Header list of 2ca7.pdb file
Complete list - n 15 2 Bytes
HEADER TOXIN 19-DEC-05 2CA7 TITLE CONKUNITZIN-S1 IS THE FIRST MEMBER OF A NEW KUNITZ-TYPE NEUROTOXIN TITLE 2 FAMILY- STRUCTURAL AND FUNCTIONAL CHARACTERIZATION COMPND MOL_ID: 1; COMPND 2 MOLECULE: CONKUNITZIN-S1; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: DISULFIDE BONDS BETWEEN C7-C57 AND C32-C53 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CONUS STRIATUS; SOURCE 3 ORGANISM_TAXID: 6493; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_VECTOR: PTWIN1 KEYWDS CONKUNITZIN, NEUROTOXIN, TOXIN, KUNITZ-TYPE FOLD, POTASSIUM CHANNEL KEYWDS 2 INHIBITOR, KUNITZ-DOMAIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.BAYRHUBER,V.VIJAYAN,M.FERBER,R.GRAF,J.KORUKOTTU,J.IMPERIAL, AUTHOR 2 J.E.GARRETT,B.M.OLIVERA,H.TERLAU,M.ZWECKSTETTER,S.BECKER REVDAT 4 15-JAN-20 2CA7 1 REMARK REVDAT 3 17-JAN-18 2CA7 1 SOURCE JRNL REVDAT 2 24-FEB-09 2CA7 1 VERSN REVDAT 1 05-JAN-06 2CA7 0 SPRSDE 19-DEC-05 2CA7 1YL2 JRNL AUTH M.BAYRHUBER,V.VIJAYAN,M.FERBER,R.GRAF,J.KORUKOTTU, JRNL AUTH 2 J.IMPERIAL,J.E.GARRETT,B.M.OLIVERA,H.TERLAU,M.ZWECKSTETTER, JRNL AUTH 3 S.BECKER JRNL TITL CONKUNITZIN-S1 IS THE FIRST MEMBER OF A NEW KUNITZ-TYPE JRNL TITL 2 NEUROTOXIN FAMILY. STRUCTURAL AND FUNCTIONAL JRNL TITL 3 CHARACTERIZATION. JRNL REF J. BIOL. CHEM. V. 280 23766 2005 JRNL REFN ISSN 0021-9258 JRNL PMID 15833744 JRNL DOI 10.1074/JBC.C500064200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XPLOR-NIH 2.9.7 REMARK 3 AUTHORS : NILGES M. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2CA7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-DEC-05. REMARK 100 THE DEPOSITION ID IS D_1290026888. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300.0 REMARK 210 PH : 5.2 REMARK 210 IONIC STRENGTH : 100 REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : 100MM SODIUM ACETATE/10% REMARK 210 D2O,0.5MM U-15N- CONKUNITZIN-S1; REMARK 210 100MM SODIUM ACETATE/10% D2O, REMARK 210 1MM U-15N/13C- CONKUNITZIN-S1 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 700 MHZ; 800 MHZ; 900 REMARK 210 MHZ REMARK 210 SPECTROMETER MODEL : OTHER REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.5, NMRPIPE 027.12.56, REMARK 210 NMRDRAW 2004.245.17.31, SPARKY REMARK 210 110, ARIA2ALPHA, CYANA 32, MARS REMARK 210 1.0 REMARK 210 METHOD