Header list of 1ctd.pdb file
Complete list - 16 20 Bytes
HEADER MUSCLE PROTEIN 12-NOV-92 1CTD TITLE DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC TWO-SITE TITLE 2 CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR SPECTROSCOPY COMPND MOL_ID: 1; COMPND 2 MOLECULE: TROPONIN C SITE III - SITE III HOMODIMER; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1 KEYWDS MUSCLE PROTEIN EXPDTA SOLUTION NMR NUMMDL 7 AUTHOR G.S.SHAW,B.D.SYKES REVDAT 3 16-FEB-22 1CTD 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1CTD 1 VERSN REVDAT 1 31-OCT-93 1CTD 0 JRNL AUTH G.S.SHAW,R.S.HODGES,B.D.SYKES JRNL TITL DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC JRNL TITL 2 TWO-SITE CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR JRNL TITL 3 SPECTROSCOPY. JRNL REF BIOCHEMISTRY V. 31 9572 1992 JRNL REFN ISSN 0006-2960 JRNL PMID 1390738 JRNL DOI 10.1021/BI00155A009 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NULL REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1CTD 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_1000172516. 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 : 7 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 C ACE B 0 H LYS B 1 0.60 REMARK 500 C ACE A 0 H LYS A 1 0.61 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 4 ASN A 16 CG ASN A 16 OD1 0.195 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 C - N - CA ANGL. DEV. = 18.2 DEGREES REMARK 500 1 ASP A 18 CA - C - N ANGL. DEV. = -21.4 DEGREES REMARK 500 2 PHE B 13 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES REMARK 500 2 TYR B 20 CB - CG - CD1 ANGL. DEV. = -4.1 DEGREES REMARK 500 3 LYS A 1 C - N - CA ANGL. DEV. = 18.0 DEGREES REMARK 500 3 LYS B 1 C - N - CA ANGL. DEV. = 21.3 DEGREES REMARK 500 4 LYS A 1 C - N - CA ANGL. DEV. = 17.3 DEGREES REMARK 500 4 LYS B 1 C - N - CA ANGL. DEV. = 15.3 DEGREES REMARK 500 4 ARG B 31 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 4 ARG B 31 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 5 LYS B 1 C - N - CA ANGL. DEV. = 17.5 DEGREES REMARK 500 6 LYS A 1 C - N - CA ANGL. DEV. = 20.5 DEGREES REMARK 500 6 ALA A 7 CB - CA - C ANGL. DEV. = 9.7 DEGREES REMARK 500 6 PHE A 13 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES REMARK 500 6 LYS B 1 C - N - CA ANGL. DEV. = 17.2 DEGREES REMARK 500 6 ARG B 11 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 7 LYS B 1 C - N - CA ANGL. DEV. = 21.8 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 LYS A 15 -71.67 -62.89 REMARK 500 2 GLU A 3 -41.72 75.44 REMARK 500 2 ASP A 14 62.64 -67.07 REMARK 500 2 ALA A 32 83.38 -59.74 REMARK 500 2 ASP B 14 65.60 -69.85 REMARK 500 2 THR B 33 28.75 -78.39 REMARK 500 3 SER A 2 -149.60 57.35 REMARK 500 4 GLU A 3 -60.43 60.89 REMARK 500 4 ILE A 29 -71.48 -62.67 REMARK 500 4 ASP B 14 46.21 -65.85 REMARK 500 5 GLU A 3 -47.58 75.77 REMARK 500 5 ILE A 29 -75.59 -72.55 REMARK 500 5 THR A 33 95.58 -55.95 REMARK 500 5 GLU B 3 56.28 -106.27 REMARK 500 5 ILE B 29 -72.36 -66.23 REMARK 500 5 THR B 33 58.83 -107.77 REMARK 500 6 GLU A 3 -98.37 42.94 REMARK 500 6 ALA A 7 99.97 -40.28 REMARK 500 6 ASP A 14 52.27 -69.45 REMARK 500 6 ILE B 29 -76.09 -58.86 REMARK 500 7 SER A 2 -136.38 -126.94 REMARK 500 7 ASP A 14 51.72 -69.20 REMARK 500 7 ASP B 14 47.91 -70.13 REMARK 500 7 THR B 33 89.88 -65.00 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 ASP A 18 GLY A 19 1 112.55 REMARK 500 ALA B 7 ASN B 8 7 147.80 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 TYR B 20 0.11 SIDE CHAIN REMARK 500 3 PHE A 13 0.10 SIDE CHAIN REMARK 500 3 TYR A 20 0.12 SIDE CHAIN REMARK 500 4 PHE A 13 0.09 SIDE CHAIN REMARK 500 4 ARG B 31 0.14 SIDE CHAIN REMARK 500 5 ARG A 11 0.14 SIDE CHAIN REMARK 500 5 TYR A 20 0.07 SIDE CHAIN REMARK 500 5 TYR B 20 0.12 SIDE CHAIN REMARK 500 6 PHE A 13 0.09 