Header list of 1nkl.pdb file
Complete list - b 23 2 Bytes
HEADER SAPOSIN FOLD 17-APR-97 1NKL TITLE NK-LYSIN FROM PIG, NMR, 20 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: NK-LYSIN; COMPND 3 CHAIN: A; COMPND 4 OTHER_DETAILS: ACTIVE BY MEMBRANE-BINDING SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA; SOURCE 3 ORGANISM_COMMON: PIG; SOURCE 4 ORGANISM_TAXID: 9823; SOURCE 5 ORGAN: INTESTINE KEYWDS SAPOSIN FOLD, ANTIBACTERIAL PEPTIDE, TUMOUROLYTIC PEPTIDE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR G.OTTING,E.LIEPINSH REVDAT 3 23-FEB-22 1NKL 1 REMARK SEQADV REVDAT 2 24-FEB-09 1NKL 1 VERSN REVDAT 1 16-JUN-97 1NKL 0 JRNL AUTH E.LIEPINSH,M.ANDERSSON,J.M.RUYSSCHAERT,G.OTTING JRNL TITL SAPOSIN FOLD REVEALED BY THE NMR STRUCTURE OF NK-LYSIN. JRNL REF NAT.STRUCT.BIOL. V. 4 793 1997 JRNL REFN ISSN 1072-8368 JRNL PMID 9334742 JRNL DOI 10.1038/NSB1097-793 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : OPAL REMARK 3 AUTHORS : LUGINBUHL,GUNTERT,BILLETER,WUTHRICH REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: USING DEFAULT PARAMETERS PROVIDED BY REMARK 3 THE PROGRAM WITH RESTRAINTS FOR PEPTIDE BOND PLANARITY. PROGRAM REMARK 3 DIANA BY GUNTERT, BRAUN, WUTHRICH ALSO WAS USED. REMARK 4 REMARK 4 1NKL 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_1000175320. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 309 REMARK 210 PH : 5.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : DMX600; UNITY750 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DIANA, OPAL REMARK 210 METHOD USED : VARIABLE TARGET FUNCTION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION 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: 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 OE1 GLU A 24 HG SER A 57 1.54 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 VAL A 34 CA - CB - CG1 ANGL. DEV. = 10.7 DEGREES REMARK 500 2 VAL A 34 CA - CB - CG1 ANGL. DEV. = 10.0 DEGREES REMARK 500 3 VAL A 34 CA - CB - CG1 ANGL. DEV. = 9.7 DEGREES REMARK 500 4 VAL A 34 CA - CB - CG1 ANGL. DEV. = 9.2 DEGREES REMARK 500 5 VAL A 34 CA - CB - CG1 ANGL. DEV. = 9.2 DEGREES REMARK 500 5 ASP A 36 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES REMARK 500 6 VAL A 34 CA - CB - CG1 ANGL. DEV. = 11.1 DEGREES REMARK 500 7 VAL A 34 CA - CB - CG1 ANGL. DEV. = 9.2 DEGREES REMARK 500 8 VAL A 34 CA - CB - CG1 ANGL. DEV. = 9.0 DEGREES REMARK 500 9 VAL A 34 CA - CB - CG1 ANGL. DEV. = 9.9 DEGREES REMARK 500 9 ASP A 59 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES REMARK 500 10 VAL A 34 CA - CB - CG1 ANGL. DEV. = 11.1 DEGREES REMARK 500 10 ASP A 59 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES REMARK 500 11 VAL A 34 CA - CB - CG1 ANGL. DEV. = 11.1 DEGREES REMARK 500 11 ASP A 59 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES REMARK 500 12 VAL A 34 CA - CB - CG1 ANGL. DEV. = 10.7 DEGREES REMARK 500 13 VAL A 34 CA - CB - CG1 ANGL. DEV. = 10.7 DEGREES REMARK 500 14 VAL A 34 CA - CB - CG1 ANGL. DEV. = 10.4 DEGREES REMARK 500 15 VAL A 34 CA - CB - CG1 ANGL. DEV. = 10.0 DEGREES REMARK 500 16 VAL A 34 CA - CB - CG1 ANGL. DEV. = 10.5 DEGREES REMARK 500 16 ASP A 36 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES REMARK 500 17 VAL A 34 CA - CB - CG1 ANGL. DEV. = 10.0 DEGREES REMARK 500 18 VAL A 34 CA - CB - CG1 ANGL. DEV. = 10.1 DEGREES REMARK 500 18 LYS A 39 CB - CA - C ANGL. DEV. = 13.4 DEGREES REMARK 500 19 VAL A 34 CA - CB - CG1 ANGL. DEV. = 10.6 DEGREES REMARK 500 20 VAL A 34 CA - CB - CG1 ANGL. DEV. = 10.9 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 TYR A 2 -60.36 57.91 REMARK 500 1 PHE A 3 -38.56 -29.41 REMARK 500 1 GLN A 21 66.34 20.15 REMARK 500 1 ILE A 40 -64.92 75.17 REMARK 500 1 