USED : MOLECULAR DYNAMICS, SIMULATED REMARK 210 ANNEALING, TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 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: NONE 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 O LYS A 1 N ASP A 2 0.34 REMARK 500 C ASP A 2 H ARG A 3 0.53 REMARK 500 O ASP A 2 N ARG A 3 0.56 REMARK 500 O ASP A 2 H ARG A 3 0.68 REMARK 500 O LYS A 1 CB ASP A 2 0.84 REMARK 500 CA LYS A 1 N ASP A 2 0.85 REMARK 500 O LYS A 1 CA ASP A 2 0.86 REMARK 500 C LYS A 1 CB ASP A 2 0.90 REMARK 500 C LYS A 1 CA ASP A 2 0.91 REMARK 500 O LYS A 1 OD1 ASP A 2 1.08 REMARK 500 N LYS A 1 N ASP A 2 1.09 REMARK 500 O LYS A 1 CG ASP A 2 1.14 REMARK 500 C LYS A 1 OD1 ASP A 2 1.15 REMARK 500 C LYS A 1 CG ASP A 2 1.20 REMARK 500 CA LYS A 1 CB ASP A 2 1.32 REMARK 500 CA LYS A 1 CA ASP A 2 1.39 REMARK 500 C THR A 38 H GLY A 39 1.51 REMARK 500 N LYS A 1 CA ASP A 2 1.52 REMARK 500 CA LYS A 1 CG ASP A 2 1.56 REMARK 500 O LYS A 1 OD2 ASP A 2 1.57 REMARK 500 CA LYS A 1 OD1 ASP A 2 1.57 REMARK 500 CB LYS A 1 N ASP A 2 1.58 REMARK 500 C LYS A 1 OD2 ASP A 2 1.61 REMARK 500 N LYS A 1 CB ASP A 2 1.62 REMARK 500 O ASP A 2 CA ARG A 3 1.67 REMARK 500 CB LYS A 1 CB ASP A 2 1.73 REMARK 500 REMARK 500 REMARK: NULL 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 LYS A 1 N LYS A 1 CA -0.701 REMARK 500 1 LYS A 1 CA LYS A 1 CB -0.581 REMARK 500 1 LYS A 1 CB LYS A 1 CG -0.623 REMARK 500 1 LYS A 1 CG LYS A 1 CD -0.686 REMARK 500 1 LYS A 1 CD LYS A 1 CE -0.943 REMARK 500 1 LYS A 1 CE LYS A 1 NZ -0.727 REMARK 500 1 LYS A 1 CA LYS A 1 C -1.037 REMARK 500 1 LYS A 1 C LYS A 1 O -1.134 REMARK 500 1 LYS A 1 C ASP A 2 N -0.971 REMARK 500 1 ASP A 2 N ASP A 2 CA -0.916 REMARK 500 1 ASP A 2 CA ASP A 2 CB -0.837 REMARK 500 1 ASP A 2 CB ASP A 2 CG -1.139 REMARK 500 1 ASP A 2 CG ASP A 2 OD1 -0.967 REMARK 500 1 ASP A 2 CG ASP A 2 OD2 -0.695 REMARK 500 1 ASP A 2 C ASP A 2 O -0.701 REMARK 500 1 ASP A 2 C ARG A 3 N -0.612 REMARK 500 1 ARG A 3 CA ARG A 3 CB -0.175 REMARK 500 1 ARG A 3 CB ARG A 3 CG -0.547 REMARK 500 1 ARG A 3 CG ARG A 3 CD -0.557 REMARK 500 1 ARG A 3 CD ARG A 3 NE -0.529 REMARK 500 1 ARG A 3 NE ARG A 3 CZ -0.456 REMARK 500 1 ARG A 3 CZ ARG A 3 NH1 -0.932 REMARK 500 1 ARG A 3 CZ ARG A 3 NH2 -0.558 REMARK 500 1 SER A 5 CB SER A 5 OG -0.300 REMARK 500 1 LEU A 6 CB LEU A 6 CG -0.504 