Header list of 1bon.pdb file
Complete list - 25 20 Bytes
HEADER HORMONE 21-JUL-94 1BON
TITLE THREE-DIMENSIONAL STRUCTURE OF BOMBYXIN-II, AN INSULIN-RELATED BRAIN-
TITLE 2 SECRETORY PEPTIDE OF THE SILKMOTH BOMBYX MORI: COMPARISON WITH
TITLE 3 INSULIN AND RELAXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BOMBYXIN-II,BOMBYXIN A-2;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: BOMBYXIN-II,BOMBYXIN A-6;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOMBYX MORI;
SOURCE 3 ORGANISM_COMMON: DOMESTIC SILKWORM;
SOURCE 4 ORGANISM_TAXID: 7091;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: BOMBYX MORI;
SOURCE 7 ORGANISM_COMMON: DOMESTIC SILKWORM;
SOURCE 8 ORGANISM_TAXID: 7091
KEYWDS HORMONE, STRUCTURAL PROTEOMICS IN EUROPE, SPINE, STRUCTURAL GENOMICS
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR K.NAGATA,H.HATANAKA,D.KOHDA,F.INAGAKI,STRUCTURAL PROTEOMICS IN EUROPE
AUTHOR 2 (SPINE)
REVDAT 3 25-DEC-19 1BON 1 REMARK SEQRES LINK
REVDAT 2 24-FEB-09 1BON 1 VERSN
REVDAT 1 26-JAN-95 1BON 0
JRNL AUTH K.NAGATA,H.HATANAKA,D.KOHDA,H.KATAOKA,H.NAGASAWA,A.ISOGAI,
JRNL AUTH 2 H.ISHIZAKI,A.SUZUKI,F.INAGAKI
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF BOMBYXIN-II AN
JRNL TITL 2 INSULIN-LIKE PEPTIDE OF THE SILKMOTH BOMBYX MORI: STRUCTURAL
JRNL TITL 3 COMPARISON WITH INSULIN AND RELAXIN.
JRNL REF J.MOL.BIOL. V. 253 749 1995
JRNL REFN ISSN 0022-2836
JRNL PMID 7473749
JRNL DOI 10.1006/JMBI.1995.0588
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: NULL
REMARK 4
REMARK 4 1BON 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_1000171967.
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 : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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: 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 H CYS A 11 H SER A 12 1.26
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 B 4 CG HIS B 4 ND1 -0.102
REMARK 500 1 HIS B 10 CG HIS B 10 ND1 -0.099
REMARK 500 2 HIS B 4 CG HIS B 4 ND1 -0.104
REMARK 500 2 HIS B 10 CG HIS B 10 ND1 -0.105
REMARK 500 2 TRP B 20 CG TRP B 20 CD2 -0.108
REMARK 500 3 HIS B 4 CG HIS B 4 ND1 -0.103
REMARK 500 3 HIS B 10 CG HIS B 10 ND1 -0.100
REMARK 500 4 HIS B 4 CG HIS B 4 ND1 -0.100
REMARK 500 4 HIS B 10 CG HIS B 10 ND1 -0.101
REMARK 500 5 HIS B 4 CG HIS B 4 ND1 -0.104
REMARK 500 5 HIS B 10 CG HIS B 10 ND1 -0.101
REMARK 500 6 HIS B 4 CG HIS B 4 ND1 -0.102
REMARK 500 6 HIS B 10 CG HIS B 10 ND1 -0.097
REMARK 500 7 HIS B 4 CG HIS B 4 ND1 -0.101
REMARK 500 7 HIS B 10 CG HIS B 10 ND1 -0.100
REMARK 500 8 HIS B 4 CG HIS B 4 ND1 -0.101
REMARK 500 8 HIS B 10 CG HIS B 10 ND1 -0.108
REMARK 500 9 HIS B 4 CG HIS B 4 ND1 -0.103
REMARK 500 9 HIS B 10 CG HIS B 10 ND1 -0.102
REMARK 500 10 HIS B 4 CG HIS B 4 ND1 -0.103
REMARK 500 10 HIS B 10 CG HIS B 10 ND1 -0.100