PHE A 52 39.77 -144.06 REMARK 500 1 LYS A 74 73.40 65.91 REMARK 500 1 CYS A 76 -94.09 -83.24 REMARK 500 1 LYS A 77 80.65 172.67 REMARK 500 2 GLN A 21 79.21 -0.45 REMARK 500 2 ILE A 40 -61.75 74.44 REMARK 500 2 LEU A 53 -70.53 -61.04 REMARK 500 2 LYS A 74 77.49 68.22 REMARK 500 2 CYS A 76 -83.89 -83.60 REMARK 500 2 LYS A 77 54.80 -149.61 REMARK 500 3 PHE A 3 -38.63 -38.46 REMARK 500 3 GLN A 21 60.18 33.49 REMARK 500 3 PRO A 22 -162.66 -78.90 REMARK 500 3 ILE A 40 -69.18 68.89 REMARK 500 3 PHE A 52 38.52 -144.16 REMARK 500 3 LYS A 74 81.47 61.52 REMARK 500 3 CYS A 76 -103.53 -83.78 REMARK 500 3 LYS A 77 82.19 -173.76 REMARK 500 4 TYR A 2 -47.58 61.38 REMARK 500 4 GLN A 21 65.88 22.31 REMARK 500 4 PRO A 22 -167.75 -78.20 REMARK 500 4 ILE A 40 -61.63 69.71 REMARK 500 4 PHE A 52 38.40 -148.79 REMARK 500 4 THR A 62 30.15 -89.07 REMARK 500 4 LYS A 74 76.78 69.62 REMARK 500 4 ILE A 75 -27.00 -141.52 REMARK 500 5 GLN A 21 93.06 -28.00 REMARK 500 5 ILE A 40 -60.85 75.82 REMARK 500 5 PHE A 52 39.23 -143.86 REMARK 500 5 LYS A 74 87.03 72.86 REMARK 500 5 CYS A 76 -87.69 -88.67 REMARK 500 5 LYS A 77 71.20 -156.99 REMARK 500 6 GLN A 21 59.53 29.22 REMARK 500 6 ILE A 40 -49.90 79.10 REMARK 500 6 LYS A 74 80.45 69.08 REMARK 500 6 ILE A 75 -24.07 -140.91 REMARK 500 6 CYS A 76 -84.58 -84.17 REMARK 500 6 LYS A 77 69.01 -163.11 REMARK 500 7 TYR A 2 -60.20 61.50 REMARK 500 7 PHE A 3 -38.92 -29.34 REMARK 500 7 GLN A 21 58.99 34.85 REMARK 500 7 ILE A 40 -52.61 81.07 REMARK 500 7 LYS A 74 75.98 61.81 REMARK 500 7 CYS A 76 -100.86 -82.90 REMARK 500 7 LYS A 77 71.23 -171.01 REMARK 500 8 TYR A 2 -48.43 61.55 REMARK 500 REMARK 500 THIS ENTRY HAS 123 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 2 0.12 SIDE CHAIN REMARK 500 1 ASP A 16 0.09 SIDE CHAIN REMARK 500 2 TYR A 2 0.08 SIDE CHAIN REMARK 500 2 ARG A 42 0.09 SIDE CHAIN REMARK 500 3 TYR A 2 0.12 SIDE CHAIN REMARK 500 3 ARG A 54 0.10 SIDE CHAIN REMARK 500 5 TYR A 2 0.11 SIDE CHAIN REMARK 500 8 ASP A 16 0.08 SIDE CHAIN REMARK 500 9 ASP A 16 0.08 SIDE CHAIN REMARK 500 10 TYR A 2 0.11 SIDE CHAIN REMARK 500 11 TYR A 2 0.13 SIDE CHAIN REMARK 500 11 ARG A 54 0.08 SIDE CHAIN REMARK 500 12 ASP A 16 0.10 SIDE CHAIN REMARK 500 12 ARG A 42 0.08 SIDE CHAIN REMARK 500 13 ASP A 16 0.10 SIDE CHAIN REMARK 500 14 ASP A 16 0.08 SIDE CHAIN REMARK 500 15 ASP A 16 0.08 SIDE CHAIN REMARK 500 15 ARG A 42 0.08 SIDE CHAIN REMARK 500 16 ASP A 16 0.07 SIDE CHAIN REMARK 500 17 TYR A 2 0.10 SIDE CHAIN REMARK 500 18 ASP A 16 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 3 LYS A 77 10.96 REMARK 500 REMARK 500 REMARK: NULL DBREF 1NKL A 1 78 UNP Q29075 NKL_PIG 47 124 SEQADV 1NKL TYR A 2 UNP Q29075 LEU 48 CONFLICT SEQADV 1NKL PHE A 3 UNP Q29075 ILE 49 CONFLICT SEQADV 1NKL GLN A 33 UNP Q29075 ARG 79 CONFLICT SEQADV 1NKL LEU A 38 UNP Q29075 MET 84 CONFLICT SEQADV 1NKL LEU A 44 UNP Q29075 VAL 90 CONFLICT SEQADV 1NKL SER A 51 UNP Q29075 THR 97 CONFLICT SEQADV 1NKL TRP A 58 UNP Q29075 LYS 104 CONFLICT SEQRES 1 A 78 GLY TYR PHE CYS GLU SER CYS ARG LYS ILE ILE GLN LYS SEQRES 2 A 78 LEU GLU ASP MET VAL GLY PRO GLN PRO ASN GLU ASP THR SEQRES 3 A 78 VAL THR GLN ALA ALA SER GLN VAL CYS ASP LYS LEU LYS SEQRES 4 A 78 ILE LEU ARG GLY LEU CYS LYS LYS ILE MET ARG SER PHE SEQRES 5 A 78 LEU ARG ARG ILE SER TRP ASP ILE LEU THR GLY LYS LYS SEQRES 6 A 78 PRO GLN ALA ILE CYS VAL ASP ILE LYS ILE CYS LYS GLU HELIX 1 1 PHE A 3 VAL A 18 1 16 HELIX 2 2 GLU A 24 LYS A 37 1 14 HELIX 3 3 ARG A 42 SER A 51 1 10 HELIX 4 4 LEU A 53 LEU A 61 1 9 HELIX 5 5 PRO A 66 ASP A 72 1 7 SSBOND 1 CYS A 4 CYS A 76 1555 1555 2.04 SSBOND 2 CYS A 7 CYS A 70 1555 1555 2.03 SSBOND 3 CYS A 35 CYS A 45 1555 1555 2.01 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