Header list of 1t0w.pdb file
Complete list - l 29 2 Bytes
HEADER SUGAR BINDING PROTEIN 13-APR-04 1T0W TITLE 25 NMR STRUCTURES OF TRUNCATED HEVEIN OF 32 AA (HEVEIN-32) COMPLEX TITLE 2 WITH N,N,N-TRIACETYLGLUCOSAMINA CAVEAT 1T0W NAG B 2 HAS WRONG CHIRALITY AT ATOM C1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEVEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL DOMAIN; COMPND 5 SYNONYM: ALLERGEN HEV B 6; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: SEQUENCE PREPARED ON A MBHA RESIN BY STANDARD SOLID SOURCE 4 PHASE PEPTIDE SYNTHESIS PROTOCOLS. THE SEQUENCE OF THE PEPTIDE IS SOURCE 5 NATURALLY FOUND IN HEVEA BRASILIENSIS (PARA RUBBER TREE). KEYWDS ALPHA-HELIX, ANTI-PARALLEL BETA-SHEET, SUGAR BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 25 AUTHOR N.ABOITIZ,M.VILA-PERELLO,P.GROVES,J.L.ASENSIO,D.ANDREU,F.J.CANADA, AUTHOR 2 J.JIMENEZ-BARBERO REVDAT 4 29-JUL-20 1T0W 1 CAVEAT COMPND REMARK HETNAM REVDAT 4 2 1 LINK SITE ATOM REVDAT 3 13-JUL-11 1T0W 1 VERSN REVDAT 2 24-FEB-09 1T0W 1 VERSN REVDAT 1 28-SEP-04 1T0W 0 JRNL AUTH N.ABOITIZ,M.VILA-PERELLO,P.GROVES,J.L.ASENSIO,D.ANDREU, JRNL AUTH 2 F.J.CANADA,J.JIMENEZ-BARBERO JRNL TITL NMR AND MODELING STUDIES OF PROTEIN-CARBOHYDRATE JRNL TITL 2 INTERACTIONS: SYNTHESIS, THREE-DIMENSIONAL STRUCTURE, AND JRNL TITL 3 RECOGNITION PROPERTIES OF A MINIMUM HEVEIN DOMAIN WITH JRNL TITL 4 BINDING AFFINITY FOR CHITOOLIGOSACCHARIDES JRNL REF CHEMBIOCHEM V. 5 1245 2004 JRNL REFN ISSN 1439-4227 JRNL PMID 15368576 JRNL DOI 10.1002/CBIC.200400025 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.L.ASENSIO,F.J.CANADA,M.BRUIX,A.RODRIGUEZ-ROMERO, REMARK 1 AUTH 2 J.JIMENEZ-BARBERO REMARK 1 TITL THE INTERACTION OF HEVEIN WITH REMARK 1 TITL 2 N-ACETYLGLUCOSAMINE-CONTAINING OLIGOSACCHARIDES. SOLUTION REMARK 1 TITL 3 STRUCTURE OF HEVEIN COMPLEXED TO CHITOBIOSE REMARK 1 REF EUR.J.BIOCHEM. V. 230 621 1995 REMARK 1 REFN ISSN 0014-2956 REMARK 1 REFERENCE 2 REMARK 1 AUTH J.C.MARTINS,D.MAES,R.LORIS,H.A.PEPERMANS,L.WYNS,R.WILLEM, REMARK 1 AUTH 2 P.VERHEYDEN REMARK 1 TITL H NMR STUDY OF THE SOLUTION STRUCTURE OF AC-AMP2, A SUGAR REMARK 1 TITL 2 BINDING ANTIMICROBIAL PROTEIN ISOLATED FROM AMARANTHUS REMARK 1 TITL 3 CAUDATUS REMARK 1 REF J.MOL.BIOL. V. 258 322 1996 REMARK 1 REFN ISSN 0022-2836 REMARK 1 DOI 10.1006/JMBI.1996.0253 REMARK 1 REFERENCE 3 REMARK 1 AUTH J.L.ASENSIO,F.J.CANADA,M.BRUIX,C.GONZALEZ,N.KHIAR, REMARK 1 AUTH 2 A.RODRIGUEZ-ROMERO,J.JIMENEZ-BARBERO REMARK 1 TITL NMR INVESTIGATIONS OF PROTEIN-CARBOHYDRATE INTERACTIONS: REMARK 1 TITL 2 REFINED THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN REMARK 1 TITL 3 HEVEIN AND METHYL BETA-CHITOBIOSIDE REMARK 1 REF GLYCOBIOLOGY V. 8 569 1998 REMARK 1 REFN ISSN 0959-6658 REMARK 1 DOI 10.1093/GLYCOB/8.6.569 REMARK 1 REFERENCE 4 REMARK 1 AUTH J.L.ASENSIO,H.-C.SIEBERT,C.-W.VON DER LIETH,J.LAYNEZ, REMARK 1 AUTH 2 M.BRUIX,U.M.SOEDJANAAMADJA,J.J.BEINTEMA,F.J.CANADA, REMARK 1 AUTH 3 H.-J.GABIUS,J.JIMENEZ-BARBERO REMARK 1 TITL NMR INVESTIGATIONS OF PROTEIN-CARBOHYDRATE INTERACTIONS: REMARK 1 TITL 2 STUDIES ON THE RELEVANCE OF TRP/TYR VARIATIONS IN LECTIN REMARK 1 TITL 3 BINDING SITES AS DEDUCED FROM TITRATION MICROCALORIMETRY AND REMARK 1 TITL 4 NMR STUDIES ON HEVEIN DOMAINS. DETERMINATION OF THE NMR REMARK 1 TITL 5 STRUCTURE OF THE COMPLEX BETWEEN PSEUDOHEVEIN AND REMARK 1 TITL 6 N'N',N''-TRIACETYLCHITOTRIOSE REMARK 1 REF PROTEINS: V. 40 218 2000 REMARK 1 REF 2 STRUCT.,FUNCT.,GENET. REMARK 1 REFN ISSN 0887-3585 REMARK 1 DOI 10.1002/(SICI)1097-0134(20000801)40:2<218::AID-PROT50>3.3.CO REMARK 1 DOI 2 ;2-G REMARK 1 REFERENCE 5 REMARK 1 AUTH J.L.ASENSIO,F.J.CANADA,H.