Header list of 1r4y.pdb file
Complete list - t 27 2 Bytes
HEADER HYDROLASE 09-OCT-03 1R4Y TITLE SOLUTION STRUCTURE OF THE DELETION MUTANT DELTA(7-22) OF THE CYTOTOXIC TITLE 2 RIBONUCLEASE ALPHA-SARCIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: RIBONUCLEASE ALPHA-SARCIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: RRNA ENDONUCLEASE; COMPND 5 EC: 3.1.27.10; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS GIGANTEUS; SOURCE 3 ORGANISM_TAXID: 5060; SOURCE 4 GENE: SAR; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PINPGOMPAASD(7-22) KEYWDS ALPHA-BETA PROTEIN, HYDROLASE EXPDTA SOLUTION NMR NUMMDL 25 AUTHOR M.F.GARCIA-MAYORAL,L.GARCIA-ORTEGA,M.P.LILLO,J.SANTORO,A.MARTINEZ DEL AUTHOR 2 POZO,J.G.GAVILANES,M.RICO,M.BRUIX REVDAT 3 27-OCT-21 1R4Y 1 REMARK SEQADV REVDAT 2 24-FEB-09 1R4Y 1 VERSN REVDAT 1 06-APR-04 1R4Y 0 JRNL AUTH M.F.GARCIA-MAYORAL,L.GARCIA-ORTEGA,M.P.LILLO,J.SANTORO, JRNL AUTH 2 A.MARTINEZ DEL POZO,J.G.GAVILANES,M.RICO,M.BRUIX JRNL TITL NMR STRUCTURE OF THE NONCYTOTOXIC {ALPHA}-SARCIN MUTANT JRNL TITL 2 {DELTA}(7-22): THE IMPORTANCE OF THE NATIVE CONFORMATION OF JRNL TITL 3 PERIPHERAL LOOPS FOR ACTIVITY. JRNL REF PROTEIN SCI. V. 13 1000 2004 JRNL REFN ISSN 0961-8368 JRNL PMID 15044731 JRNL DOI 10.1110/PS.03532204 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.M.PEREZ-CANADILLAS,R.CAMPOS-OLIVAS,J.LACADENA, REMARK 1 AUTH 2 A.MARTINEZ DEL POZO,J.G.GAVILANES,J.SANTORO,M.RICO,M.BRUIX REMARK 1 TITL CHARACTERIZATION OF PKA VALUES AND TITRATION SHIFTS IN THE REMARK 1 TITL 2 CYTOTOXIC RIBONUCLEASE ALPHA-SARCIN BY NMR. RELATIONSHIP REMARK 1 TITL 3 BETWEEN ELECTROSTATIC INTERACTIONS, STRUCTURE, AND CATALYTIC REMARK 1 TITL 4 FUNCTION. REMARK 1 REF BIOCHEMISTRY V. 37 15865 1998 REMARK 1 REFN ISSN 0006-2960 REMARK 1 DOI 10.1021/BI981672T REMARK 1 REFERENCE 2 REMARK 1 AUTH R.CAMPOS-OLIVAS,M.BRUIX,J.SANTORO,A.MARTINEZ DEL POZO, REMARK 1 AUTH 2 J.LACADENA,J.G.GAVILANES,M.RICO REMARK 1 TITL STRUCTURAL BASIS FOR THE CATALYTIC MECHANISM AND SUBSTRATE REMARK 1 TITL 2 SPECIFICITY OF THE RIBONUCLEASE ALPHA-SARCIN. REMARK 1 REF FEBS LETT. V. 399 163 1996 REMARK 1 REFN ISSN 0014-5793 REMARK 1 DOI 10.1016/S0014-5793(96)01320-8 REMARK 1 REFERENCE 3 REMARK 1 AUTH J.M.PEREZ-CANADILLAS,J.SANTORO,R.CAMPOS-OLIVAS,J.LACADENA, REMARK 1 AUTH 2 A.MARTINEZ DEL POZO,J.G.GAVILANES,M.RICO,M.BRUIX REMARK 1 TITL THE HIGHLY REFINED SOLUTION STRUCTURE OF THE CYTOTOXIC REMARK 1 TITL 2 RIBONUCLEASE ALPHA-SARCIN REVEALS