Header list of 1lwr.pdb file
Complete list - b 23 2 Bytes
HEADER CELL ADHESION 03-JUN-02 1LWR TITLE SOLUTION STRUCTURE OF THE NCAM FIBRONECTIN TYPE III MODULE 2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEURAL CELL ADHESION MOLECULE 1, 140 KDA ISOFORM; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: NCAM; NCAM POLYPEPTIDE; N-CAM 140; NCAM-140; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 GENE: NCAM1; SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: KM71; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZA KEYWDS ALL BETA, FIBRONECTIN TYPE III MODULE, CELL ADHESION EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR V.V.KISELYOV,G.SKLADCHIKOVA,A.M.HINSBY,P.H.JENSEN,N.KULAHIN, AUTHOR 2 N.PEDERSEN,V.TSETLIN,F.M.POULSEN,V.BEREZIN,E.BOCK REVDAT 4 23-FEB-22 1LWR 1 REMARK SEQADV REVDAT 3 24-FEB-09 1LWR 1 VERSN REVDAT 2 22-MAR-05 1LWR 1 JRNL AUTHOR REVDAT 1 03-JUN-03 1LWR 0 JRNL AUTH V.V.KISELYOV,G.SKLADCHIKOVA,A.M.HINSBY,P.H.JENSEN,N.KULAHIN, JRNL AUTH 2 V.SOROKA,N.PEDERSEN,V.TSETLIN,F.M.POULSEN,V.BEREZIN,E.BOCK JRNL TITL STRUCTURAL BASIS FOR A DIRECT INTERACTION BETWEEN FGFR1 AND JRNL TITL 2 NCAM AND EVIDENCE FOR A REGULATORY ROLE OF ATP JRNL REF STRUCTURE V. 11 691 2003 JRNL REFN ISSN 0969-2126 JRNL PMID 12791257 JRNL DOI 10.1016/S0969-2126(03)00096-0 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PRONTO 19981230, X-PLOR 3.1 REMARK 3 AUTHORS : KJAER. M. (PRONTO), BRUNGER, A. (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1LWR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-02. REMARK 100 THE DEPOSITION ID IS D_1000016356. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.27 REMARK 210 IONIC STRENGTH : 40 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM NCAM FNIII MODULE 2 REMARK 210 UNLABELLED; 30 MM NACL, 10 MM REMARK 210 SODIUM PHOSPHATE, PH 7.27; 2MM REMARK 210 NCAM FNIII MODULE 2 UNLABELLED; REMARK 210 30 MM NACL, 10 MM SODIUM REMARK 210 PHOSPHATE, PH 7.27; 1MM NCAM REMARK 210 FNIII MODULE 2 U-15N; 30 MM NACL, REMARK 210 10 MM SODIUM PHOSPHATE, PH 7.27 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY; REMARK 210 3D_15N-SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : MNMR REMARK 210 METHOD USED : DISTANCE GEOMETRY; SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 78 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 REMARK 210 CONFORMERS, SELECTION CRITERIA : Z-SCORES LESS THAN 2.4 REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4 REMARK 210 REMARK 210 REMARK: REMARK 210 THIS STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR REMARK 210 TECHNIQUES REMARK 210 AND TRIPLE-RESONANCE NMR SPECTROSCOPY 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 1 TRP A 47 CG - CD1 - NE1 ANGL. DEV. = -7.1 