Header list of 1be2.pdb file
Complete list - b 16 2 Bytes
HEADER LIPID TRANSPORT 19-MAY-98 1BE2 TITLE LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITATE, NMR, 10 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: LIPID TRANSFER PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: LTP SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HORDEUM VULGARE; SOURCE 3 ORGANISM_TAXID: 4513; SOURCE 4 ORGAN: SEEDS KEYWDS LIPID TRANSPORT, LIPID TRANSFER PROTEIN, PALMITATE EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR M.H.LERCHE,F.M.POULSEN REVDAT 4 16-FEB-22 1BE2 1 REMARK REVDAT 3 24-FEB-09 1BE2 1 VERSN REVDAT 2 13-JAN-99 1BE2 1 REMARK TITLE REVDAT 1 02-DEC-98 1BE2 0 JRNL AUTH M.H.LERCHE,F.M.POULSEN JRNL TITL SOLUTION STRUCTURE OF BARLEY LIPID TRANSFER PROTEIN JRNL TITL 2 COMPLEXED WITH PALMITATE. TWO DIFFERENT BINDING MODES OF JRNL TITL 3 PALMITATE IN THE HOMOLOGOUS MAIZE AND BARLEY NONSPECIFIC JRNL TITL 4 LIPID TRANSFER PROTEINS. JRNL REF PROTEIN SCI. V. 7 2490 1998 JRNL REFN ISSN 0961-8368 JRNL PMID 9865943 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.H.LERCHE,B.B.KRAGELUND,L.M.BECH,F.M.POULSEN REMARK 1 TITL BARLEY LIPID-TRANSFER PROTEIN COMPLEXED WITH PALMITOYL COA: REMARK 1 TITL 2 THE STRUCTURE REVEALS A HYDROPHOBIC BINDING SITE THAT CAN REMARK 1 TITL 3 EXPAND TO FIT BOTH LARGE AND SMALL LIPID-LIKE LIGANDS REMARK 1 REF STRUCTURE V. 5 291 1997 REMARK 1 REFN ISSN 0969-2126 REMARK 1 REFERENCE 2 REMARK 1 AUTH B.HEINEMANN,K.V.ANDERSEN,P.R.NIELSEN,L.M.BECH,F.M.POULSEN REMARK 1 TITL STRUCTURE IN SOLUTION OF A FOUR-HELIX LIPID BINDING PROTEIN REMARK 1 REF PROTEIN SCI. V. 5 13 1996 REMARK 1 REFN ISSN 0961-8368 REMARK 1 REFERENCE 3 REMARK 1 AUTH D.H.SHIN,J.Y.LEE,K.Y.HWANG,K.K.KIM,S.W.SUH REMARK 1 TITL HIGH-RESOLUTION CRYSTAL STRUCTURE OF THE NON-SPECIFIC REMARK 1 TITL 2 LIPID-TRANSFER PROTEIN FROM MAIZE SEEDLINGS REMARK 1 REF STRUCTURE V. 3 189 1995 REMARK 1 REFN ISSN 0969-2126 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.8 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1BE2 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_1000171644. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 7.2 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; TOCSY; NOESY; HSQC; REMARK 210 HSQC-NOE REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : PRONTO, X-PLOR 3.8 REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 40 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TOTAL ENERGY 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: 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 LYS A 11 N - CA - CB ANGL. DEV. = -11.0 DEGREES REMARK 500 1 ARG A 32 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES REMARK 500 1 ARG A 56 NE - CZ - NH1 ANGL. DEV. = -5.7 DEGREES REMARK 500 1 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -5.8 DEGREES REMARK 500 2 ASP A 33 CB - CG - OD2 ANGL. DEV. = -7.3 DEGREES REMARK 500 2 ASP A 43 CB - CG - OD1 ANGL. DEV. = -6.2 DEGREES REMARK 500 2 ARG A 44 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES REMARK 500 2 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 2 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 3 ARG A 44 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES REMARK 500 3 ARG A 56 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES REMARK 500 4 ASP A 33 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 4 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES REMARK 500 4 ASP A 86 CB - CG - OD2 ANGL. DEV. = -8.0 DEGREES REMARK 500 4 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES REMARK 500 5 CYS A 28 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 5 ARG A 32 