-C.SIEBERT,J.LAYNEZ,A.POVEDA, REMARK 1 AUTH 2 P.M.NIETO,U.M.SOEDJANAAMADJA,H.-J.GABIUS,J.JIMENEZ-BARBERO REMARK 1 TITL STRUCTURAL BASIS FOR CHITIN RECOGNITION BY DEFENSE PROTEINS: REMARK 1 TITL 2 GLCNAC RESIDUES ARE BOUND IN A MULTIVALENT FASHION BY REMARK 1 TITL 3 EXTENDED BINDING SITES IN HEVEIN DOMAINS REMARK 1 REF CHEM.BIOL. V. 7 529 2000 REMARK 1 REFN ISSN 1074-5521 REMARK 1 DOI 10.1016/S1074-5521(00)00136-8 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.2, AMBER 5.0 REMARK 3 AUTHORS : REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH, REMARK 3 WEINER,KOLLMAN (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 339 RESTRAINTS: 321 ARE NOE-DERIVED DISTANCE CONSTRAINTS AND 18 REMARK 3 COME FROM CYS-CYS DISULFIDE BRIDGES REMARK 4 REMARK 4 1T0W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-04. REMARK 100 THE DEPOSITION ID IS D_1000022173. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 5.6 REMARK 210 IONIC STRENGTH : 100 MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5 MM HEV32, 3 MM CHITOTRIOSE, REMARK 210 20 MM PHOSPHATE BUFFER, 90% H2O, REMARK 210 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 1.3.13, DIANA 1.5 REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR REMARK 210 DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 25 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES REMARK 210 SUBMITTED REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D REMARK 210 HOMONUCLEAR TECHNIQUES AT TM = 200 AND 300 MS 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, 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 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 2 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 3 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 7 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES REMARK 500 8 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 9 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 10 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 13 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES REMARK 500 13 ARG A 5 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 15 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES REMARK 500 16 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 19 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES REMARK 500 21 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES REMARK 500 22 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 23 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 24 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 25 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.5 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 ASN A 14 -68.28 53.33 REMARK 500 1 ASN A 15 12.94 -162.98 REMARK 500 1 SER A 26 2.41 91.91 REMARK 500 2 ALA A 7 -20.53 168.68 REMARK 500 2 ASN A 14 -69.05 64.04 REMARK 500 2 ASN A 15 13.67 -167.44 REMARK 500 2 ASP A 28 -74.53 -38.61 REMARK 500 2 CYS A 31 -25.46 -142.02 REMARK 500 3 GLN A 6 -43.30 58.49 REMARK 500 3 ASN A 14 2.77 57.77 REMARK 500 3 ASN A 15 16.61 85.25 REMARK 500 3 GLN A 20 -17.07 -47.46 REMARK 500 3 THR A 27 -154.47 -87.74 REMARK 500 3 CYS A 31 -39.71 -135.61 