Header list of 1dmf.pdb file
Complete list - 16 20 Bytes
HEADER METALLOTHIONEIN 22-NOV-94 1DMF
TITLE THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF CALLINECTES SAPIDUS
TITLE 2 METALLOTHIONEIN-I DETERMINED BY HOMONUCLEAR AND HETERONUCLEAR
TITLE 3 MAGNETIC RESONANCE SPECTOSCOPY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CD6 METALLOTHIONEIN-1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CALLINECTES SAPIDUS;
SOURCE 3 ORGANISM_COMMON: BLUE CRAB;
SOURCE 4 ORGANISM_TAXID: 6763
KEYWDS METALLOTHIONEIN
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR S.S.NARULA,M.BROUWER,Y.HUA,I.M.ARMITAGE
REVDAT 3 16-FEB-22 1DMF 1 REMARK LINK
REVDAT 2 24-FEB-09 1DMF 1 VERSN
REVDAT 1 07-FEB-95 1DMF 0
JRNL AUTH S.S.NARULA,M.BROUWER,Y.HUA,I.M.ARMITAGE
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF CALLINECTES SAPIDUS
JRNL TITL 2 METALLOTHIONEIN-1 DETERMINED BY HOMONUCLEAR AND
JRNL TITL 3 HETERONUCLEAR MAGNETIC RESONANCE SPECTROSCOPY.
JRNL REF BIOCHEMISTRY V. 34 620 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7819257
JRNL DOI 10.1021/BI00002A029
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.S.NARULA,M.BROUWER,I.M.ARMITAGE
REMARK 1 TITL ESTABLISHMENT OF TWO DISTINCT PROTEIN DOMAINS IN BLUE CRAB
REMARK 1 TITL 2 CALLINECTES SAPIDUS METALLOTHIONEIN-I THROUGH HETERONUCLEAR
REMARK 1 TITL 3 (1H-113CD) AND HOMONUCLEAR (1H-1H) CORRELATION NMR
REMARK 1 TITL 4 EXPERIMENT
REMARK 1 REF MAGN.RESON.CHEM. V. 31 96 1993
REMARK 1 REFN ISSN 0749-1581
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.A.MESSERLE,A.SCHAEFFER,M.VASAK,J.H.R.KAEGI,K.WUTHRICH
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF HUMAN [113CD-7]
REMARK 1 TITL 2 METALLOTHIONEIN-2 IN SOLUTION DETERMINED BY NUCLEAR MAGNETIC
REMARK 1 TITL 3 RESONANCE SPECTROSCOPY
REMARK 1 REF J.MOL.BIOL. V. 214 765 1990
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DMF 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_1000172842.
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: 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 PRO A 3 -160.44 -79.47
REMARK 500 1 ASP A 7 24.75 -160.53
REMARK 500 1 GLU A 13 -99.52 -127.43
REMARK 500 1 CYS A 16 -169.34 -55.42
REMARK 500 1 ALA A 18 44.14 -84.33
REMARK 500 1 CYS A 22 166.35 -49.56
REMARK 500 1 SER A 24 21.18 -149.49
REMARK 500 1 CYS A 27 -72.55 -53.60
REMARK 500 2 PRO A 3 -156.07 -76.69
REMARK 500 2 ASP A 7 24.69 -160.27
REMARK 500 2 GLU A 13 -100.58 -124.72
REMARK 500 2 CYS A 16 -168.52 -56.14
REMARK 500 2 ALA A 18 36.44 -90.00
REMARK 500 2 CYS A 22 151.55 -49.57
REMARK 500 2 SER A 24 31.51 -144.13
REMARK 500 2 CYS A 27 -69.62 -102.10
REMARK 500 3 PRO A 3 -158.87 -78.05
REMARK 500 3 CYS A 4 -69.60 -127.74
REMARK 500 3 CYS A 5 43.90 -80.92
REMARK 500 3 ASP A 7 15.60 -153.67
REMARK 500 3 LYS A 8 113.49 -160.83
REMARK 500 3 GLU A 13 -102.44 -119.47
REMARK 500 3 CYS A 16 -168.11 -56.58
REMARK 500 3 ALA A 18 38.24 -88.49
REMARK 500 3 THR A 23 55.55 -142.16
REMARK 500 3 CYS A 25 -159.48 -106.36
REMARK 500 3 CYS A 27 -71.98 -117.45
REMARK 500 4 PRO A 3 -161.36 -77.42
REMARK 500 4 ASP A 7 24.35 -160.49
REMARK 500 4 LYS A 8 87.88 -158.17
REMARK 500 4 CYS A 9 101.52 -59.40
REMARK 500 4 GLU A 13 -100.49 -123.82
REMARK 500 4 CYS A 16 -169.41 -55.94
REMARK 500 4 ALA A 18 37.30 -86.56
