Header list of 1cta.pdb file
Complete list - 16 202 Bytes
HEADER MUSCLE PROTEIN 12-NOV-92 1CTA
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
AUTHOR G.S.SHAW,B.D.SYKES
REVDAT 3 16-FEB-22 1CTA 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1CTA 1 VERSN
REVDAT 1 31-OCT-93 1CTA 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 1CTA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172515.
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 : 1
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 0.56
REMARK 500 O ACE A 0 H LYS A 1 1.18
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 LYS A 1 C - N - CA ANGL. DEV. = 31.9 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 SER A 2 148.55 -15.92
REMARK 500 GLU A 3 -62.21 67.66
REMARK 500 ARG A 31 92.63 -55.72
REMARK 500 ALA A 32 47.29 -82.33
REMARK 500 THR A 33 101.34 -18.70
REMARK 500 SER B 2 67.03 69.72
REMARK 500 GLU B 3 -24.96 54.41
REMARK 500 THR B 33 47.74 -89.95
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 ALA A 32 THR A 33 -105.60
REMARK 500 LYS B 1 SER B 2 -127.39
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 ARG B 31 0.14 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 ALA A 9 -11.67
REMARK 500 PHE A 10 -10.31
REMARK 500 PHE B 10 -10.65
REMARK 500 ALA B 17 -10.66
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 ND2 85.2
REMARK 620 3 ASN A 16 OD1 122.6 47.2
REMARK 620 4 ASP A 18 OD1 60.1 64.8 108.6
REMARK 620 5 TYR A 20 O 68.8 131.5 164.6 66.7
REMARK 620 6 GLU A 25 OE2 116.3 97.0 56.2 161.3 131.0
REMARK 620 7 GLU A 25 OE1 156.9 112.4 67.8 140.2 105.9 49.1
REMARK 620 N 1 2 3 4 5 6
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 125.1
REMARK 620 3 ASP B 18 OD1 61.7 116.2
REMARK 620 4 TYR B 20 O 67.2 167.6 65.9
REMARK 620 5 GLU B 25 OE2 116.3 58.8 173.1 120.0
REMARK 620 6 GLU B 25 OE1 149.7 73.5 136.6 96.5 48.5
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: 1CTD RELATED DB: PDB
DBREF 1CTA A 1 34 UNP P02588 TPCS_CHICK 93 126
DBREF 1CTA B 1 34 UNP P02588 TPCS_CHICK 93 126
SEQADV 1CTA ALA A 9 UNP P02588 CYS 101 CONFLICT
SEQADV 1CTA TYR A 20 UNP P02588 PHE 112 CONFLICT
SEQADV 1CTA ALA B 9 UNP P02588 CYS 101 CONFLICT
SEQADV 1CTA 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 GLU A 3 ASP A 14 1 12
HELIX 2 2 ASP A 22 ARG A 31 1 10
HELIX 3 3 GLU B 3 ASP B 14 1 12
HELIX 4 4 ASP B 22 ARG B 31 1 10
LINK C ACE A 0 H LYS A 1 1555 1555 0.90
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 1.15
LINK C ACE B 0 N LYS B 1 1555 1555 1.31
LINK C GLY B 34 N NH2 B 35 1555 1555 1.32
LINK OD1 ASP A 14 CA CA A 69 1555 1555 2.72
LINK ND2 ASN A 16 CA CA A 69 1555 1555 2.61
LINK OD1 ASN A 16 CA CA A 69 1555 1555 2.83
LINK OD1 ASP A 18 CA CA A 69 1555 1555 2.76
LINK O TYR A 20 CA CA A 69 1555 1555 2.71
LINK OE2 GLU A 25 CA CA A 69 1555 1555 2.79
LINK OE1 GLU A 25 CA CA A 69 1555 1555 2.58
LINK OD1 ASP B 14 CA CA B 70 1555 1555 2.72
LINK OD1 ASN B 16 CA CA B 70 1555 1555 2.72
LINK OD1 ASP B 18 CA CA B 70 1555 1555 2.70
LINK O TYR B 20 CA CA B 70 1555 1555 2.75
LINK OE2 GLU B 25 CA CA B 70 1555 1555 2.76
LINK OE1 GLU B 25 CA CA B 70 1555 1555 2.67
SITE 1 AC1 6 ASP A 14 ASN A 16 ASP A 18 TYR A 20
SITE 2 AC1 6 ASP A 22 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
Complete list - 16 202 Bytes