REMARK 500 4 ARG A 5 -98.44 -84.52 REMARK 500 4 ASN A 14 -71.97 53.42 REMARK 500 4 CYS A 31 -56.30 -129.93 REMARK 500 5 ASN A 14 -67.32 52.54 REMARK 500 5 ASN A 15 16.44 -161.19 REMARK 500 6 ASN A 14 11.85 43.38 REMARK 500 6 ASN A 15 18.37 88.17 REMARK 500 6 SER A 26 39.49 -70.83 REMARK 500 6 CYS A 31 -48.51 -132.18 REMARK 500 7 ASN A 14 -84.71 56.77 REMARK 500 7 ASN A 15 24.11 -162.92 REMARK 500 7 SER A 26 54.08 -118.19 REMARK 500 8 ARG A 5 -69.34 -29.01 REMARK 500 8 LYS A 10 108.78 0.42 REMARK 500 8 LEU A 11 175.14 -57.94 REMARK 500 8 ASN A 14 -71.74 57.75 REMARK 500 8 ASN A 15 7.66 -154.69 REMARK 500 9 LYS A 10 80.92 26.56 REMARK 500 9 ASN A 14 -66.48 50.07 REMARK 500 9 ASN A 15 17.57 -157.59 REMARK 500 9 TRP A 21 -70.37 -70.86 REMARK 500 10 ASN A 14 -68.85 63.74 REMARK 500 10 ASN A 15 24.23 -175.12 REMARK 500 11 GLN A 6 -47.80 63.25 REMARK 500 11 ALA A 7 47.73 -72.57 REMARK 500 11 ASN A 14 -68.77 55.20 REMARK 500 11 ASN A 15 17.13 -166.82 REMARK 500 12 GLN A 2 -62.05 -108.92 REMARK 500 12 ASN A 14 -71.40 50.69 REMARK 500 12 ASN A 15 15.86 -164.97 REMARK 500 12 SER A 26 11.78 80.33 REMARK 500 12 ASP A 28 -84.11 1.96 REMARK 500 13 ASN A 14 -74.08 59.20 REMARK 500 13 ASN A 15 16.61 -162.28 REMARK 500 13 SER A 19 146.91 -38.17 REMARK 500 13 CYS A 31 -81.97 -129.80 REMARK 500 REMARK 500 THIS ENTRY HAS 86 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 TYR A 30 CYS A 31 5 146.69 REMARK 500 SER A 26 THR A 27 6 -148.96 REMARK 500 SER A 26 THR A 27 11 -146.87 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 2 ARG A 5 0.11 SIDE CHAIN REMARK 500 2 TYR A 30 0.08 SIDE CHAIN REMARK 500 3 TYR A 30 0.08 SIDE CHAIN REMARK 500 6 ARG A 5 0.09 SIDE CHAIN REMARK 500 7 TYR A 30 0.10 SIDE CHAIN REMARK 500 8 ARG A 5 0.15 SIDE CHAIN REMARK 500 9 TYR A 30 0.08 SIDE CHAIN REMARK 500 11 TYR A 30 0.07 SIDE CHAIN REMARK 500 15 TYR A 30 0.07 SIDE CHAIN REMARK 500 18 TYR A 30 0.11 SIDE CHAIN REMARK 500 20 ARG A 5 0.09 SIDE CHAIN REMARK 500 24 TYR A 30 0.07 SIDE CHAIN REMARK 500 25 TYR A 30 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1HEV RELATED DB: PDB REMARK 900 NMR STRUCTURE OF HEVEIN (FULL PROTEIN, 43 AA) IN THE FREE STATE REMARK 900 RELATED ID: 1Q9B RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HEVEIN (FULL PROTEIN, 43 AA) IN THE FREE STATE REMARK 900 RELATED ID: 1MMC RELATED DB: PDB REMARK 900 NMR STRUCTURE OF AC-AMP2 (AMARANTHUS CAUDATUS ANTIMICROBIAL PEPTIDE REMARK 900 2) IN THE FREE STATE REMARK 900 RELATED ID: 10261 RELATED DB: BMRB REMARK 900 NMR SPECTRAL PARAMETERS OF HEV32 (TRUNCATED HEVEIN OF 32 AA) REMARK 900 COMPLEXED WITH CHITOTRIOSE DBREF 1T0W A 1 32 UNP P02877 HEVE_HEVBR 18 49 SEQRES 1 A 33 GLU GLN CYS GLY ARG GLN ALA GLY GLY LYS LEU CYS PRO SEQRES 2 A 33 ASN ASN LEU CYS CYS SER GLN TRP GLY TRP CYS GLY SER SEQRES 3 A 33 THR ASP GLU TYR CYS SER NH2 HET NH2 A 33 3 HET NAG B 1 29 HET NAG B 2 27 HET NAG B 3 28 HETNAM NH2 AMINO GROUP HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE FORMUL 1 NH2 H2 N FORMUL 2 NAG 3(C8 H15 N O6) HELIX 1 1 GLY A 4 GLY A 8 5 5 HELIX 2 2 THR A 27 SER A 32 1 6 SSBOND 1 CYS A 3 CYS A 18 1555 1555 2.03 SSBOND 2 CYS A 12 CYS A 24 1555 1555 2.03 SSBOND 3 CYS A 17 CYS A 31 1555 1555 2.05 LINK C SER A 32 N NH2 A 33 1555 1555 1.34 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.40 LINK O4 NAG B 2 C1 NAG B 3 1555 1555 1.40 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 - l 29 2 Bytes