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 TRP B 20 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 1 TRP B 20 CD1 - NE1 - CE2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 1 TRP B 20 NE1 - CE2 - CZ2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 1 TRP B 20 NE1 - CE2 - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 2 TRP B 20 CG - CD1 - NE1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 2 TRP B 20 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 2 TRP B 20 NE1 - CE2 - CZ2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 2 TRP B 20 NE1 - CE2 - CD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 3 TRP B 20 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 3 TRP B 20 CD1 - NE1 - CE2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 3 TRP B 20 NE1 - CE2 - CZ2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 4 TRP B 20 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 4 TRP B 20 CD1 - NE1 - CE2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 4 TRP B 20 NE1 - CE2 - CZ2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 4 TRP B 20 NE1 - CE2 - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 5 TRP B 20 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 5 TRP B 20 CD1 - NE1 - CE2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 5 TRP B 20 NE1 - CE2 - CZ2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 5 TRP B 20 NE1 - CE2 - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 6 HIS B 4 CA - CB - CG ANGL. DEV. = -10.4 DEGREES
REMARK 500 6 TRP B 20 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 6 TRP B 20 CD1 - NE1 - CE2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 6 TRP B 20 NE1 - CE2 - CZ2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 6 TRP B 20 NE1 - CE2 - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 7 TRP B 20 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 7 TRP B 20 CD1 - NE1 - CE2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 7 TRP B 20 NE1 - CE2 - CZ2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 7 TRP B 20 NE1 - CE2 - CD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 8 TRP B 20 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 8 TRP B 20 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 8 TRP B 20 NE1 - CE2 - CZ2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 8 TRP B 20 NE1 - CE2 - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 9 TRP B 20 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 9 TRP B 20 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 9 TRP B 20 NE1 - CE2 - CZ2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 10 TRP B 20 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 10 TRP B 20 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 10 TRP B 20 NE1 - CE2 - CZ2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 10 TRP B 20 NE1 - CE2 - CD2 ANGL. DEV. = -6.3 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 PRO A 10 174.18 -43.26
REMARK 500 1 CYS A 11 18.84 -179.40
REMARK 500 1 SER A 12 137.31 -35.43
REMARK 500 1 VAL A 13 -51.76 -13.28
REMARK 500 1 ASP A 14 13.99 -62.87
REMARK 500 1 VAL A 15 -31.36 -131.85
REMARK 500 1 GLN B -1 59.54 -149.72
REMARK 500 1 PRO B 0 -151.05 -85.98
REMARK 500 1 GLN B 1 39.97 -154.02
REMARK 500 1 ALA B 2 -102.42 -85.94
REMARK 500 1 HIS B 4 35.23 -70.39
REMARK 500 1 THR B 5 153.73 -44.99
REMARK 500 1 TYR B 6 -153.39 -92.97
REMARK 500 1 CYS B 7 108.24 -171.47
REMARK 500 1 ARG B 9 -67.86 62.48
REMARK 500 1 HIS B 10 -9.68 -55.04
REMARK 500 1 VAL B 24 -15.40 -45.37
