Header list of 1jnj.pdb file
Complete list - b 23 2 Bytes
HEADER IMMUNE SYSTEM 24-JUL-01 1JNJ
TITLE NMR SOLUTION STRUCTURE OF THE HUMAN BETA2-MICROGLOBULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA2-MICROGLOBULIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: B2M;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHN1
KEYWDS IMMUNOGLOBULIN CONSTANT DOMAIN, IMMUNE SYSTEM
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.VERDONE,A.CORAZZA,P.VIGLINO,F.PETTIROSSI,S.GIORGETTI,P.MANGIONE,
AUTHOR 2 A.ANDREOLA,M.STOPPINI,V.BELLOTTI,G.ESPOSITO
REVDAT 3 23-FEB-22 1JNJ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1JNJ 1 VERSN
REVDAT 1 27-FEB-02 1JNJ 0
JRNL AUTH G.VERDONE,A.CORAZZA,P.VIGLINO,F.PETTIROSSI,S.GIORGETTI,
JRNL AUTH 2 P.MANGIONE,A.ANDREOLA,M.STOPPINI,V.BELLOTTI,G.ESPOSITO
JRNL TITL THE SOLUTION STRUCTURE OF HUMAN BETA2-MICROGLOBULIN REVEALS
JRNL TITL 2 THE PRODROMES OF ITS AMYLOID TRANSITION.
JRNL REF PROTEIN SCI. V. 11 487 2002
JRNL REFN ISSN 0961-8368
JRNL PMID 11847272
JRNL DOI 10.1110/PS.29002
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.ESPOSITO,R.MICHELUTTI,G.VERDONE,P.VIGLINO,H.HERNANDEZ,
REMARK 1 AUTH 2 C.V.ROBINSON,A.AMORESANO,F.DAL PIAZ,M.MONTI,P.PUCCI,
REMARK 1 AUTH 3 P.MANGIONE,M.STOPPINI,G.MERLINI,G.FERRI,V.BELLOTTI
REMARK 1 TITL REMOVAL OF THE N-TERMINAL HEXAPEPTIDE FROM HUMAN
REMARK 1 TITL 2 BETA2-MICROGLOBULIN FACILITATES PROTEIN AGGREGATION AND
REMARK 1 TITL 3 FIBRIL FORMATION
REMARK 1 REF PROTEIN SCI. V. 9 831 2000
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH V.BELLOTTI,M.STOPPINI,P.MANGIONE,M.SUNDE,C.V.ROBINSON,
REMARK 1 AUTH 2 L.ASTI,D.BRANCACCIO,G.FERRI
REMARK 1 TITL BETA2-MICROGLOBULIN CAN BE REFOLDED INTO A NATIVE STATE FROM
REMARK 1 TITL 2 EX VIVO AMYLOID FIBRILS.
REMARK 1 REF EUR.J.BIOCHEM. V. 258 61 1998
REMARK 1 REFN ISSN 0014-2956
REMARK 1 DOI 10.1046/J.1432-1327.1998.2580061.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, DISCOVER 2000
REMARK 3 AUTHORS : BRUKER (XWINNMR), MSI (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1608 RESTRAINTS, 1541 ARE NOE-DERIVED DISTANCE CONTRAINTS, 67
REMARK 3 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1JNJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000013974.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310; 310
REMARK 210 PH : 6.4; 6.4
REMARK 210 IONIC STRENGTH : 100 MM NACL, 70 MM PHOSPHATE
REMARK 210 BUFFER; 100 MM NACL, 70 MM
REMARK 210 PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.68 MM BETA2-M; 70 MM PHOSPHATE
REMARK 210 BUFFER NA, 100 MM NACL.; 0.37 MM
REMARK 210 BETA2-M; 70 MM PHOSPHATE BUFFER
REMARK 210 NA, 100 MM NACL.