DEGREES REMARK 500 1 TRP A 47 CD1 - NE1 - CE2 ANGL. DEV. = 8.1 DEGREES REMARK 500 1 TRP A 47 NE1 - CE2 - CZ2 ANGL. DEV. = 7.0 DEGREES REMARK 500 1 TRP A 67 CG - CD1 - NE1 ANGL. DEV. = -7.3 DEGREES REMARK 500 1 TRP A 67 CD1 - NE1 - CE2 ANGL. DEV. = 8.3 DEGREES REMARK 500 1 TRP A 67 NE1 - CE2 - CZ2 ANGL. DEV. = 7.8 DEGREES REMARK 500 2 TRP A 47 CG - CD1 - NE1 ANGL. DEV. = -7.1 DEGREES REMARK 500 2 TRP A 47 CD1 - NE1 - CE2 ANGL. DEV. = 8.1 DEGREES REMARK 500 2 TRP A 47 NE1 - CE2 - CZ2 ANGL. DEV. = 6.9 DEGREES REMARK 500 2 TRP A 67 CG - CD1 - NE1 ANGL. DEV. = -7.3 DEGREES REMARK 500 2 TRP A 67 CD1 - NE1 - CE2 ANGL. DEV. = 8.3 DEGREES REMARK 500 2 TRP A 67 NE1 - CE2 - CZ2 ANGL. DEV. = 7.8 DEGREES REMARK 500 3 TRP A 47 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES REMARK 500 3 TRP A 47 CD1 - NE1 - CE2 ANGL. DEV. = 8.1 DEGREES REMARK 500 3 TRP A 47 NE1 - CE2 - CZ2 ANGL. DEV. = 6.8 DEGREES REMARK 500 3 TRP A 67 CG - CD1 - NE1 ANGL. DEV. = -7.2 DEGREES REMARK 500 3 TRP A 67 CD1 - NE1 - CE2 ANGL. DEV. = 8.3 DEGREES REMARK 500 3 TRP A 67 NE1 - CE2 - CZ2 ANGL. DEV. = 7.9 DEGREES REMARK 500 4 TRP A 47 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES REMARK 500 4 TRP A 47 CD1 - NE1 - CE2 ANGL. DEV. = 8.1 DEGREES REMARK 500 4 TRP A 47 NE1 - CE2 - CZ2 ANGL. DEV. = 7.1 DEGREES REMARK 500 4 TRP A 67 CG - CD1 - NE1 ANGL. DEV. = -7.3 DEGREES REMARK 500 4 TRP A 67 CD1 - NE1 - CE2 ANGL. DEV. = 8.3 DEGREES REMARK 500 4 TRP A 67 NE1 - CE2 - CZ2 ANGL. DEV. = 7.9 DEGREES REMARK 500 5 TRP A 47 CG - CD1 - NE1 ANGL. DEV. = -7.1 DEGREES REMARK 500 5 TRP A 47 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES REMARK 500 5 TRP A 47 NE1 - CE2 - CZ2 ANGL. DEV. = 6.7 DEGREES REMARK 500 5 TRP A 67 CG - CD1 - NE1 ANGL. DEV. = -7.3 DEGREES REMARK 500 5 TRP A 67 CD1 - NE1 - CE2 ANGL. DEV. = 8.4 DEGREES REMARK 500 5 TRP A 67 NE1 - CE2 - CZ2 ANGL. DEV. = 8.1 DEGREES REMARK 500 6 TRP A 47 CG - CD1 - NE1 ANGL. DEV. = -7.2 DEGREES REMARK 500 6 TRP A 47 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES REMARK 500 6 TRP A 47 NE1 - CE2 - CZ2 ANGL. DEV. = 7.4 DEGREES REMARK 500 6 TRP A 67 CG - CD1 - NE1 ANGL. DEV. = -7.2 DEGREES REMARK 500 6 TRP A 67 CD1 - NE1 - CE2 ANGL. DEV. = 8.3 DEGREES REMARK 500 6 TRP A 67 NE1 - CE2 - CZ2 ANGL. DEV. = 7.8 DEGREES REMARK 500 7 TRP A 47 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES REMARK 500 7 TRP A 47 CD1 - NE1 - CE2 ANGL. DEV. = 8.1 DEGREES REMARK 500 7 TRP A 47 NE1 - CE2 - CZ2 ANGL. DEV. = 6.8 DEGREES REMARK 500 7 TRP A 67 CG - CD1 - NE1 ANGL. DEV. = -7.3 DEGREES REMARK 500 7 TRP A 67 CD1 - NE1 - CE2 ANGL. DEV. = 8.3 DEGREES REMARK 500 7 TRP A 67 NE1 - CE2 - CZ2 ANGL. DEV. = 7.8 DEGREES REMARK 500 8 TRP A 47 CG - CD1 - NE1 ANGL. DEV. = -7.1 DEGREES REMARK 