Header list of 1sfw.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 23-FEB-96 1SFW TITLE PORCINE PANCREAS PHOSPHOLIPASE A2, NMR, 18 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: PHOSPHOLIPASE A2; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PLA2, PHOSPHATIDYLCHOLINE 2-ACYLHYDROLASE; COMPND 5 EC: 3.1.1.4; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: THIS ENTRY PRESENTS THE SOLUTION STRUCTURE OF THE COMPND 8 ENZYME IN THE PRESENCE OF LIPID MICELLES AND A COMPETITIVE INHIBITOR SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA; SOURCE 3 ORGANISM_COMMON: PIG; SOURCE 4 ORGANISM_TAXID: 9823; SOURCE 5 ORGAN: PANCREAS; SOURCE 6 GENE: PORCINE PANCREAS PLA2; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PAB3 (PGEX T2 DERIVED EXPRESSION SOURCE 10 PLASMID); SOURCE 11 EXPRESSION_SYSTEM_GENE: PORCINE PANCREAS PLA2; SOURCE 12 OTHER_DETAILS: DETAILS CONCERNING THE EXPRESSION OF THE PLA2 CAN BE SOURCE 13 FOUND IN REFERENCES BELOW KEYWDS PHOSPHOLIPASE A2, PHOSPHATIDE-2-ACYL-HYDROLASE, HYDROLASE EXPDTA SOLUTION NMR NUMMDL 18 AUTHOR B.VAN DEN BERG,M.TESSARI,R.BOELENS,R.DIJKMAN,R.KAPTEIN,G.H.DE HAAS, AUTHOR 2 H.M.VERHEIJ REVDAT 4 02-MAR-22 1SFW 1 REMARK LINK REVDAT 3 24-FEB-09 1SFW 1 VERSN REVDAT 2 01-APR-03 1SFW 1 JRNL REVDAT 1 11-JUL-96 1SFW 0 JRNL AUTH B.VAN DEN BERG,M.TESSARI,R.BOELENS,R.DIJKMAN,R.KAPTEIN, JRNL AUTH 2 G.H.DE HAAS,H.M.VERHEIJ JRNL TITL SOLUTION STRUCTURE OF PORCINE PANCREATIC PHOSPHOLIPASE A2 JRNL TITL 2 COMPLEXED WITH MICELLES AND A COMPETITIVE INHIBITOR. JRNL REF J.BIOMOL.NMR V. 5 110 1995 JRNL REFN ISSN 0925-2738 JRNL PMID 7703697 JRNL DOI 10.1007/BF00208802 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH B.VAN DEN BERG,M.TESSARI,G.H.DE HAAS,H.M.VERHEIJ,R.BOELENS, REMARK 1 AUTH 2 R.KAPTEIN REMARK 1 TITL SOLUTION STRUCTURE OF PORCINE PANCREATIC PHOSPHOLIPASE A2 REMARK 1 REF EMBO J. V. 14 4123 1995 REMARK 1 REFN ISSN 0261-4189 REMARK 1 REFERENCE 2 REMARK 1 AUTH B.VAN DEN BERG,M.TESSARI,R.BOELENS,R.DIJKMAN,G.H.DE HAAS, REMARK 1 AUTH 2 R.KAPTEIN,H.M.VERHEIJ REMARK 1 TITL NMR STRUCTURES OF PHOSPHOLIPASE A2 REVEAL CONFORMATIONAL REMARK 1 TITL 2 CHANGES DURING INTERFACIAL ACTIVATION REMARK 1 REF NAT.STRUCT.BIOL. V. 2 402 1995 REMARK 1 REFN ISSN 1072-8368 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER REMARK 3 AUTHORS : BIOSYM REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1SFW 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_1000176357. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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 LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 1 GLU A 40 CD GLU A 40 OE2 0.120 REMARK 500 1 GLU A 46 CD GLU A 46 OE1 0.119 REMARK 500 1 HIS A 48 CG HIS A 48 CD2 0.059 REMARK 500 1 GLU A 71 CD GLU A 71 OE1 0.120 REMARK 500 1 GLU A 81 CD GLU A 81 OE2 0.121 REMARK 500 1 GLU A 92 CD GLU A 92 OE1 0.121 REMARK 500 1 GLU A 114 CD GLU A 114 OE2 0.120 REMARK 500 1 CYS A 124 C CYS A 124 OXT 0.144 REMARK 500 2 GLU A 40 CD GLU A 40 OE2 0.119 REMARK 500 2 GLU A 46 CD GLU A 46 OE2 0.117 REMARK 500 2 HIS A 48 CG HIS A 48 CD2 0.061 REMARK 500 2 GLU A 71 CD GLU A 71 OE1 0.122 REMARK 500 2 GLU A 81 CD GLU A 81 OE1 0.120 REMARK 500 2 GLU A 92 CD GLU A 92 OE2 0.118 REMARK 500 2 GLU A 114 CD GLU A 114 OE1 0.120 REMARK 500 2 CYS A 124 C CYS A 124 OXT 0.143 REMARK 500 3 GLU A 40 CD GLU A 40 OE2 0.120 REMARK 500 3 GLU A 46 CD GLU A 46 OE2 0.118 REMARK 500 3 HIS A 48 CG HIS A 48 CD2 0.056 REMARK 500 3 GLU A 71 CD GLU A 71 OE2 0.117 REMARK 500 3 GLU A 81 CD GLU A 81 OE1 0.120 REMARK 500 3 GLU A 92 CD GLU A 92 OE2 0.116 REMARK 500 3 GLU A 114 CD GLU A 114 OE2 0.120 REMARK 500 3 CYS A 124 C CYS A 124 OXT 0.143 REMARK 500 4 GLU A 40 CD GLU A 40 OE1 0.119 REMARK 500 4 GLU A 46 CD GLU A 46 OE2 0.118 REMARK 500 4 HIS A 48 CG HIS A 48 CD2 0.065 REMARK 500 4 GLU A 71 CD GLU A 71 OE2 0.119 REMARK 500 4 GLU A 81 CD GLU A 81 OE1 0.119 REMARK 500 4 GLU A 92 CD GLU A 92 OE2 0.118 REMARK 500 4 GLU A 114 CD GLU A 114 OE1 0.119 REMARK 500 4 CYS A 124 C CYS A 124 OXT 0.146 REMARK 500 5 GLU A 40 CD GLU A 40 OE2 0.119 REMARK 500 5 GLU A 46 CD GLU A 46 OE2 0.118 REMARK 500 5 HIS A 48 CG HIS A 48 CD2 0.062 REMARK 500 5 GLU A 71 CD GLU A 71 OE2 0.121 REMARK 500 5 GLU A 81 CD GLU A 81 OE1 0.120 REMARK 500 5 GLU A 92 CD GLU A 92 OE2 0.117 REMARK 500 5 GLU A 114 CD GLU A 114 OE2 0.120 REMARK 500 5 CYS A 124 C CYS A 124 OXT 0.145 REMARK 500 6 GLU A 40 CD GLU A 40 OE2 0.120 REMARK 500 6 GLU A 46 CD GLU A 46 OE2 0.118 REMARK 500 6 HIS A 48 CG HIS A 48 CD2 0.065 REMARK 500 6 GLU A 71 CD GLU A 71 OE1 0.120 REMARK 500 6 GLU A 81 CD GLU A 81 OE1 0.120 REMARK 500 6 GLU A 92 CD GLU A 92 OE2 0.119 REMARK 500 6 GLU A 114 CD GLU A 114 OE2 0.119 REMARK 500 6 CYS A 124 C CYS A 124 OXT 0.144 REMARK 500 7 GLU A 40 CD GLU A 40 OE2 0.120 REMARK 500 7 GLU A 46 CD GLU A 46 OE2 0.117 REMARK 500 REMARK 500 THIS ENTRY HAS 140 BOND DEVIATIONS. 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 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES REMARK 500 1 ILE A 13 N - CA - C ANGL. DEV. = -17.1 DEGREES REMARK 500 1 HIS A 17 CB - CG - CD2 ANGL. DEV. = -12.0 DEGREES REMARK 500 1 HIS A 17 CG - ND1 - CE1 ANGL. DEV. = -7.9 DEGREES REMARK 500 1 HIS A 17 ND1 - CE1 - NE2 ANGL. DEV. = 8.5 DEGREES REMARK 500 1 MET A 20 N - CA - CB ANGL. DEV. = -12.8 DEGREES REMARK 500 1 ASP A 21 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES REMARK 500 1 TYR A 28 CB - CG - CD2 ANGL. DEV. = -6.3 DEGREES REMARK 500 1 TYR A 28 CB - CG - CD1 ANGL. DEV. = 6.6 DEGREES REMARK 