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000, DIANA 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING, RESTRAINED
REMARK 210 MOLECULAR DYNAMICS, RESTRAINED
REMARK 210 MOLECULAR MECHANICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 380
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR 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: 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 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 5 TYR A 63 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 18 TYR A 63 CB - CG - CD1 ANGL. DEV. = -3.7 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 GLN A 2 71.96 -114.15
REMARK 500 1 ASN A 21 -147.85 -118.32
REMARK 500 1 LYS A 41 -133.08 -81.91
REMARK 500 1 ASP A 53 170.69 66.29
REMARK 500 1 SER A 57 19.29 52.81
REMARK 500 1 LYS A 58 41.75 21.71
REMARK 500 1 ASP A 59 -109.72 -108.44
REMARK 500 1 GLU A 74 -93.72 55.62
REMARK 500 1 ASN A 83 76.08 -151.91
REMARK 500 1 TRP A 95 -86.13 -62.97
REMARK 500 1 ASP A 96 177.87 165.54
REMARK 500 2 ILE A 1 13.04 -144.73
REMARK 500 2 ASN A 21 -154.35 -127.51
REMARK 500 2 HIS A 31 143.81 -174.85
REMARK 500 2 PRO A 32 -151.74 -85.43
REMARK 500 2 LYS A 41 -140.55 -79.07
REMARK 500 2 SER A 55 64.12 -113.97
REMARK 500 2 ASP A 59 -85.57 -66.96
REMARK 500 2 TRP A 60 63.81 -172.20
REMARK 500 2 GLU A 74 -100.71 43.41
REMARK 500 2 SER A 88 -41.71 71.99
REMARK 500 2 TRP A 95 -98.71 -76.94
REMARK 500 2 ASP A 96 -171.94 170.69
REMARK 500 2 ARG A 97 -61.92 -160.90
REMARK 500 2 ASP A 98 62.24 -154.93
REMARK 500 3 ILE A 1 173.62 -56.54
REMARK 500 3 ALA A 15 141.98 64.14
REMARK 500 3 ASN A 21 -149.73 -120.63
REMARK 500 3 HIS A 31 145.16 -171.75
REMARK 500 3 PRO A 32 -149.43 -87.31
REMARK 500 3 LYS A 41 -138.78 -79.60
REMARK 500 3 SER A 57 -150.44 51.64
REMARK 500 3 PHE A 62 124.54 -170.54
REMARK 500 3 GLU A 74 -93.51 59.68
REMARK 500 3 SER A 88 -38.94 72.45
REMARK 500 3 LYS A 94 85.67 43.11
REMARK 500 3 TRP A 95 111.18 -31.93
REMARK 500 4 ALA A 15 -175.27 59.02
REMARK 500 4 GLU A 16 -162.21 -167.85
REMARK 500 4 ASN A 21 -145.55 -114.74
REMARK 500 4 HIS A 31 148.14 -171.53
REMARK 500 4 PRO A 32 -158.29 -84.17
REMARK 500 4 LYS A 41 -142.23 -82.16
REMARK 500 4 ASP A 53 -78.30 -8.51
REMARK 500 4 LYS A 58 41.87 24.76
REMARK 500 4 GLU A 74 -91.87 59.84
REMARK 500 4 SER A 88 -43.00 75.08
REMARK 500 4 ARG A 97 -83.90 -14.60
REMARK 500 5 ASN A 21 -139.99 -115.94
REMARK 500 5 LYS A 41 -142.01 -85.06
REMARK 500
REMARK 500 THIS ENTRY HAS 224 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 57 LYS A 58 5 -143.50
REMARK 500 SER A 57 LYS A 58 13 -134.62
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 TYR A 26 0.07 SIDE CHAIN
REMARK 500 1 TYR A 63 0.09 SIDE CHAIN
REMARK 500 1 TYR A 66 0.18 SIDE CHAIN
REMARK 500 2 TYR A 63 0.08 SIDE CHAIN
REMARK 500 2 TYR A 66 0.20 SIDE CHAIN
REMARK 500 3 TYR A 66 0.21 SIDE CHAIN
REMARK 500 4 TYR A 63 0.12 SIDE CHAIN
REMARK 500 4 TYR A 66 0.18 SIDE CHAIN
REMARK 500 4 TYR A 67 0.10 SIDE CHAIN
REMARK 500 5 PHE A 30 0.13 SIDE CHAIN
REMARK 500 5 TYR A 63 0.17 SIDE CHAIN
REMARK 500 5 TYR A 66 0.23 SIDE CHAIN
REMARK 500 5 TYR A 67 0.06 SIDE CHAIN
REMARK 500 6 TYR A 63 0.07 SIDE CHAIN
REMARK 500 6 TYR A 66 0.21 SIDE CHAIN
REMARK 500 7 TYR A 26 0.07 SIDE CHAIN
REMARK 500 7 TYR A 66 0.18 SIDE CHAIN
REMARK 500 8 TYR A 63 0.09 SIDE CHAIN
REMARK 500 8 TYR A 66 0.19 SIDE CHAIN
REMARK 500 9 TYR A 10 0.09 SIDE CHAIN
REMARK 500 9 TYR A 66 0.21 SIDE CHAIN
REMARK 500 10 PHE A 30 0.08 SIDE CHAIN
REMARK 500 10 TYR A 66 0.17 SIDE CHAIN