REMARK 500 1 LEU A 6 CG LEU A 6 CD1 -0.381 REMARK 500 1 LEU A 6 CG LEU A 6 CD2 -0.754 REMARK 500 1 CYS A 7 CB CYS A 7 SG -0.382 REMARK 500 1 ASP A 8 CG ASP A 8 OD1 -0.784 REMARK 500 1 ASP A 8 CG ASP A 8 OD2 -0.539 REMARK 500 1 LEU A 9 CB LEU A 9 CG -0.687 REMARK 500 1 LEU A 9 CG LEU A 9 CD1 -0.920 REMARK 500 1 LEU A 9 CG LEU A 9 CD2 -0.831 REMARK 500 1 LEU A 9 C LEU A 9 O -0.178 REMARK 500 1 LEU A 9 C PRO A 10 N -0.134 REMARK 500 1 PRO A 10 N PRO A 10 CA -0.106 REMARK 500 1 PRO A 10 CA PRO A 10 CB -0.193 REMARK 500 1 PRO A 10 CG PRO A 10 CD -0.249 REMARK 500 1 PRO A 10 CD PRO A 10 N -0.203 REMARK 500 1 PRO A 10 C ALA A 11 N -0.144 REMARK 500 1 ALA A 11 CA ALA A 11 CB -0.159 REMARK 500 1 ASP A 12 CG ASP A 12 OD1 -0.347 REMARK 500 1 ASP A 12 CG ASP A 12 OD2 -0.560 REMARK 500 1 SER A 13 CB SER A 13 OG -0.577 REMARK 500 1 SER A 15 CA SER A 15 CB -0.099 REMARK 500 1 SER A 15 CB SER A 15 OG -0.705 REMARK 500 1 THR A 17 CB THR A 17 OG1 -0.787 REMARK 500 1 THR A 17 CB THR A 17 CG2 -0.840 REMARK 500 1 LYS A 18 CG LYS A 18 CD -0.756 REMARK 500 1 LYS A 18 CD LYS A 18 CE -0.266 REMARK 500 REMARK 500 THIS ENTRY HAS 161 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 LYS A 1 N - CA - CB ANGL. DEV. = 25.8 DEGREES REMARK 500 1 LYS A 1 CA - CB - CG ANGL. DEV. = 47.0 DEGREES REMARK 500 1 LYS A 1 CB - CG - CD ANGL. DEV. = 40.9 DEGREES REMARK 500 1 LYS A 1 CD - CE - NZ ANGL. DEV. = 21.0 DEGREES REMARK 500 1 LYS A 1 N - CA - C ANGL. DEV. = -19.0 DEGREES REMARK 500 1 LYS A 1 CA - C - N ANGL. DEV. = 47.3 DEGREES REMARK 500 1 LYS A 1 O - C - N ANGL. DEV. = -58.3 DEGREES REMARK 500 1 ASP A 2 C - N - CA ANGL. DEV. = 51.0 DEGREES REMARK 500 1 ASP A 2 CB - CA - C ANGL. DEV. = 38.2 DEGREES REMARK 500 1 ASP A 2 N - CA - CB ANGL. DEV. = -43.3 DEGREES REMARK 500 1 ASP A 2 CA - CB - CG ANGL. DEV. = 35.2 DEGREES REMARK 500 1 ASP A 2 OD1 - CG - OD2 ANGL. DEV. = 31.9 DEGREES REMARK 500 1 ASP A 2 CB - CG - OD1 ANGL. DEV. = -73.1 DEGREES REMARK 500 1 ASP A 2 CB - CG - OD2 ANGL. DEV. = 41.2 DEGREES REMARK 500 1 ASP A 2 N - CA - C ANGL. DEV. = 23.8 DEGREES REMARK 500 1 ASP A 2 CA - C - O ANGL. DEV. = 33.0 DEGREES REMARK 500 1 ASP A 2 CA - C - N ANGL. DEV. = 39.2 DEGREES REMARK 500 1 ASP A 2 O - C - N ANGL. DEV. = -72.2 DEGREES REMARK 500 1 ARG A 3 C - N - CA ANGL. DEV. = 38.9 DEGREES REMARK 500 1 