500 1 LEU A 31 CB - CA - C ANGL. DEV. = 12.5 DEGREES REMARK 500 1 VAL A 38 CG1 - CB - CG2 ANGL. DEV. = -10.2 DEGREES REMARK 500 1 ASP A 39 CB - CG - OD1 ANGL. DEV. = -6.5 DEGREES REMARK 500 1 ASP A 39 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES REMARK 500 1 ASP A 42 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES REMARK 500 1 ARG A 43 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 1 HIS A 48 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES REMARK 500 1 ASP A 49 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES REMARK 500 1 ASP A 49 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES REMARK 500 1 ARG A 53 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES REMARK 500 1 ASP A 54 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES REMARK 500 1 ASP A 59 CB - CG - OD1 ANGL. DEV. = -6.1 DEGREES REMARK 500 1 ASP A 66 CB - CG - OD1 ANGL. DEV. = -5.6 DEGREES REMARK 500 1 TYR A 73 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES REMARK 500 1 TYR A 75 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES REMARK 500 1 TYR A 75 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES REMARK 500 1 ILE A 82 CB - CA - C ANGL. DEV. = 12.1 DEGREES REMARK 500 1 CYS A 84 N - CA - CB ANGL. DEV. = 11.4 DEGREES REMARK 500 1 ASP A 99 CB - CG - OD1 ANGL. DEV. = -6.1 DEGREES REMARK 500 1 ARG A 100 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES REMARK 500 1 PHE A 106 CB - CG - CD2 ANGL. DEV. = -7.0 DEGREES REMARK 500 1 PHE A 106 CB - CG - CD1 ANGL. DEV. = 7.0 DEGREES REMARK 500 1 TYR A 111 CB - CG - CD2 ANGL. DEV. = 6.3 DEGREES REMARK 500 1 TYR A 111 CB - CG - CD1 ANGL. DEV. = -7.8 DEGREES REMARK 500 1 GLU A 114 CB - CA - C ANGL. DEV. = 13.9 DEGREES REMARK 500 1 GLU A 114 N - CA - CB ANGL. DEV. = -11.2 DEGREES REMARK 500 1 HIS A 115 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES REMARK 500 1 LYS A 116 N - CA - CB ANGL. DEV. = -12.2 DEGREES REMARK 500 1 LEU A 118 CB - CG - CD1 ANGL. DEV. = 17.9 DEGREES REMARK 500 1 ASP A 119 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES REMARK 500 1 LYS A 122 N - CA - CB ANGL. DEV. = -14.4 DEGREES REMARK 500 1 TYR A 123 N - CA - CB ANGL. DEV. = -17.4 DEGREES REMARK 500 1 TYR A 123 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 1 CYS A 124 CB - CA - C ANGL. DEV. = 7.8 DEGREES REMARK 500 2 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES REMARK 500 2 HIS A 17 CB - CG - CD2 ANGL. DEV. = -12.8 DEGREES REMARK 500 2 HIS A 17 CG - ND1 - CE1 ANGL. DEV. = -8.1 DEGREES REMARK 500 2 HIS A 17 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES REMARK 500 2 ASP A 21 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES REMARK 500 2 LEU A 31 CA - C - N ANGL. DEV. = -13.5 DEGREES REMARK 500 2 ASP A 39 