500 8 TRP A 47 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES REMARK 500 8 TRP A 47 NE1 - CE2 - CZ2 ANGL. DEV. = 6.9 DEGREES REMARK 500 8 TRP A 67 CG - CD1 - NE1 ANGL. DEV. = -7.2 DEGREES REMARK 500 8 TRP A 67 CD1 - NE1 - CE2 ANGL. DEV. = 8.4 DEGREES REMARK 500 8 TRP A 67 NE1 - CE2 - CZ2 ANGL. DEV. = 8.2 DEGREES REMARK 500 9 TRP A 47 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES REMARK 500 9 TRP A 47 CD1 - NE1 - CE2 ANGL. DEV. = 8.1 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 179 ANGLE DEVIATIONS. 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 3 173.70 -56.53 REMARK 500 1 GLU A 14 13.18 -65.07 REMARK 500 1 GLN A 26 -48.20 -143.99 REMARK 500 1 ASP A 28 -37.59 -130.77 REMARK 500 1 PRO A 32 40.00 -88.75 REMARK 500 1 HIS A 35 -172.95 35.66 REMARK 500 1 LEU A 43 42.68 -82.43 REMARK 500 1 ALA A 44 -56.81 -150.56 REMARK 500 1 TRP A 47 95.78 10.50 REMARK 500 1 PRO A 49 102.28 -44.89 REMARK 500 1 SER A 64 51.57 86.97 REMARK 500 1 LYS A 85 165.17 -41.38 REMARK 500 2 PRO A 3 170.09 -55.22 REMARK 500 2 GLU A 14 12.05 -64.73 REMARK 500 2 GLN A 26 -67.53 -170.31 REMARK 500 2 PRO A 32 46.44 -86.93 REMARK 500 2 HIS A 35 -176.26 36.86 REMARK 500 2 LEU A 43 43.09 -77.02 REMARK 500 2 ALA A 44 -58.05 -148.73 REMARK 500 2 TRP A 47 92.14 24.81 REMARK 500 2 PRO A 49 96.12 -49.17 REMARK 500 2 SER A 64 44.03 93.32 REMARK 500 2 LYS A 85 165.63 -42.09 REMARK 500 3 GLU A 14 10.22 -64.07 REMARK 500 3 GLN A 26 -74.13 -166.27 REMARK 500 3 SER A 31 79.07 36.80 REMARK 500 3 PRO A 32 35.46 -87.55 REMARK 500 3 HIS A 35 -173.72 34.44 REMARK 500 3 LEU A 43 43.60 -74.95 REMARK 500 3 ALA A 44 -57.91 -148.49 REMARK 500 3 TRP A 47 84.08 58.81 REMARK 500 3 PRO A 49 105.14 -44.66 REMARK 500 3 LYS A 85 159.29 -39.59 REMARK 500 4 PRO A 3 172.23 -58.05 REMARK 500 4 GLU A 14 10.68 -64.18 REMARK 500 4 GLN A 26 -70.12 -136.87 REMARK 500 4 ASP A 28 -34.54 -134.02 REMARK 500 4 HIS A 35 -172.55 33.65 REMARK 500 4 LEU A 43 40.17 -91.83 REMARK 500 4 ALA A 44 -58.21 -146.44 REMARK 500 4 TRP A 47 89.79 25.24 REMARK 500 4 PRO A 49 100.33 -44.28 REMARK 500 4 SER A 55 85.57 -65.62 REMARK 500 4 SER A 64 48.50 90.07 REMARK 500 4 GLN A 80 -35.93 -37.69 REMARK 500 4 LYS A 85 164.00 -40.75 REMARK 500 5 GLU A 14 13.00 -63.45 REMARK 500 5 ASN A 17 18.92 -143.46 REMARK 500 5 GLN A 26 -63.76 -130.61 REMARK 500 5 ASP A 28 -35.42 -133.42 REMARK 500 REMARK 500 THIS ENTRY HAS 348 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 34 0.31 SIDE CHAIN REMARK 500 1 ARG A 41 0.24 SIDE CHAIN REMARK 500 1 ARG A 52 0.30 SIDE CHAIN REMARK 500 1 ARG A 92 0.32 SIDE CHAIN REMARK 500 2 ARG A 34 0.31 SIDE CHAIN REMARK 500 2 ARG A 41 0.32 SIDE CHAIN REMARK 500 2 ARG A 52 0.32 SIDE CHAIN REMARK 500 2 ARG A 92 0.29 SIDE CHAIN REMARK 500 