THE STRUCTURAL REMARK 1 TITL 3 REQUIREMENTS FOR SUBSTRATE RECOGNITION AND RIBONUCLEOLYTIC REMARK 1 TITL 4 ACTIVITY. REMARK 1 REF J.MOL.BIOL. V. 299 1061 2000 REMARK 1 REFN ISSN 0022-2836 REMARK 1 DOI 10.1006/JMBI.2000.3813 REMARK 1 REFERENCE 4 REMARK 1 AUTH M.F.GARCIA-MAYORAL,J.M.PEREZ-CANADILLAS,J.SANTORO, REMARK 1 AUTH 2 B.IBARRA-MOLERO,J.M.SANCHEZ-RUIZ,J.LACADENA, REMARK 1 AUTH 3 A.MARTINEZ DEL POZO,J.G.GAVILANES,M.RICO,M.BRUIX REMARK 1 TITL DISSECTING STRUCTURAL AND ELECTROSTATIC INTERACTIONS OF REMARK 1 TITL 2 CHARGED GROUPS IN ALPHA-SARCIN. AN NMR STUDY OF SOME MUTANTS REMARK 1 TITL 3 INVOLVING THE CATALYTIC RESIDUES. REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.1, DYANA 1.5, AMBER 7 REMARK 3 AUTHORS : GUNTERT, P. (DYANA), 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 2088 RESTRAINTS, 1990 NOE-DERIVED DISTANCE CONSTRAINTS AND 98 REMARK 3 DIHEDRAL ANGLE RESTRAINTS. THE BEST 25 REPRESENTATIVE CONFORMERS REMARK 3 ARE ENERGY-MINIMIZED WITH AMBER7 REMARK 4 REMARK 4 1R4Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-03. REMARK 100 THE DEPOSITION ID IS D_1000020442. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM RIBONUCLEASE; 90% H2O, 10% REMARK 210 D2O; 2MM RIBONUCLEASE; D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.1, ANSIG 3.3, DYANA REMARK 210 1.5 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D NOE 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: 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 1 ASP A 88 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES REMARK 500 3 ASP A 88 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES REMARK 500 9 TYR A 42 CB - CG - CD1 ANGL. DEV. = -4.1 DEGREES REMARK 500 13 TYR A 42 CB - CG - CD2 ANGL. DEV. = 3.8 DEGREES REMARK 500 13 TYR A 42 CB - CG - CD1 ANGL. DEV. = -5.0 DEGREES REMARK 500 13 CYS A 62 CA - CB - SG ANGL. DEV. = 7.6 DEGREES REMARK 500 13 THR A 76 CA - CB - CG2 ANGL. DEV. = 9.6 DEGREES REMARK 500 13 PHE A 94 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES REMARK 500 15 TYR A 34 CG - CD2 - CE2 ANGL. DEV. = -4.9 DEGREES REMARK 500 20 ASP A 88 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES REMARK 500 21 TYR A 11 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES REMARK 500 21 TYR A 42 CB - CG - CD1 ANGL. DEV. = -5.6 DEGREES REMARK 500 21 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES REMARK 500 22 CYS A 134 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 24 CYS A 