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 731 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 ARG A 6 44.95 -84.31 REMARK 500 1 SER A 16 -109.60 -155.90 REMARK 500 1 LEU A 19 -115.27 -68.18 REMARK 500 1 MET A 20 -29.15 5.16 REMARK 500 1 ASP A 21 -5.85 -54.89 REMARK 500 1 PHE A 22 -44.00 -141.01 REMARK 500 1 ASN A 24 -83.35 -85.85 REMARK 500 1 TYR A 25 -165.09 43.40 REMARK 500 1 CYS A 27 -48.10 -135.22 REMARK 500 1 TYR A 28 7.61 -163.41 REMARK 500 1 LEU A 31 -75.24 -96.83 REMARK 500 1 PRO A 37 -151.67 -88.12 REMARK 500 1 VAL A 38 -58.78 -132.22 REMARK 500 1 ASP A 49 -64.85 165.48 REMARK 500 1 LEU A 58 140.93 -37.33 REMARK 500 1 ASN A 67 120.68 83.65 REMARK 500 1 THR A 70 -46.33 -172.49 REMARK 500 1 SER A 72 -165.53 -100.17 REMARK 500 1 TYR A 73 137.69 109.00 REMARK 500 1 SER A 74 69.99 -174.20 REMARK 500 1 TYR A 75 -136.46 -103.38 REMARK 500 1 SER A 76 -169.26 -170.62 REMARK 500 1 CYS A 77 145.35 175.35 REMARK 500 1 SER A 78 -135.00 -124.32 REMARK 500 1 ASN A 79 -34.10 -37.52 REMARK 500 1 THR A 80 -7.41 166.29 REMARK 500 1 ILE A 82 -119.19 -115.64 REMARK 500 1 THR A 83 -98.27 -170.20 REMARK 500 1 CYS A 84 -70.38 175.09 REMARK 500 1 SER A 86 58.28 -147.06 REMARK 500 1 LYS A 87 -65.10 -158.61 REMARK 500 1 ASN A 88 84.32 61.70 REMARK 500 1 CYS A 91 -56.11 -18.72 REMARK 500 1 GLU A 92 -65.79 -94.31 REMARK 500 1 LYS A 108 -72.11 -137.95 REMARK 500 1 ALA A 109 -169.52 32.34 REMARK 500 1 LYS A 113 76.25 -114.18 REMARK 500 1 GLU A 114 -58.88 -160.49 REMARK 500 1 ASN A 117 -44.74 91.19 REMARK 500 1 LEU A 118 -135.07 21.66 REMARK 500 1 ASP A 119 178.66 143.69 REMARK 500 1 LYS A 121 -69.94 -151.38 REMARK 500 2 SER A 7 -67.75 -107.71 REMARK 500 2 SER A 16 -114.65 -105.07 REMARK 500 2 LEU A 19 -120.52 -72.59 REMARK 500 2 MET A 20 -32.81 -0.74 REMARK 500 2 ASP A 21 -12.11 -46.63 REMARK 500 2 PHE A 22 -24.97 -148.84 REMARK 500 2 TYR A 25 100.02 -162.59 REMARK 500 2 CYS A 29 -65.79 -7.39 REMARK 500 REMARK 500 THIS ENTRY HAS 740 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 PRO A 14 GLY A 15 1 118.49 REMARK 500 MET A 20 ASP A 21 1 133.31 REMARK 500 LEU A 31 GLY A 32 1 -147.26 REMARK 500 ARG A 53 ASP A 54 1 -149.88 REMARK 500 LEU A 64 VAL A 65 1 -146.09 REMARK 500 ASN A 88 ASN A 89 1 143.33 REMARK 500 LYS A 113 GLU A 114 1 -139.56 REMARK 500 LEU A 118 ASP A 119 1 -128.66 REMARK 500 PRO A 14 GLY A 15 2 116.71 REMARK 500 MET A 20 ASP A 21 2 130.83 REMARK 500 TYR A 28 CYS A 29 2 -123.24 REMARK 500 LEU A 31 GLY A 32 2 127.00 REMARK 500 ASN A 88 ASN A 89 2 149.94 REMARK 500 LYS A 113 GLU A 114 2 -136.79 REMARK 500 ARG A 6 SER A 7 3 148.70 REMARK 500 PRO A 14 GLY A 15 3 132.67 REMARK 500 MET A 20 ASP A 21 3 134.44 REMARK 500 GLY A 26 CYS A 27 3 138.71 REMARK 500 THR A 36 PRO A 37 3 -147.66 REMARK 500 LEU