3 ARG A 34 0.31 SIDE CHAIN REMARK 500 3 ARG A 41 0.26 SIDE CHAIN REMARK 500 3 ARG A 52 0.32 SIDE CHAIN REMARK 500 3 ARG A 92 0.32 SIDE CHAIN REMARK 500 4 ARG A 34 0.31 SIDE CHAIN REMARK 500 4 ARG A 41 0.28 SIDE CHAIN REMARK 500 4 ARG A 52 0.32 SIDE CHAIN REMARK 500 4 ARG A 92 0.31 SIDE CHAIN REMARK 500 5 ARG A 34 0.30 SIDE CHAIN REMARK 500 5 ARG A 41 0.22 SIDE CHAIN REMARK 500 5 ARG A 52 0.30 SIDE CHAIN REMARK 500 5 ARG A 92 0.27 SIDE CHAIN REMARK 500 6 ARG A 34 0.30 SIDE CHAIN REMARK 500 6 ARG A 41 0.26 SIDE CHAIN REMARK 500 6 ARG A 52 0.31 SIDE CHAIN REMARK 500 6 ARG A 92 0.32 SIDE CHAIN REMARK 500 7 ARG A 34 0.31 SIDE CHAIN REMARK 500 7 ARG A 41 0.27 SIDE CHAIN REMARK 500 7 ARG A 52 0.31 SIDE CHAIN REMARK 500 7 ARG A 92 0.32 SIDE CHAIN REMARK 500 8 ARG A 34 0.31 SIDE CHAIN REMARK 500 8 ARG A 41 0.32 SIDE CHAIN REMARK 500 8 ARG A 52 0.31 SIDE CHAIN REMARK 500 8 ARG A 92 0.32 SIDE CHAIN REMARK 500 9 ARG A 34 0.24 SIDE CHAIN REMARK 500 9 ARG A 41 0.25 SIDE CHAIN REMARK 500 9 ARG A 52 0.29 SIDE CHAIN REMARK 500 9 ARG A 92 0.32 SIDE CHAIN REMARK 500 10 ARG A 34 0.32 SIDE CHAIN REMARK 500 10 ARG A 41 0.31 SIDE CHAIN REMARK 500 10 ARG A 52 0.30 SIDE CHAIN REMARK 500 10 ARG A 92 0.32 SIDE CHAIN REMARK 500 11 ARG A 34 0.26 SIDE CHAIN REMARK 500 11 ARG A 41 0.31 SIDE CHAIN REMARK 500 11 ARG A 52 0.31 SIDE CHAIN REMARK 500 11 ARG A 92 0.30 SIDE CHAIN REMARK 500 12 ARG A 34 0.32 SIDE CHAIN REMARK 500 12 ARG A 41 0.32 SIDE CHAIN REMARK 500 12 ARG A 52 0.30 SIDE CHAIN REMARK 500 12 ARG A 92 0.32 SIDE CHAIN REMARK 500 13 ARG A 34 0.30 SIDE CHAIN REMARK 500 13 ARG A 41 0.26 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 120 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1LWR A 1 96 UNP P13596 NCAM1_RAT 612 707 SEQADV 1LWR ALA A 1 UNP P13596 ARG 612 CLONING ARTIFACT SEQADV 1LWR GLY A 2 UNP P13596 GLU 613 CLONING ARTIFACT SEQRES 1 A 96 ALA GLY PRO SER ALA PRO LYS LEU GLU GLY GLN MET GLY SEQRES 2 A 96 GLU ASP GLY ASN SER ILE LYS VAL ASN LEU ILE LYS GLN SEQRES 3 A 96 ASP ASP GLY GLY SER PRO ILE ARG HIS TYR LEU VAL LYS SEQRES 4 A 96 TYR ARG ALA LEU ALA SER GLU TRP LYS PRO GLU ILE ARG SEQRES 5 A 96 LEU PRO SER GLY SER ASP HIS VAL MET LEU LYS SER LEU SEQRES 6 A 96 ASP TRP ASN ALA GLU TYR GLU VAL TYR VAL VAL ALA GLU SEQRES 7 A 96 ASN GLN GLN GLY LYS SER LYS ALA ALA HIS PHE VAL PHE SEQRES 8 A 96 ARG THR SER ALA GLN SHEET 1 A 3 LYS A 7 GLY A 13 0 SHEET 2 A 3 SER A 18 ILE A 24 -1 O ILE A 24 N LYS A 7 SHEET 3 A 3 HIS A 59 LYS A 63 -1 O VAL A 60 N VAL A 21 SHEET 1 B 4 ILE A 51 ARG A 52 0 SHEET 2 B 4 ILE A 33 ALA A 42 -1 N VAL A 38 O ILE A 51 SHEET 3 B 4 GLU A 70 ASN A 79 -1 O GLU A 78 N ARG A 34 SHEET 4 B 4 GLY A 82 ARG A 92 -1 O SER A 84 N ALA A 77 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