62 CA - CB - SG ANGL. DEV. = 6.9 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 VAL A 2 156.54 -43.63 REMARK 500 1 TYR A 11 85.94 -160.99 REMARK 500 1 ALA A 23 128.78 -35.41 REMARK 500 1 LEU A 25 102.86 -59.47 REMARK 500 1 SER A 26 151.30 178.93 REMARK 500 1 LYS A 29 45.76 -150.06 REMARK 500 1 SER A 32 -77.98 -68.48 REMARK 500 1 SER A 33 -61.73 -178.07 REMARK 500 1 THR A 39 -36.58 -38.91 REMARK 500 1 ASP A 45 -63.87 -133.27 REMARK 500 1 LYS A 47 174.80 -53.16 REMARK 500 1 LYS A 50 97.76 -54.65 REMARK 500 1 ASP A 71 -44.86 -177.79 REMARK 500 1 LYS A 75 -105.12 -73.11 REMARK 500 1 ASP A 77 98.74 -31.56 REMARK 500 1 HIS A 78 44.41 -85.11 REMARK 500 1 ASP A 91 92.04 -61.84 REMARK 500 1 TYR A 92 142.89 -38.32 REMARK 500 1 PRO A 103 -165.75 -72.25 REMARK 500 1 ASN A 114 108.09 -47.72 REMARK 500 1 LYS A 115 79.75 -62.91 REMARK 500 1 PHE A 117 114.12 -36.10 REMARK 500 1 THR A 124 36.53 -98.16 REMARK 500 1 GLU A 126 -63.14 -169.09 REMARK 500 1 ASN A 127 -45.28 -155.50 REMARK 500 1 GLN A 128 75.43 -158.45 REMARK 500 1 CYS A 134 -174.32 -58.59 REMARK 500 2 CYS A 6 -80.40 -126.93 REMARK 500 2 ALA A 23 127.59 -35.74 REMARK 500 2 LEU A 25 93.92 -60.60 REMARK 500 2 SER A 26 162.46 179.20 REMARK 500 2 SER A 32 -78.09 -69.23 REMARK 500 2 SER A 33 -63.75 -179.00 REMARK 500 2 TYR A 42 170.53 -50.64 REMARK 500 2 ASP A 45 -96.29 -85.76 REMARK 500 2 LYS A 50 101.12 -54.89 REMARK 500 2 PHE A 57 -53.87 -125.93 REMARK 500 2 LYS A 67 58.86 -140.03 REMARK 500 2 ASP A 71 -42.40 -177.18 REMARK 500 2 ASN A 73 81.89 -150.11 REMARK 500 2 LYS A 75 -89.34 -52.45 REMARK 500 2 ASP A 77 105.08 -27.05 REMARK 500 2 TYR A 79 132.95 -33.96 REMARK 500 2 ASP A 91 89.72 -64.19 REMARK 500 2 TYR A 92 142.91 -36.41 REMARK 500 2 PRO A 103 -166.46 -73.18 REMARK 500 2 LYS A 115 74.81 -64.87 REMARK 500 2 PHE A 117 107.98 -46.93 REMARK 500 2 THR A 124 38.55 -97.63 REMARK 500 2 GLU A 126 -63.07 -171.03 REMARK 500 REMARK 500 THIS ENTRY HAS 624 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 TYR A 110 0.09 SIDE CHAIN REMARK 500 3 TYR A 110 0.09 SIDE CHAIN REMARK 500 5 TYR A 11 0.09 SIDE CHAIN REMARK 500 7 TYR A 11 0.07 SIDE CHAIN REMARK 500 7 TYR A 110 0.07 SIDE CHAIN REMARK 500 9 TYR A 11 0.10 SIDE CHAIN REMARK 500 9 TYR A 110 0.07 SIDE CHAIN REMARK 500 12 TYR A 110 0.08 SIDE CHAIN REMARK 500 21 TYR A 34 0.12 SIDE CHAIN REMARK 500 21 TYR A 92 0.10 SIDE CHAIN REMARK 500 21 TYR A 112 0.18 SIDE CHAIN REMARK 500 24 TYR A 11 0.07 SIDE CHAIN REMARK 500 24 TYR A 