ARG A 3 CA - CB - CG ANGL. DEV. = 33.1 DEGREES REMARK 500 1 ARG A 3 CB - CG - CD ANGL. DEV. = 38.6 DEGREES REMARK 500 1 ARG A 3 CG - CD - NE ANGL. DEV. = 38.0 DEGREES REMARK 500 1 ARG A 3 CD - NE - CZ ANGL. DEV. = 28.7 DEGREES REMARK 500 1 ARG A 3 NH1 - CZ - NH2 ANGL. DEV. = -30.7 DEGREES REMARK 500 1 ARG A 3 NE - CZ - NH2 ANGL. DEV. = 32.0 DEGREES REMARK 500 1 LEU A 6 CA - CB - CG ANGL. DEV. = 21.7 DEGREES REMARK 500 1 CYS A 7 CA - CB - SG ANGL. DEV. = 11.3 DEGREES REMARK 500 1 ASP A 8 OD1 - CG - OD2 ANGL. DEV. = -91.7 DEGREES REMARK 500 1 ASP A 8 CB - CG - OD1 ANGL. DEV. = 42.3 DEGREES REMARK 500 1 ASP A 8 CB - CG - OD2 ANGL. DEV. = 49.2 DEGREES REMARK 500 1 LEU A 9 CA - CB - CG ANGL. DEV. = 28.4 DEGREES REMARK 500 1 LEU A 9 CD1 - CG - CD2 ANGL. DEV. = -20.5 DEGREES REMARK 500 1 LEU A 9 CB - CG - CD1 ANGL. DEV. = 10.5 DEGREES REMARK 500 1 LEU A 9 CB - CG - CD2 ANGL. DEV. = 14.6 DEGREES REMARK 500 1 ASP A 12 OD1 - CG - OD2 ANGL. DEV. = -39.7 DEGREES REMARK 500 1 ASP A 12 CB - CG - OD1 ANGL. DEV. = 26.1 DEGREES REMARK 500 1 ASP A 12 CB - CG - OD2 ANGL. DEV. = 13.7 DEGREES REMARK 500 1 THR A 17 OG1 - CB - CG2 ANGL. DEV. = -40.9 DEGREES REMARK 500 1 THR A 17 CA - CB - OG1 ANGL. DEV. = 27.7 DEGREES REMARK 500 1 THR A 17 CA - CB - CG2 ANGL. DEV. = 27.1 DEGREES REMARK 500 1 LYS A 18 CB - CG - CD ANGL. DEV. = 40.4 DEGREES REMARK 500 1 LYS A 18 CG - CD - CE ANGL. DEV. = 50.2 DEGREES REMARK 500 1 LYS A 18 CD - CE - NZ ANGL. DEV. = 18.6 DEGREES REMARK 500 1 GLU A 20 OE1 - CD - OE2 ANGL. DEV. = -85.0 DEGREES REMARK 500 1 GLU A 20 CG - CD - OE1 ANGL. DEV. = 44.1 DEGREES REMARK 500 1 GLU A 20 CG - CD - OE2 ANGL. DEV. = 40.9 DEGREES REMARK 500 1 LYS A 21 CB - CG - CD ANGL. DEV. = 21.8 DEGREES REMARK 500 1 LYS A 21 CG - CD - CE ANGL. DEV. = 30.2 DEGREES REMARK 500 1 LYS A 21 CD - CE - NZ ANGL. DEV. = 55.7 DEGREES REMARK 500 1 ARG A 22 CD - NE - CZ ANGL. DEV. = 19.6 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 187 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 3 133.69 -19.14 REMARK 500 2 ARG A 3 95.50 33.15 REMARK 500 2 THR A 38 32.37 -99.13 REMARK 500 3 ASP A 2 -86.24 -99.16 REMARK 500 4 ASP A 2 106.39 69.93 REMARK 500 4 SER A 5 3.73 -62.95 REMARK 500 4 ASN A 45 77.36 -66.82 REMARK 500 5 ASP A 2 70.63 -118.08 REMARK 500 5 SER A 5 4.77 -63.40 REMARK 500 5 CYS A 7 