SIDE CHAIN REMARK 500 6 TYR A 20 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 1 PHE A 10 -14.51 REMARK 500 1 ASP A 18 17.27 REMARK 500 1 ALA B 17 -10.65 REMARK 500 3 ALA A 9 -10.71 REMARK 500 3 PHE A 10 -14.18 REMARK 500 4 ALA A 9 -10.68 REMARK 500 4 ALA A 17 -11.89 REMARK 500 4 ALA B 17 -10.63 REMARK 500 5 PHE A 10 -11.03 REMARK 500 6 ALA A 7 12.32 REMARK 500 6 ALA A 9 -10.61 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 69 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 14 OD1 REMARK 620 2 ASN A 16 OD1 142.5 REMARK 620 3 ASN A 16 ND2 139.9 43.0 REMARK 620 4 ASN A 16 N 142.3 59.8 77.8 REMARK 620 5 ASN A 16 O 125.0 89.8 60.0 66.1 REMARK 620 6 ASP A 18 OD2 91.6 120.1 117.7 60.6 61.5 REMARK 620 7 TYR A 20 O 58.3 132.4 92.1 139.1 74.4 91.6 REMARK 620 8 GLU A 25 OE1 65.2 78.4 89.8 130.4 143.9 152.4 88.5 REMARK 620 9 GLU A 25 OE2 79.7 68.6 106.7 90.5 154.4 117.0 130.2 47.2 REMARK 620 N 1 2 3 4 5 6 7 8 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 70 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 14 OD1 REMARK 620 2 ASN B 16 OD1 114.8 REMARK 620 3 ASP B 18 OD1 59.9 111.6 REMARK 620 4 TYR B 20 O 66.2 173.8 63.2 REMARK 620 5 GLU B 25 OE2 113.7 62.2 169.4 123.5 REMARK 620 6 GLU B 25 OE1 152.5 77.5 141.3 104.5 48.1 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 69 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 70 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1CTA RELATED DB: PDB DBREF 1CTD A 1 34 UNP P02588 TPCS_CHICK 93 126 DBREF 1CTD B 1 34 UNP P02588 TPCS_CHICK 93 126 SEQADV 1CTD ALA A 9 UNP P02588 CYS 101 CONFLICT SEQADV 1CTD TYR A 20 UNP P02588 PHE 112 CONFLICT SEQADV 1CTD ALA B 9 UNP P02588 CYS 101 CONFLICT SEQADV 1CTD TYR B 20 UNP P02588 PHE 112 CONFLICT SEQRES 1 A 36 ACE LYS SER GLU GLU GLU LEU ALA ASN ALA PHE ARG ILE SEQRES 2 A 36 PHE ASP LYS ASN ALA ASP GLY TYR ILE ASP ILE GLU GLU SEQRES 3 A 36 LEU GLY GLU ILE LEU ARG ALA THR GLY NH2 SEQRES 1 B 36 ACE LYS SER GLU GLU GLU LEU ALA ASN ALA PHE ARG ILE SEQRES 2 B 36 PHE ASP LYS ASN ALA ASP GLY TYR ILE ASP ILE GLU GLU SEQRES 3 B 36 LEU GLY GLU ILE LEU ARG ALA THR GLY NH2 HET ACE A 0 3 HET NH2 A 35 3 HET ACE B 0 3 HET NH2 B 35 3 HET CA A 69 1 HET CA B 70 1 HETNAM ACE ACETYL GROUP HETNAM NH2 AMINO GROUP HETNAM CA CALCIUM ION FORMUL 1 ACE 2(C2 H4 O) FORMUL 1 NH2 2(H2 N) FORMUL 3 CA 2(CA 2+) HELIX 1 1 LYS A 1 ILE A 12 1 12 HELIX 2 2 ASP A 22 GLY A 34 1 13 HELIX 3 3 SER B 2 ASP B 14 1 13 HELIX 4 4 ASP B 22 ALA B 32 1 11 LINK O ACE A 0 H LYS A 1 1555 1555 1.15 LINK C ACE A 0 N LYS A 1 1555 1555 1.31 LINK C GLY A 34 N NH2 A 35 1555 1555 1.31 LINK O ACE B 0 H LYS B 1 1555 1555 1.14 LINK C ACE B 0 N LYS B 1 1555 1555 1.31 LINK C GLY B 34 N NH2 B 35 1555 1555 1.31 LINK OD1 ASP A 14 CA CA A 69 1555 1555 2.58 LINK OD1 ASN A 16 CA CA A 69 1555 1555 2.79 LINK ND2 ASN A 16 CA CA A 69 1555 1555 3.11 LINK N ASN A 16 CA CA A 69 1555 1555 2.95 LINK O ASN A 16 CA CA A 69 1555 1555 2.62 LINK OD2 ASP A 18 CA CA A 69 1555 1555 2.87 LINK O TYR A 20 CA CA A 69 1555 1555 2.85 LINK OE1 GLU A 25 CA CA A 69 1555 1555 2.80 LINK OE2 GLU A 25 CA CA A 69 1555 1555 2.75 LINK OD1 ASP B 14 CA CA B 70 1555 1555 2.72 LINK OD1 ASN B 16 CA CA B 70 1555 1555 2.73 LINK OD1 ASP B 18 CA CA B 70 1555 1555 2.72 LINK O TYR B 20 CA CA B 70 1555 1555 2.74 LINK OE2 GLU B 25 CA CA B 70 1555 1555 2.77 LINK OE1 GLU B 25 CA CA B 70 1555 1555 2.71 CISPEP 1 ALA B 32 THR B 33 1 -10.10 CISPEP 2 GLU A 5 LEU A 6 2 6.79 CISPEP 3 GLU A 5 LEU A 6 6 -20.16 CISPEP 4 GLU A 5 LEU A 6 7 -14.00 CISPEP 5 GLU B 5 LEU B 6 7 -7.95 CISPEP 6 ASN B 8 ALA B 9 7 -13.54 SITE 1 AC1 6 ASP A 14 LYS A 15 ASN A 16 ASP A 18 SITE 2 AC1 6 TYR A 20 GLU A 25 SITE 1 AC2 5 ASP B 14 ASN B 16 ASP B 18 TYR B 20 SITE 2 AC2 5 GLU B 25 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 - 16 20 Bytes