110 0.07 SIDE CHAIN REMARK 500 25 TYR A 11 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1DE3 RELATED DB: PDB REMARK 900 THE WILD TYPE PROTEIN DBREF 1R4Y A 1 136 UNP P00655 RNAS_ASPGI 28 177 SEQADV 1R4Y GLY A 7 UNP P00655 LEU 34 ENGINEERED MUTATION SEQADV 1R4Y A UNP P00655 ASN 35 DELETION SEQADV 1R4Y A UNP P00655 ASP 36 DELETION SEQADV 1R4Y A UNP P00655 GLN 37 DELETION SEQADV 1R4Y A UNP P00655 LYS 38 DELETION SEQADV 1R4Y A UNP P00655 ASN 39 DELETION SEQADV 1R4Y A UNP P00655 PRO 40 DELETION SEQADV 1R4Y A UNP P00655 LYS 41 DELETION SEQADV 1R4Y A UNP P00655 THR 42 DELETION SEQADV 1R4Y A UNP P00655 ASN 43 DELETION SEQADV 1R4Y A UNP P00655 LYS 44 DELETION SEQADV 1R4Y A UNP P00655 TYR 45 DELETION SEQADV 1R4Y A UNP P00655 GLU 46 DELETION SEQADV 1R4Y A UNP P00655 THR 47 DELETION SEQADV 1R4Y A UNP P00655 LYS 48 DELETION SEQADV 1R4Y GLY A 8 UNP P00655 ARG 49 ENGINEERED MUTATION SEQRES 1 A 136 ALA VAL THR TRP THR CYS GLY GLY LEU LEU TYR ASN GLN SEQRES 2 A 136 ASN LYS ALA GLU SER ASN SER HIS HIS ALA PRO LEU SER SEQRES 3 A 136 ASP GLY LYS THR GLY SER SER TYR PRO HIS TRP PHE THR SEQRES 4 A 136 ASN GLY TYR ASP GLY ASP GLY LYS LEU PRO LYS GLY ARG SEQRES 5 A 136 THR PRO ILE LYS PHE GLY LYS SER ASP CYS ASP ARG PRO SEQRES 6 A 136 PRO LYS HIS SER LYS ASP GLY ASN GLY LYS THR ASP HIS SEQRES 7 A 136 TYR LEU LEU GLU PHE PRO THR PHE PRO ASP GLY HIS ASP SEQRES 8 A 136 TYR LYS PHE ASP SER LYS LYS PRO LYS GLU ASN PRO GLY SEQRES 9 A 136 PRO ALA ARG VAL ILE TYR THR TYR PRO ASN LYS VAL PHE SEQRES 10 A 136 CYS GLY ILE ILE ALA HIS THR LYS GLU ASN GLN GLY GLU SEQRES 11 A 136 LEU LYS LEU CYS SER HIS HELIX 1 1 GLN A 13 ALA A 23 1 11 SHEET 1 A 2 THR A 3 THR A 5 0 SHEET 2 A 2 LEU A 10 ASN A 12 -1 O TYR A 11 N TRP A 4 SHEET 1 B 5 HIS A 36 TRP A 37 0 SHEET 2 B 5 LEU A 81 PRO A 84 -1 O GLU A 82 N HIS A 36 SHEET 3 B 5 ARG A 107 TYR A 110 -1 O VAL A 108 N PHE A 83 SHEET 4 B 5 GLY A 119 ALA A 122 -1 O GLY A 119 N ILE A 109 SHEET 5 B 5 LYS A 132 LEU A 133 -1 O LYS A 132 N ALA A 122 SSBOND 1 CYS A 6 CYS A 134 1555 1555 2.00 SSBOND 2 CYS A 62 CYS A 118 1555 1555 2.01 CISPEP 1 TYR A 34 PRO A 35 1 1.45 CISPEP 2 LYS A 98 PRO A 99 1 -2.66 CISPEP 3 TYR A 112 PRO A 113 1 -6.87 CISPEP 4 TYR A 34 PRO A 35 2 -0.74 CISPEP 5 LYS A 98 PRO A 99 2 -2.92 CISPEP 6 TYR A 112 PRO A 113 2 -5.86 CISPEP 7 TYR A 34 PRO A 35 3 3.51 CISPEP 8 LYS A 98 PRO A 99 3 -3.96 CISPEP 9 TYR A 112 PRO A 113 3 -6.62 CISPEP 10 TYR A 34 PRO A 35 4 -1.00 CISPEP 11 LYS A 98 PRO A 99 4 -2.35 