NH1 - CZ - NH2 ANGL. DEV. = 6.9 DEGREES REMARK 500 5 ARG A 32 NE - CZ - NH1 ANGL. DEV. = -5.7 DEGREES REMARK 500 5 ARG A 44 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES REMARK 500 5 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES REMARK 500 6 ARG A 32 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES REMARK 500 6 ASP A 33 CB - CG - OD2 ANGL. DEV. = -7.4 DEGREES REMARK 500 6 ARG A 56 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES REMARK 500 6 ASP A 86 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES REMARK 500 6 ARG A 89 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES REMARK 500 7 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES REMARK 500 7 TYR A 79 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 7 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 8 ASP A 33 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES REMARK 500 8 ARG A 44 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES REMARK 500 8 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES REMARK 500 8 CYS A 87 CA - CB - SG ANGL. DEV. = 7.8 DEGREES REMARK 500 9 ARG A 32 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES REMARK 500 9 ASP A 33 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES REMARK 500 9 ARG A 44 NE - CZ - NH1 ANGL. DEV. = -7.5 DEGREES REMARK 500 9 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 9 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 10 TYR A 16 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 10 CYS A 28 CA - CB - SG ANGL. DEV. = 8.0 DEGREES REMARK 500 10 ARG A 32 NE - CZ - NH2 ANGL. DEV. = -6.7 DEGREES REMARK 500 10 ARG A 44 NE - CZ - NH1 ANGL. DEV. = -7.5 DEGREES REMARK 500 10 ARG A 44 NE - CZ - NH2 ANGL. DEV. = 4.1 DEGREES REMARK 500 10 ARG A 56 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES REMARK 500 10 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -5.2 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 2 75.06 -21.01 REMARK 500 1 CYS A 3 -58.39 1.89 REMARK 500 1 LYS A 9 -62.33 -92.60 REMARK 500 1 LYS A 11 -61.71 -20.90 REMARK 500 1 PRO A 21 49.44 -94.61 REMARK 500 1 CYS A 27 -78.11 -50.26 REMARK 500 1 CYS A 28 -47.46 -27.75 REMARK 500 1 SER A 41 -49.61 -22.20 REMARK 500 1 GLN A 45 -71.10 -30.54 REMARK 500 1 ILE A 58 -162.50 -121.17 REMARK 500 1 HIS A 59 -83.32 -97.38 REMARK 500 1 LEU A 61 126.88 -33.65 REMARK 500 1 LEU A 63 -51.08 -18.51 REMARK 500 1 ILE A 69 -72.74 -44.96 REMARK 500 1 ASN A 74 56.41 72.67 REMARK 500 1 ASN A 76 72.39 4.67 REMARK 500 1 ILE A 81 80.37 -27.51 REMARK 500 1 ASP A 84 77.99 -111.11 REMARK 500 1 CYS A 87 -28.88 -37.62 REMARK 500 2 CYS A 3 -72.25 8.13 REMARK 500 2 LYS A 9 -62.14 -93.99 REMARK 500 2 LYS A 11 -70.44 -18.34 REMARK 500 2 SER A 24 -10.11 -28.08 REMARK 500 2 GLU A 26 -53.33 -29.09 REMARK 500 2 ASN A 60 57.54 -158.78 REMARK 500 2 LEU A 61 126.57 -35.69 REMARK 500 2 LEU A 63 -47.31 -18.02 REMARK 500 2 ILE A 69 -71.93 -43.64 REMARK 500 2 ASN A 76 39.62 24.86 REMARK 500 2 PRO A 78 -46.14 -29.18 REMARK 500 2 ILE A 81 71.61 -12.54 REMARK 500 2 ASP A 84 47.09 -108.29 REMARK 500 2 ASP A 86 46.92 -106.16 REMARK 500 2 CYS A 87 -33.79 -38.30 REMARK 500 2 SER A 88 -54.89 -27.48 REMARK 500 2 ILE A 90 98.16 90.10 REMARK 500 3 LYS A 11 -62.71 -22.31 REMARK 500 3 SER A 24 46.11 -98.64 REMARK 500 3 SER A 40 -141.68 -98.40 REMARK 500 3 SER A 41 -71.22 -97.49 REMARK 500 3 ASP A 43 -84.73 -89.89 REMARK 500 3 ASN A 60 67.35 -160.73 REMARK 500 3 LEU A 61 132.83 -33.61 REMARK 500 3 LEU A 63 -52.90 -16.97 REMARK 500 3 ILE A 69 -71.22 -41.49 REMARK 500 3 ASN A 76 63.22 13.96 REMARK 500 3 ILE A 81 71.02 -16.22 REMARK 500 3 ASP A 84 53.47 -95.55 REMARK 500 3 ASP A 86 34.32 -74.74 REMARK 500 3 CYS A 87 -54.97 -15.72 REMARK 500 REMARK 500 THIS ENTRY HAS 156 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 82 PRO A 83 7 144.32 REMARK 500 SER A 82 PRO A 83 8 138.77 REMARK 500 SER A 82 PRO A 83 10 118.78 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 32 0.29 SIDE CHAIN REMARK 500 1 ARG A 44 0.32 SIDE CHAIN REMARK 500 1 ARG A 56 0.30 SIDE CHAIN REMARK 500 1 ARG A 89 0.28 SIDE CHAIN REMARK 500 2 ARG A 32 0.14 SIDE CHAIN REMARK 500 2 ARG A 44 0.15 SIDE CHAIN REMARK 500 2 ARG A 56 0.32 SIDE CHAIN REMARK 500 2 ARG A 89 0.31 SIDE CHAIN REMARK 500 3 ARG A 32 0.29 SIDE CHAIN REMARK 500 3 ARG A 44 0.21 SIDE CHAIN REMARK 500 3 ARG A 56 0.28 SIDE CHAIN REMARK 500 3 ARG A 89 0.22 SIDE CHAIN REMARK 500 4 ARG A 32 0.30 SIDE CHAIN REMARK 500 4 ARG A 44 0.28 SIDE CHAIN REMARK 500 4 ARG A 56 0.30 SIDE CHAIN REMARK 500 4 ARG A 89 0.24 SIDE CHAIN REMARK 500 5 ARG A 32 0.30 SIDE CHAIN REMARK 500 5 ARG A 44 0.28 SIDE CHAIN REMARK 500 5 ARG A 56 0.30 SIDE CHAIN REMARK 500 5 ARG A 89 0.19 SIDE CHAIN REMARK 500 6 ARG A 32 0.30 SIDE CHAIN REMARK 500 6 ARG A 44 0.26 SIDE CHAIN REMARK 500 6 ARG A 56 0.30 SIDE CHAIN REMARK 500 6 ARG A 89 0.26 SIDE CHAIN REMARK 500 7 ARG A 32 0.19 SIDE CHAIN REMARK 500 7 ARG A 44 0.28 SIDE CHAIN REMARK 500 7 ARG A 56 0.29 SIDE CHAIN REMARK 500 7 ARG A 89 0.29 SIDE CHAIN REMARK 500 8 ARG A 32 0.12 SIDE CHAIN REMARK 500 8 ARG A 44 0.26 SIDE CHAIN REMARK 500 8 ARG A 56 0.10 SIDE CHAIN REMARK 500 8 ARG A 89 0.21 SIDE CHAIN REMARK 500 9 ARG A 32 0.28 SIDE CHAIN REMARK 500 9 ARG A 44 0.29 SIDE CHAIN REMARK 500 9 ARG A 56 0.30 SIDE CHAIN REMARK 500 9 ARG A 89 0.27 SIDE CHAIN REMARK 500 10 ARG A 32 0.29 SIDE CHAIN REMARK 500 10 ARG A 44 0.29 SIDE CHAIN REMARK 500 10 ARG A 56 0.28 SIDE CHAIN REMARK 500 10 ARG A 89 0.24 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: PLB REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: BINDING SITE OF PALMITATE. REMARK 800 REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM A 92 DBREF 1BE2 A 1 91 UNP P07597 NLTP1_HORVU 27 117 SEQRES 1 A 91 LEU ASN CYS GLY GLN VAL ASP SER LYS MET LYS PRO CYS SEQRES 2 A 91 LEU THR TYR VAL GLN GLY GLY PRO GLY PRO SER GLY GLU SEQRES 3 A 91 CYS CYS ASN GLY VAL ARG ASP LEU HIS ASN GLN ALA GLN SEQRES 4 A 91 SER SER GLY ASP ARG GLN THR VAL CYS ASN CYS LEU LYS SEQRES 5 A 91 GLY ILE ALA ARG GLY ILE HIS ASN LEU ASN LEU ASN ASN SEQRES 6 A 91 ALA ALA SER ILE PRO SER LYS CYS ASN VAL ASN VAL PRO SEQRES 7 A 91 TYR THR ILE SER PRO ASP ILE ASP CYS SER ARG ILE TYR HET PLM A 92 49 HETNAM PLM PALMITIC ACID FORMUL 2 PLM C16 H32 O2 HELIX 1 1 GLY A 4 GLY A 19 1 16 HELIX 2 2 GLU A 26 GLN A 37 1 12 HELIX 3 3 SER A 41 ARG A 56 1 16 HELIX 4 4 LEU A 63 CYS A 73 1 11 SSBOND 1 CYS A 3 CYS A 50 1555 1555 2.01 SSBOND 2 CYS A 13 CYS A 27 1555 1555 2.02 SSBOND 3 CYS A 28 CYS A 73 1555 1555 2.02 SSBOND 4 CYS A 48 CYS A 87 1555 1555 2.02 CISPEP 1 GLY A 22 PRO A 23 1 1.79 CISPEP 2 GLY A 22 PRO A 23 2 -2.72 CISPEP 3 GLY A 22 PRO A 23 3 -8.07 CISPEP 4 GLY A 22 PRO A 23 4 -3.94 CISPEP 5 GLY A 22 PRO A 23 5 7.81 CISPEP 6 GLY A 22 PRO A 23 6 3.50 CISPEP 7 GLY A 22 PRO A 23 7 5.21 CISPEP 8 GLY A 22 PRO A 23 8 -11.26 CISPEP 9 GLY A 22 PRO A 23 9 12.22 CISPEP 10 GLY A 22 PRO A 23 10 2.77 SITE 1 PLB 16 LYS A 9 MET A 10 CYS A 13 LEU A 14 SITE 2 PLB 16 CYS A 27 LEU A 34 HIS A 35 ARG A 44 SITE 3 PLB 16 GLN A 45 VAL A 47 CYS A 48 LEU A 51 SITE 4 PLB 16 ILE A 69 TYR A 79 ILE A 81 ILE A 85 SITE 1 AC1 14 LYS A 9 MET A 10 CYS A 13 LEU A 14 SITE 2 AC1 14 TYR A 16 VAL A 17 VAL A 31 ARG A 44 SITE 3 AC1 14 VAL A 47 CYS A 48 LEU A 51 ILE A 69 SITE 4 AC1 14 TYR A 79 ILE A 81 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 16 2 Bytes