0.31 SIDE CHAIN
REMARK 500 5 ARG B 59 0.31 SIDE CHAIN
REMARK 500 6 ARG A 35 0.24 SIDE CHAIN
REMARK 500 6 ARG A 55 0.26 SIDE CHAIN
REMARK 500 6 ARG A 59 0.21 SIDE CHAIN
REMARK 500 6 ARG B 35 0.23 SIDE CHAIN
REMARK 500 6 ARG B 55 0.26 SIDE CHAIN
REMARK 500 6 ARG B 59 0.31 SIDE CHAIN
REMARK 500 7 ARG A 55 0.25 SIDE CHAIN
REMARK 500 7 ARG A 59 0.31 SIDE CHAIN
REMARK 500 7 ARG B 55 0.31 SIDE CHAIN
REMARK 500 7 ARG B 59 0.21 SIDE CHAIN
REMARK 500 8 ARG A 35 0.27 SIDE CHAIN
REMARK 500 8 ARG A 55 0.21 SIDE CHAIN
REMARK 500 8 ARG A 59 0.32 SIDE CHAIN
REMARK 500 8 ARG B 35 0.26 SIDE CHAIN
REMARK 500 8 ARG B 55 0.19 SIDE CHAIN
REMARK 500 8 ARG B 59 0.28 SIDE CHAIN
REMARK 500 9 ARG A 35 0.17 SIDE CHAIN
REMARK 500 9 ARG A 55 0.18 SIDE CHAIN
REMARK 500 9 ARG A 59 0.22 SIDE CHAIN
REMARK 500 9 ARG B 35 0.19 SIDE CHAIN
REMARK 500 9 ARG B 55 0.28 SIDE CHAIN
REMARK 500 9 ARG B 59 0.30 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 54 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1NG7 A 2 60 UNP P03300 POLH_POL1M 1456 1514
DBREF 1NG7 B 2 60 UNP P03300 POLH_POL1M 1456 1514
SEQADV 1NG7 MET A 1 UNP P03300 CLONING ARTIFACT
SEQADV 1NG7 MET B 1 UNP P03300 CLONING ARTIFACT
SEQRES 1 A 60 MET GLY PRO LEU GLN TYR LYS ASP LEU LYS ILE ASP ILE
SEQRES 2 A 60 LYS THR SER PRO PRO PRO GLU CYS ILE ASN ASP LEU LEU
SEQRES 3 A 60 GLN ALA VAL ASP SER GLN GLU VAL ARG ASP TYR CYS GLU
SEQRES 4 A 60 LYS LYS GLY TRP ILE VAL ASN ILE THR SER GLN VAL GLN
SEQRES 5 A 60 THR GLU ARG ASN ILE ASN ARG ALA
SEQRES 1 B 60 MET GLY PRO LEU GLN TYR LYS ASP LEU LYS ILE ASP ILE
SEQRES 2 B 60 LYS THR SER PRO PRO PRO GLU CYS ILE ASN ASP LEU LEU
SEQRES 3 B 60 GLN ALA VAL ASP SER GLN GLU VAL ARG ASP TYR CYS GLU
SEQRES 4 B 60 LYS LYS GLY TRP ILE VAL ASN ILE THR SER GLN VAL GLN
SEQRES 5 B 60 THR GLU ARG ASN ILE ASN ARG ALA
HELIX 1 1 ILE A 22 ASP A 30 1 9
HELIX 2 2 SER A 31 GLY A 42 1 12
HELIX 3 3 ILE B 22 ASP B 30 1 9
HELIX 4 4 SER B 31 GLY B 42 1 12
CISPEP 1 SER A 16 PRO A 17 1 0.59
CISPEP 2 SER B 16 PRO B 17 1 0.74
CISPEP 3 SER A 16 PRO A 17 2 0.34
CISPEP 4 SER B 16 PRO B 17 2 0.76
CISPEP 5 SER A 16 PRO A 17 3 0.74
CISPEP 6 SER B 16 PRO B 17 3 0.56
CISPEP 7 SER A 16 PRO A 17 4 0.76
CISPEP 8 SER B 16 PRO B 17 4 0.54
CISPEP 9 SER A 16 PRO A 17 5 0.87
CISPEP 10 SER B 16 PRO B 17 5 0.89
CISPEP 11 SER A 16 PRO A 17 6 0.54
CISPEP 12 SER B 16 PRO B 17 6 0.35
CISPEP 13 SER A 16 PRO A 17 7 0.64
CISPEP 14 SER B 16 PRO B 17 7 0.50
CISPEP 15 SER A 16 PRO A 17 8 0.83
CISPEP 16 SER B 16 PRO B 17 8 0.42
CISPEP 17 SER A 16 PRO A 17 9 0.53
CISPEP 18 SER B 16 PRO B 17 9 0.56
CISPEP 19 SER A 16 PRO A 17 10 0.96
CISPEP 20 SER B 16 PRO B 17 10 0.42
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 23 2 Bytes