A 64 VAL A 65 3 137.13 REMARK 500 SER A 76 CYS A 77 3 -149.93 REMARK 500 ASN A 88 ASN A 89 3 146.31 REMARK 500 LYS A 113 GLU A 114 3 -136.27 REMARK 500 SER A 7 MET A 8 4 143.48 REMARK 500 PRO A 14 GLY A 15 4 -122.39 REMARK 500 MET A 20 ASP A 21 4 129.58 REMARK 500 THR A 70 GLU A 71 4 133.29 REMARK 500 TYR A 75 SER A 76 4 -148.76 REMARK 500 SER A 76 CYS A 77 4 -148.21 REMARK 500 ASN A 88 ASN A 89 4 140.04 REMARK 500 LYS A 113 GLU A 114 4 -137.38 REMARK 500 PRO A 14 GLY A 15 5 119.19 REMARK 500 MET A 20 ASP A 21 5 149.27 REMARK 500 TYR A 28 CYS A 29 5 -144.80 REMARK 500 LEU A 31 GLY A 32 5 -147.47 REMARK 500 TYR A 69 THR A 70 5 147.05 REMARK 500 THR A 70 GLU A 71 5 138.39 REMARK 500 SER A 74 TYR A 75 5 -147.86 REMARK 500 LYS A 113 GLU A 114 5 -136.23 REMARK 500 LEU A 118 ASP A 119 5 -140.89 REMARK 500 PRO A 14 GLY A 15 6 114.37 REMARK 500 MET A 20 ASP A 21 6 129.69 REMARK 500 LEU A 31 GLY A 32 6 -148.42 REMARK 500 THR A 47 HIS A 48 6 143.98 REMARK 500 ASN A 50 CYS A 51 6 148.72 REMARK 500 LEU A 64 VAL A 65 6 -140.32 REMARK 500 ASN A 88 ASN A 89 6 140.05 REMARK 500 LYS A 113 GLU A 114 6 -138.43 REMARK 500 LEU A 118 ASP A 119 6 -120.08 REMARK 500 PRO A 14 GLY A 15 7 123.12 REMARK 500 REMARK 500 THIS ENTRY HAS 142 NON CIS, NON-TRANS OMEGA 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 25 0.09 SIDE CHAIN REMARK 500 1 TYR A 52 0.08 SIDE CHAIN REMARK 500 1 TYR A 69 0.12 SIDE CHAIN REMARK 500 1 TYR A 73 0.12 SIDE CHAIN REMARK 500 1 TYR A 75 0.12 SIDE CHAIN REMARK 500 1 HIS A 115 0.21 SIDE CHAIN REMARK 500 1 TYR A 123 0.07 SIDE CHAIN REMARK 500 2 PHE A 22 0.11 SIDE CHAIN REMARK 500 2 TYR A 25 0.11 SIDE CHAIN REMARK 500 2 TYR A 52 0.10 SIDE CHAIN REMARK 500 2 TYR A 69 0.15 SIDE CHAIN REMARK 500 2 TYR A 73 0.11 SIDE CHAIN REMARK 500 2 TYR A 75 0.13 SIDE CHAIN REMARK 500 2 TYR A 111 0.07 SIDE CHAIN REMARK 500 2 HIS A 115 0.21 SIDE CHAIN REMARK 500 2 TYR A 123 0.13 SIDE CHAIN REMARK 500 3 PHE A 22 0.09 SIDE CHAIN REMARK 500 3 TYR A 25 0.12 SIDE CHAIN REMARK 500 3 TYR A 28 0.16 SIDE CHAIN REMARK 500 3 TYR A 52 0.09 SIDE CHAIN REMARK 500 3 TYR A 69 0.09 SIDE CHAIN REMARK 500 3 TYR A 73 0.12 SIDE CHAIN REMARK 500 3 TYR A 75 0.10 SIDE CHAIN REMARK 500 3 TYR A 111 0.08 SIDE CHAIN REMARK 500 3 HIS A 115 0.21 SIDE CHAIN REMARK 500 3 TYR A 123 0.14 SIDE CHAIN REMARK 500 4 PHE A 22 0.11 SIDE CHAIN REMARK 500 4 TYR A 25 0.12 SIDE CHAIN REMARK 500 4 TYR A 52 0.09 SIDE CHAIN REMARK 500 4 TYR A 69 0.08 SIDE CHAIN REMARK 500 4 TYR A 73 0.09 SIDE CHAIN REMARK 500 4 TYR A 75 0.13 SIDE CHAIN REMARK 500 4 PHE A 94 0.07 SIDE CHAIN REMARK 500 4 HIS A 115 0.21 SIDE CHAIN REMARK 500 5 TYR A 28 0.09 SIDE CHAIN REMARK 500 5 TYR A 52 0.10 SIDE CHAIN REMARK 500 5 TYR A 69 0.12 SIDE CHAIN REMARK 500 5 TYR A 75 0.07 SIDE CHAIN REMARK 