REMARK 500 4 CYS A 25 -158.71 -109.03
REMARK 500 4 CYS A 27 -72.43 -119.58
REMARK 500 5 PRO A 3 -162.43 -77.91
REMARK 500 5 CYS A 4 -65.85 -123.58
REMARK 500 5 CYS A 5 47.32 -82.86
REMARK 500 5 ASP A 7 19.20 -158.22
REMARK 500 5 LYS A 8 104.55 -160.70
REMARK 500 5 GLU A 13 -100.61 -122.42
REMARK 500 5 CYS A 16 -170.76 -54.63
REMARK 500 5 ALA A 18 37.84 -89.18
REMARK 500 5 CYS A 25 -159.24 -113.09
REMARK 500 5 CYS A 27 -70.94 -128.40
REMARK 500 6 PRO A 3 -163.08 -77.47
REMARK 500 6 ASP A 7 26.64 -160.20
REMARK 500 6 GLU A 13 -101.00 -122.61
REMARK 500 6 CYS A 16 -168.91 -55.99
REMARK 500
REMARK 500 THIS ENTRY HAS 163 RAMACHANDRAN 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 ARG A 26 0.30 SIDE CHAIN
REMARK 500 2 ARG A 26 0.24 SIDE CHAIN
REMARK 500 3 ARG A 26 0.25 SIDE CHAIN
REMARK 500 4 ARG A 26 0.32 SIDE CHAIN
REMARK 500 5 ARG A 26 0.17 SIDE CHAIN
REMARK 500 6 ARG A 26 0.31 SIDE CHAIN
REMARK 500 7 ARG A 26 0.23 SIDE CHAIN
REMARK 500 8 ARG A 26 0.31 SIDE CHAIN
REMARK 500 9 ARG A 26 0.30 SIDE CHAIN
REMARK 500 10 ARG A 26 0.19 SIDE CHAIN
REMARK 500 11 ARG A 26 0.32 SIDE CHAIN
REMARK 500 12 ARG A 26 0.13 SIDE CHAIN
REMARK 500 13 ARG A 26 0.08 SIDE CHAIN
REMARK 500 14 ARG A 26 0.32 SIDE CHAIN
REMARK 500 15 ARG A 26 0.16 SIDE CHAIN
REMARK 500 16 ARG A 26 0.31 SIDE CHAIN
REMARK 500 17 ARG A 26 0.10 SIDE CHAIN
REMARK 500 18 ARG A 26 0.19 SIDE CHAIN
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 CD A 103 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 4 SG
REMARK 620 2 CYS A 5 SG 116.9
REMARK 620 3 CYS A 16 SG 111.8 98.0
REMARK 620 4 CYS A 20 SG 109.2 110.3 110.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 104 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 5 SG
REMARK 620 2 CYS A 9 SG 113.0
REMARK 620 3 CYS A 22 SG 103.0 106.8
REMARK 620 4 CYS A 25 SG 115.9 107.9 109.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 105 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 11 SG
REMARK 620 2 CYS A 16 SG 110.6
REMARK 620 3 CYS A 25 SG 96.9 110.0
REMARK 620 4 CYS A 27 SG 110.8 109.1 118.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 105
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DME RELATED DB: PDB
DBREF 1DMF A 1 28 UNP P55949 MT1_CALSI 2 29
SEQRES 1 A 28 PRO GLY PRO CYS CYS ASN ASP LYS CYS VAL CYS GLN GLU
SEQRES 2 A 28 GLY GLY CYS LYS ALA GLY CYS GLN CYS THR SER CYS ARG
SEQRES 3 A 28 CYS SER
HET CD A 103 1
HET CD A 104 1
HET CD A 105 1
HETNAM CD CADMIUM ION
FORMUL 2 CD 3(CD 2+)
LINK SG CYS A 4 CD CD A 103 1555 1555 2.51
LINK SG CYS A 5 CD CD A 103 1555 1555 2.48
LINK SG CYS A 5 CD CD A 104 1555 1555 2.54
LINK SG CYS A 9 CD CD A 104 1555 1555 2.54
LINK SG CYS A 11 CD CD A 105 1555 1555 2.49
LINK SG CYS A 16 CD CD A 103 1555 1555 2.47
LINK SG CYS A 16 CD CD A 105 1555 1555 2.52
LINK SG CYS A 20 CD CD A 103 1555 1555 2.52
LINK SG CYS A 22 CD CD A 104 1555 1555 2.51
LINK SG CYS A 25 CD CD A 104 1555 1555 2.57
LINK SG CYS A 25 CD CD A 105 1555 1555 2.59
LINK SG CYS A 27 CD CD A 105 1555 1555 2.54
SITE 1 AC1 5 CYS A 4 CYS A 5 CYS A 16 CYS A 20
SITE 2 AC1 5 CD A 105
SITE 1 AC2 4 CYS A 5 CYS A 9 CYS A 22 CYS A 25
SITE 1 AC3 6 CYS A 11 CYS A 16 CYS A 20 CYS A 25
SITE 2 AC3 6 CYS A 27 CD A 103
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