33.09 -84.60 REMARK 500 5 ASN A 45 79.97 -66.79 REMARK 500 6 ARG A 3 92.89 42.29 REMARK 500 6 CYS A 7 39.39 -86.22 REMARK 500 7 ASP A 2 84.69 -160.55 REMARK 500 7 ARG A 3 158.26 61.49 REMARK 500 7 LEU A 6 10.33 -48.70 REMARK 500 7 PRO A 10 171.57 -53.56 REMARK 500 8 ASP A 2 107.28 78.15 REMARK 500 8 ARG A 3 80.92 42.90 REMARK 500 8 TYR A 59 56.89 -91.33 REMARK 500 9 ASP A 2 -71.69 -114.61 REMARK 500 9 ARG A 3 140.81 52.39 REMARK 500 9 SER A 5 0.63 -59.28 REMARK 500 9 CYS A 7 33.28 -78.77 REMARK 500 10 ARG A 3 129.39 74.01 REMARK 500 11 ASP A 2 23.58 -156.30 REMARK 500 11 ASN A 45 82.06 -67.10 REMARK 500 12 SER A 5 -6.70 -59.74 REMARK 500 13 ASP A 2 -133.31 -114.60 REMARK 500 13 LEU A 6 -18.29 -47.10 REMARK 500 13 TYR A 59 81.53 -68.44 REMARK 500 14 ASP A 2 -61.78 72.31 REMARK 500 14 PRO A 10 102.45 -21.39 REMARK 500 14 ALA A 11 95.05 -59.20 REMARK 500 15 ARG A 3 152.22 55.61 REMARK 500 15 PRO A 10 94.02 -69.43 REMARK 500 15 ALA A 11 96.96 -58.56 REMARK 500 16 ASP A 2 -61.78 72.31 REMARK 500 16 PRO A 10 102.45 -21.39 REMARK 500 16 ALA A 11 95.05 -59.20 REMARK 500 17 ARG A 3 152.22 55.61 REMARK 500 17 PRO A 10 94.02 -69.43 REMARK 500 17 ALA A 11 96.96 -58.56 REMARK 500 18 ALA A 11 83.47 -63.88 REMARK 500 20 ARG A 3 149.48 175.24 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 LYS A 1 ASP A 2 1 147.77 REMARK 500 ASP A 2 ARG A 3 2 148.37 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 2 ARG A 48 0.10 SIDE CHAIN REMARK 500 5 ARG A 48 0.12 SIDE CHAIN REMARK 500 6 ARG A 48 0.09 SIDE CHAIN REMARK 500 18 ARG A 29 0.07 SIDE CHAIN REMARK 500 19 ARG A 49 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6506 RELATED DB: BMRB DBREF 2CA7 A 1 60 PDB 2CA7 2CA7 1 60 SEQRES 1 A 60 LYS ASP ARG PRO SER LEU CYS ASP LEU PRO ALA ASP SER SEQRES 2 A 60 GLY SER GLY THR LYS ALA GLU LYS ARG ILE TYR TYR ASN SEQRES 3 A 60 SER ALA ARG LYS GLN CYS LEU ARG PHE ASP TYR THR GLY SEQRES 4 A 60 GLN GLY GLY ASN GLU ASN ASN PHE ARG ARG THR TYR ASP SEQRES 5 A 60 CYS GLN ARG THR CYS LEU TYR THR HELIX 1 1 PRO A 4 ASP A 8 5 5 HELIX 2 2 ARG A 49 TYR A 59 1 11 SHEET 1 AA 2 GLU A 20 ASN A 26 0 SHEET 2 AA 2 GLN A 31 TYR A 37 -1 O GLN A 31 N ASN A 26 SSBOND 1 CYS A 7 CYS A 57 1555 1555 1.66 SSBOND 2 CYS A 32 CYS A 53 1555 1555 1.65 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 - n 15 2 Bytes