Header list of 1pon.pdb file
Complete list - v 3 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 02-APR-96 1PON
TITLE SITE III-SITE IV TROPONIN C HETERODIMER, NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TROPONIN C;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SITE III AND IV;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TROPONIN C;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: SITE III AND IV;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 7 ORGANISM_COMMON: CHICKEN;
SOURCE 8 ORGANISM_TAXID: 9031
KEYWDS EF-HAND, MUSCLE PROTEIN, CALCIUM-BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 42
AUTHOR G.S.SHAW,B.D.SYKES
REVDAT 4 03-NOV-21 1PON 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1PON 1 VERSN
REVDAT 2 01-APR-03 1PON 1 JRNL
REVDAT 1 08-NOV-96 1PON 0
JRNL AUTH G.S.SHAW,B.D.SYKES
JRNL TITL NMR SOLUTION STRUCTURE OF A SYNTHETIC TROPONIN C
JRNL TITL 2 HETERODIMERIC DOMAIN.
JRNL REF BIOCHEMISTRY V. 35 7429 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8652520
JRNL DOI 10.1021/BI9528006
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.S.SHAW,R.S.HODGES,C.M.KAY,B.D.SYKES
REMARK 1 TITL RELATIVE STABILITIES OF SYNTHETIC PEPTIDE HOMO-AND
REMARK 1 TITL 2 HETERODIMERIC TROPONIN-C DOMAINS JOURNAL TITLE: PROTEIN
REMARK 1 TITL 3 SCIENCE
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII
REMARK 3 AUTHORS : HAVEL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PON 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_1000175770.
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 : 42
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 HG22 ILE B 58 HB2 GLU B 62 1.35
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 12 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 2 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 2 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 3 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 3 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 4 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 4 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 4 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 5 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 5 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 5 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 6 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 6 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 6 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 7 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 7 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 7 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 8 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 8 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 8 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 9 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 9 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 9 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 10 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 10 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 10 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 11 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 11 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 11 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 12 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 12 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 12 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 13 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 13 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 13 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 14 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 14 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 14 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 15 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 15 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 15 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 16 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 16 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 16 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 17 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 17 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 126 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 SER A 3 -108.68 -103.62
REMARK 500 1 ALA A 8 -71.36 -64.19
REMARK 500 1 LYS A 16 -76.47 -68.96
REMARK 500 1 ALA A 18 54.26 81.59
REMARK 500 1 ARG A 32 -71.81 -135.63
REMARK 500 1 LYS B 52 -60.50 -140.17
REMARK 500 1 ASP B 61 -83.13 -47.16
REMARK 500 1 GLU B 62 -39.80 -25.23
REMARK 500 1 MET B 67 -70.33 -75.93
REMARK 500 2 ASP A 15 90.23 -66.37
REMARK 500 2 ALA A 18 67.05 79.04
REMARK 500 2 THR A 34 -56.26 -142.51
REMARK 500 2 LYS B 52 -141.77 -59.83
REMARK 500 2 ASN B 54 122.38 68.31
REMARK 500 2 ASP B 55 43.82 -85.58
REMARK 500 2 ASP B 61 -84.31 -48.78
REMARK 500 2 GLU B 62 -36.17 -25.03
REMARK 500 2 MET B 67 -98.39 -75.49
REMARK 500 3 SER A 3 -148.98 -164.65
REMARK 500 3 PHE A 14 -78.27 -60.67
REMARK 500 3 ALA A 18 45.51 80.61
REMARK 500 3 THR A 34 -63.18 -135.02
REMARK 500 3 ASP B 49 -71.15 -67.50
REMARK 500 3 LYS B 52 -128.78 -67.99
REMARK 500 3 ASN B 54 95.20 46.12
REMARK 500 3 ASP B 59 -168.88 -117.07
REMARK 500 3 ASP B 61 -83.35 -48.45
REMARK 500 3 GLU B 62 -39.76 -24.62
REMARK 500 4 ASN A 17 83.98 179.81
REMARK 500 4 ALA A 18 76.19 67.08
REMARK 500 4 LEU A 27 -75.47 -46.50
REMARK 500 4 LYS B 52 -166.71 -58.22
REMARK 500 4 ASN B 54 127.50 71.88
REMARK 500 4 ASP B 61 -83.97 -49.89
REMARK 500 4 GLU B 62 -33.17 -28.57
REMARK 500 5 SER A 3 58.86 -99.14
REMARK 500 5 LYS A 16 -53.76 -134.18
REMARK 500 5 ALA A 18 54.88 77.00
REMARK 500 5 ILE A 30 -70.58 -48.46
REMARK 500 5 ALA A 33 -175.54 -68.92
REMARK 500 5 THR A 34 -83.06 -40.90
REMARK 500 5 LYS B 52 -112.39 -92.79
REMARK 500 5 ASN B 54 76.22 70.62
REMARK 500 5 ASP B 59 -168.01 -107.14
REMARK 500 5 ASP B 61 -83.18 -50.83
REMARK 500 5 GLU B 62 -42.35 -24.23
REMARK 500 5 GLU B 68 -73.15 -74.49
REMARK 500 6 SER A 3 32.46 -146.21
REMARK 500 6 ALA A 18 63.45 74.66
REMARK 500 6 ILE A 30 -72.84 -58.60
REMARK 500
REMARK 500 THIS ENTRY HAS 359 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE B 37
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 36
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 B 72
DBREF 1PON A 2 35 UNP P02588 TPCS_CHICK 93 126
DBREF 1PON B 38 71 UNP P02588 TPCS_CHICK 129 162
SEQADV 1PON ALA A 10 UNP P02588 CYS 101 ENGINEERED MUTATION
SEQADV 1PON TYR A 21 UNP P02588 PHE 112 ENGINEERED MUTATION
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 VAL THR GLU GLU ASP ILE GLU ASP LEU MET LYS ASP
SEQRES 2 B 36 SER ASP LYS ASN ASN ASP GLY ARG ILE ASP PHE ASP GLU
SEQRES 3 B 36 PHE LEU LYS MET MET GLU GLY VAL GLN NH2
HET ACE A 1 6
HET NH2 A 36 3
HET ACE B 37 6
HET NH2 B 72 3
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
FORMUL 1 ACE 2(C2 H4 O)
FORMUL 1 NH2 2(H2 N)
HELIX 1 1 GLU A 5 PHE A 14 1 10
HELIX 2 2 ILE A 24 ARG A 32 1 9
HELIX 3 3 GLU B 40 SER B 50 1 11
HELIX 4 4 PHE B 60 GLU B 68 1 9
SHEET 1 A 2 ILE A 22 ASP A 23 0
SHEET 2 A 2 ARG B 57 ILE B 58 -1 N ILE B 58 O ILE A 22
LINK C ACE A 1 N LYS A 2 1555 1555 1.35
LINK C GLY A 35 N NH2 A 36 1555 1555 1.35
LINK C ACE B 37 N VAL B 38 1555 1555 1.35
LINK C GLN B 71 N NH2 B 72 1555 1555 1.35
SITE 1 AC1 1 SER A 3
SITE 1 AC2 1 THR B 39
SITE 1 AC3 1 GLY A 35
SITE 1 AC4 2 VAL B 70 GLN B 71
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 - v 3 2 Bytes