500 5 TYR A 111 0.07 SIDE CHAIN REMARK 500 5 HIS A 115 0.22 SIDE CHAIN REMARK 500 5 TYR A 123 0.10 SIDE CHAIN REMARK 500 6 PHE A 22 0.13 SIDE CHAIN REMARK 500 6 TYR A 25 0.09 SIDE CHAIN REMARK 500 6 TYR A 52 0.11 SIDE CHAIN REMARK 500 6 TYR A 75 0.07 SIDE CHAIN REMARK 500 6 TYR A 111 0.07 SIDE CHAIN REMARK 500 6 HIS A 115 0.20 SIDE CHAIN REMARK 500 6 TYR A 123 0.09 SIDE CHAIN REMARK 500 7 PHE A 22 0.08 SIDE CHAIN REMARK 500 7 TYR A 25 0.09 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 142 PLANE DEVIATIONS. 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 5 LEU A 19 11.96 REMARK 500 8 LEU A 19 10.28 REMARK 500 9 LEU A 19 12.49 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 125 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 TYR A 28 O REMARK 620 2 LEU A 31 O 78.2 REMARK 620 3 GLY A 33 O 97.9 89.7 REMARK 620 4 ASP A 49 OD2 120.7 149.6 109.0 REMARK 620 5 ASP A 49 OD1 131.2 109.7 129.2 40.0 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: CA REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: CATALYTIC CALCIUM ION (COFACTOR). REMARK 800 REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 125 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1SFV RELATED DB: PDB DBREF 1SFW A 1 124 UNP P00592 PA21B_PIG 23 146 SEQRES 1 A 124 ALA LEU TRP GLN PHE ARG SER MET ILE LYS CYS ALA ILE SEQRES 2 A 124 PRO GLY SER HIS PRO LEU MET ASP PHE ASN ASN TYR GLY SEQRES 3 A 124 CYS TYR CYS GLY LEU GLY GLY SER GLY THR PRO VAL ASP SEQRES 4 A 124 GLU LEU ASP ARG CYS CYS GLU THR HIS ASP ASN CYS TYR SEQRES 5 A 124 ARG ASP ALA LYS ASN LEU ASP SER CYS LYS PHE LEU VAL SEQRES 6 A 124 ASP ASN PRO TYR THR GLU SER TYR SER TYR SER CYS SER SEQRES 7 A 124 ASN THR GLU ILE THR CYS ASN SER LYS ASN ASN ALA CYS SEQRES 8 A 124 GLU ALA PHE ILE CYS ASN CYS ASP ARG ASN ALA ALA ILE SEQRES 9 A 124 CYS PHE SER LYS ALA PRO TYR ASN LYS GLU HIS LYS ASN SEQRES 10 A 124 LEU ASP THR LYS LYS TYR CYS HET CA A 125 1 HETNAM CA CALCIUM ION FORMUL 2 CA CA 2+ HELIX 1 1 LEU A 2 ALA A 12 1 11 HELIX 2 2 GLU A 40 ASN A 50 1 11 HELIX 3 3 ARG A 53 ALA A 55 5 3 HELIX 4 4 ALA A 90 PHE A 106 1 17 SSBOND 1 CYS A 11 CYS A 77 1555 1555 1.99 SSBOND 2 CYS A 27 CYS A 124 1555 1555 1.97 SSBOND 3 CYS A 29 CYS A 45 1555 1555 1.99 SSBOND 4 CYS A 44 CYS A 105 1555 1555 1.99 SSBOND 5 CYS A 51 CYS A 98 1555 1555 2.01 SSBOND 6 CYS A 61 CYS A 91 1555 1555 2.02 SSBOND 7 CYS A 84 CYS A 96 1555 1555 1.98 LINK O TYR A 28 CA CA A 125 1555 1555 3.35 LINK O LEU A 31 CA CA A 125 1555 1555 3.08 LINK O GLY A 33 CA CA A 125 1555 1555 3.20 LINK OD2 ASP A 49 CA CA A 125 1555 1555 3.35 LINK OD1 ASP A 49 CA CA A 125 1555 1555 3.37 SITE 1 CA 1 CA A 125 SITE 1 AC1 4 TYR A 28 LEU A 31 GLY A 33 ASP A 49 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 - r 2 2 Bytes