REMARK 500 2 PRO A 10 167.83 -36.54
REMARK 500 2 CYS A 11 13.14 -164.53
REMARK 500 2 SER A 12 129.72 -34.39
REMARK 500 2 VAL A 13 -52.64 -11.63
REMARK 500 2 ASP A 14 0.48 -56.19
REMARK 500 2 PRO B 0 -152.26 -84.33
REMARK 500 2 ALA B 2 111.11 168.39
REMARK 500 2 HIS B 4 86.76 -36.02
REMARK 500 2 TYR B 6 -154.35 -101.08
REMARK 500 2 CYS B 7 117.10 -174.80
REMARK 500 2 ARG B 9 -55.66 62.02
REMARK 500 2 HIS B 10 -3.95 -55.01
REMARK 500 2 VAL B 24 -20.28 -39.91
REMARK 500 3 ASP A 4 25.02 -78.54
REMARK 500 3 GLU A 5 -34.91 -136.29
REMARK 500 3 PRO A 10 -179.74 -44.01
REMARK 500 3 CYS A 11 21.94 176.84
REMARK 500 3 SER A 12 136.37 -32.51
REMARK 500 3 VAL A 13 -52.90 -9.61
REMARK 500 3 ASP A 14 13.08 -61.25
REMARK 500 3 PRO B 0 -153.22 -71.02
REMARK 500 3 GLN B 1 -73.48 -74.80
REMARK 500 3 ALA B 2 94.22 175.51
REMARK 500 3 HIS B 4 75.02 -66.25
REMARK 500 3 ARG B 9 -76.76 57.81
REMARK 500 3 HIS B 10 -18.30 -47.53
REMARK 500 4 PRO A 10 164.84 -37.58
REMARK 500 4 CYS A 11 22.50 -159.14
REMARK 500 4 SER A 12 131.69 -31.19
REMARK 500 4 VAL A 13 -53.78 -3.71
REMARK 500 4 GLN B -1 75.10 48.38
REMARK 500 4 PRO B 0 -148.03 -77.42
REMARK 500 4 ALA B 2 -74.49 -0.51
REMARK 500
REMARK 500 THIS ENTRY HAS 136 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 9 0.18 SIDE CHAIN
REMARK 500 1 ARG B 9 0.23 SIDE CHAIN
REMARK 500 1 ARG B 13 0.28 SIDE CHAIN
REMARK 500 2 ARG B 9 0.28 SIDE CHAIN
REMARK 500 3 ARG A 9 0.19 SIDE CHAIN
REMARK 500 3 ARG B 9 0.18 SIDE CHAIN
REMARK 500 3 ARG B 13 0.27 SIDE CHAIN
REMARK 500 4 ARG A 9 0.22 SIDE CHAIN
REMARK 500 4 ARG B 9 0.28 SIDE CHAIN
REMARK 500 4 ARG B 13 0.31 SIDE CHAIN
REMARK 500 5 ARG A 9 0.26 SIDE CHAIN
REMARK 500 5 ARG B 9 0.28 SIDE CHAIN
REMARK 500 5 ARG B 13 0.09 SIDE CHAIN
REMARK 500 6 ARG A 9 0.28 SIDE CHAIN
REMARK 500 6 TYR B 6 0.06 SIDE CHAIN
REMARK 500 6 ARG B 9 0.28 SIDE CHAIN
REMARK 500 6 ARG B 13 0.27 SIDE CHAIN
REMARK 500 7 ARG A 9 0.09 SIDE CHAIN
REMARK 500 7 ARG B 9 0.28 SIDE CHAIN
REMARK 500 7 ARG B 13 0.23 SIDE CHAIN
REMARK 500 8 ARG A 9 0.29 SIDE CHAIN
REMARK 500 8 ARG B 9 0.15 SIDE CHAIN
REMARK 500 8 ARG B 13 0.23 SIDE CHAIN
REMARK 500 9 ARG A 9 0.30 SIDE CHAIN
REMARK 500 9 ARG B 9 0.32 SIDE CHAIN
REMARK 500 9 ARG B 13 0.32 SIDE CHAIN
REMARK 500 10 ARG A 9 0.23 SIDE CHAIN
REMARK 500 10 ARG B 9 0.26 SIDE CHAIN
REMARK 500 10 ARG B 13 0.25 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BOM RELATED DB: PDB
DBREF 1BON A 1 20 UNP P15411 BXA2_BOMMO 70 89
DBREF 1BON B -1 25 UNP P26729 BXA6_BOMMO 20 47
SEQRES 1 A 20 GLY ILE VAL ASP GLU CYS CYS LEU ARG PRO CYS SER VAL
SEQRES 2 A 20 ASP VAL LEU LEU SER TYR CYS
SEQRES 1 B 28 PCA GLN PRO GLN ALA VAL HIS THR TYR CYS GLY ARG HIS
SEQRES 2 B 28 LEU ALA ARG THR LEU ALA ASP LEU CYS TRP GLU ALA GLY
SEQRES 3 B 28 VAL ASP
MODRES 1BON PCA B -2 GLN PYROGLUTAMIC ACID
HET PCA B -2 14
HETNAM PCA PYROGLUTAMIC ACID
FORMUL 2 PCA C5 H7 N O3
HELIX 1 H1 ILE A 2 LEU A 8 1 7
HELIX 2 H2 VAL A 13 TYR A 19 1 7
HELIX 3 H3 ARG B 9 ALA B 22 1 14
SSBOND 1 CYS A 6 CYS A 11 1555 1555 2.02
SSBOND 2 CYS A 7 CYS B 7 1555 1555 2.02
SSBOND 3 CYS A 20 CYS B 19 1555 1555 2.02
LINK C PCA B -2 N GLN B -1 1555 1555 1.31
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 - 25 20 Bytes