CISPEP 12 TYR A 112 PRO A 113 4 -4.35 CISPEP 13 TYR A 34 PRO A 35 5 1.57 CISPEP 14 LYS A 98 PRO A 99 5 -9.18 CISPEP 15 TYR A 112 PRO A 113 5 -10.27 CISPEP 16 TYR A 34 PRO A 35 6 -1.52 CISPEP 17 LYS A 98 PRO A 99 6 -2.87 CISPEP 18 TYR A 112 PRO A 113 6 -4.14 CISPEP 19 TYR A 34 PRO A 35 7 6.57 CISPEP 20 LYS A 98 PRO A 99 7 -5.48 CISPEP 21 TYR A 112 PRO A 113 7 -11.07 CISPEP 22 TYR A 34 PRO A 35 8 0.71 CISPEP 23 LYS A 98 PRO A 99 8 -3.34 CISPEP 24 TYR A 112 PRO A 113 8 -4.98 CISPEP 25 TYR A 34 PRO A 35 9 -2.45 CISPEP 26 LYS A 98 PRO A 99 9 -3.80 CISPEP 27 TYR A 112 PRO A 113 9 -8.41 CISPEP 28 TYR A 34 PRO A 35 10 -3.45 CISPEP 29 LYS A 98 PRO A 99 10 -1.84 CISPEP 30 TYR A 112 PRO A 113 10 -5.44 CISPEP 31 TYR A 34 PRO A 35 11 1.35 CISPEP 32 LYS A 98 PRO A 99 11 -5.13 CISPEP 33 TYR A 112 PRO A 113 11 -6.75 CISPEP 34 TYR A 34 PRO A 35 12 2.24 CISPEP 35 LYS A 98 PRO A 99 12 -3.47 CISPEP 36 TYR A 112 PRO A 113 12 -8.25 CISPEP 37 TYR A 34 PRO A 35 13 -2.73 CISPEP 38 LYS A 98 PRO A 99 13 -11.10 CISPEP 39 TYR A 112 PRO A 113 13 -21.54 CISPEP 40 TYR A 34 PRO A 35 14 -1.87 CISPEP 41 LYS A 98 PRO A 99 14 -3.83 CISPEP 42 TYR A 112 PRO A 113 14 -5.68 CISPEP 43 TYR A 34 PRO A 35 15 0.77 CISPEP 44 LYS A 98 PRO A 99 15 -3.56 CISPEP 45 TYR A 112 PRO A 113 15 -5.68 CISPEP 46 TYR A 34 PRO A 35 16 2.57 CISPEP 47 LYS A 98 PRO A 99 16 -4.44 CISPEP 48 TYR A 112 PRO A 113 16 -5.02 CISPEP 49 TYR A 34 PRO A 35 17 5.15 CISPEP 50 LYS A 98 PRO A 99 17 -5.02 CISPEP 51 TYR A 112 PRO A 113 17 -8.99 CISPEP 52 TYR A 34 PRO A 35 18 -1.54 CISPEP 53 LYS A 98 PRO A 99 18 -6.48 CISPEP 54 TYR A 112 PRO A 113 18 -6.88 CISPEP 55 TYR A 34 PRO A 35 19 -4.13 CISPEP 56 LYS A 98 PRO A 99 19 -9.09 CISPEP 57 TYR A 112 PRO A 113 19 -9.95 CISPEP 58 TYR A 34 PRO A 35 20 0.48 CISPEP 59 LYS A 98 PRO A 99 20 -4.69 CISPEP 60 TYR A 112 PRO A 113 20 -7.43 CISPEP 61 TYR A 34 PRO A 35 21 -7.47 CISPEP 62 LYS A 98 PRO A 99 21 -9.86 CISPEP 63 TYR A 112 PRO A 113 21 -15.84 CISPEP 64 TYR A 34 PRO A 35 22 -1.12 CISPEP 65 LYS A 98 PRO A 99 22 -4.89 CISPEP 66 TYR A 112 PRO A 113 22 -7.80 CISPEP 67 TYR A 34 PRO A 35 23 -0.53 CISPEP 68 LYS A 98 PRO A 99 23 -4.06 CISPEP 69 TYR A 112 PRO A 113 23 -5.43 CISPEP 70 TYR A 34 PRO A 35 24 -4.60 CISPEP 71 LYS A 98 PRO A 99 24 -2.91 CISPEP 72 TYR A 112 PRO A 113 24 -9.21 CISPEP 73 TYR A 34 PRO A 35 25 0.58 CISPEP 74 LYS A 98 PRO A 99 25 -3.80 CISPEP 75 TYR A 112 PRO A 113 25 -5.96 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 - t 27 2 Bytes