REMARK 500 10 TYR A 67 0.07 SIDE CHAIN
REMARK 500 11 TYR A 66 0.18 SIDE CHAIN
REMARK 500 11 TYR A 67 0.09 SIDE CHAIN
REMARK 500 12 PHE A 62 0.09 SIDE CHAIN
REMARK 500 12 TYR A 66 0.20 SIDE CHAIN
REMARK 500 12 TYR A 67 0.11 SIDE CHAIN
REMARK 500 13 TYR A 63 0.11 SIDE CHAIN
REMARK 500 13 TYR A 66 0.20 SIDE CHAIN
REMARK 500 13 TYR A 67 0.07 SIDE CHAIN
REMARK 500 14 PHE A 30 0.11 SIDE CHAIN
REMARK 500 14 TYR A 63 0.09 SIDE CHAIN
REMARK 500 14 TYR A 66 0.20 SIDE CHAIN
REMARK 500 15 TYR A 66 0.19 SIDE CHAIN
REMARK 500 16 TYR A 66 0.26 SIDE CHAIN
REMARK 500 17 TYR A 63 0.08 SIDE CHAIN
REMARK 500 17 TYR A 66 0.19 SIDE CHAIN
REMARK 500 18 TYR A 63 0.11 SIDE CHAIN
REMARK 500 18 TYR A 66 0.18 SIDE CHAIN
REMARK 500 18 PHE A 70 0.19 SIDE CHAIN
REMARK 500 18 TYR A 78 0.07 SIDE CHAIN
REMARK 500 19 TYR A 26 0.08 SIDE CHAIN
REMARK 500 19 TYR A 63 0.07 SIDE CHAIN
REMARK 500 19 TYR A 66 0.17 SIDE CHAIN
REMARK 500 19 PHE A 70 0.14 SIDE CHAIN
REMARK 500 20 TYR A 63 0.08 SIDE CHAIN
REMARK 500 20 TYR A 66 0.19 SIDE CHAIN
REMARK 500 20 PHE A 70 0.09 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 51 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HLA RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE AT 2.6 A RESOLUTION OF THE HLA-A2 (HUMAN
REMARK 900 HISTOCOMPATIBILITY ANTIGEN) OF ALFA1, ALFA2, ALFA3 AND BETA2-
REMARK 900 MICROGLOBULIN DOMAINS.
REMARK 900 RELATED ID: 1HLA RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE AT 3.5 A RESOLUTION OF THE HLA-A2 (HUMAN
REMARK 900 HISTOCOMPATIBILITY ANTIGEN) OF ALFA1, ALFA2, ALFA3 AND BETA2-
REMARK 900 MICROGLOBULIN DOMAINS.
DBREF 1JNJ A 1 99 UNP P61769 B2MG_HUMAN 21 119
SEQADV 1JNJ MET A 0 UNP P61769 CLONING ARTIFACT
SEQRES 1 A 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 A 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 A 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 A 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 A 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 A 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 A 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 A 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SHEET 1 A 4 LYS A 6 SER A 11 0
SHEET 2 A 4 LEU A 23 SER A 28 -1 O SER A 28 N LYS A 6
SHEET 3 A 4 LEU A 64 THR A 68 -1 O TYR A 66 N CYS A 25
SHEET 4 A 4 GLU A 50 HIS A 51 -1 N GLU A 50 O TYR A 67
SHEET 1 B 3 LYS A 91 LYS A 94 0
SHEET 2 B 3 ALA A 79 HIS A 84 -1 N VAL A 82 O LYS A 91
SHEET 3 B 3 ILE A 35 GLU A 36 -1 N GLU A 36 O ASN A 83
SHEET 1 C 4 LYS A 91 LYS A 94 0
SHEET 2 C 4 ALA A 79 HIS A 84 -1 N VAL A 82 O LYS A 91
SHEET 3 C 4 LEU A 39 LEU A 40 -1 N LEU A 40 O ALA A 79
SHEET 4 C 4 ARG A 45 ILE A 46 -1 O ILE A 46 N LEU A 39
SSBOND 1 CYS A 25 CYS A 80 1555 1555 2.06
CISPEP 1 HIS A 31 PRO A 32 1 11.35
CISPEP 2 HIS A 31 PRO A 32 2 7.32
CISPEP 3 HIS A 31 PRO A 32 3 8.09
CISPEP 4 HIS A 31 PRO A 32 4 4.12
CISPEP 5 HIS A 31 PRO A 32 5 6.05
CISPEP 6 HIS A 31 PRO A 32 6 6.81
CISPEP 7 HIS A 31 PRO A 32 7 7.13
CISPEP 8 HIS A 31 PRO A 32 8 8.88
CISPEP 9 HIS A 31 PRO A 32 9 1.27
CISPEP 10 HIS A 31 PRO A 32 10 6.88
CISPEP 11 HIS A 31 PRO A 32 11 1.29
CISPEP 12 HIS A 31 PRO A 32 12 13.08
CISPEP 13 HIS A 31 PRO A 32 13 0.14
CISPEP 14 HIS A 31 PRO A 32 14 13.17
CISPEP 15 HIS A 31 PRO A 32 15 9.77
CISPEP 16 HIS A 31 PRO A 32 16 9.68
CISPEP 17 HIS A 31 PRO A 32 17 9.14
CISPEP 18 HIS A 31 PRO A 32 18 0.26
CISPEP 19 HIS A 31 PRO A 32 19 1.48
CISPEP 20 HIS A 31 PRO A 32 20 9.11
CRYST1 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