Header list of 1j5m.pdb file
Complete list - 9 202 Bytes
HEADER METAL BINDING PROTEIN 16-MAY-02 1J5M
TITLE SOLUTION STRUCTURE OF THE SYNTHETIC 113CD_3 BETA_N DOMAIN OF LOBSTER
TITLE 2 METALLOTHIONEIN-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METALLOTHIONEIN-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BETA_N DOMAIN (RESIDUES 1-28);
COMPND 5 SYNONYM: CUMT-1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THE PEPTIDE IS NATURALLY FOUND IN HOMARUS AMERICANUS (AMERICAN
SOURCE 5 LOBSTER).
KEYWDS METALLOTHIONEIN, BETA-DOMAIN, METAL-SULFUR-CLUSTER, 2D-NMR, 113CD-
KEYWDS 2 NMR, CONFORMATIONAL CHANGES, HN-S-HYDROGEN BONDS, METAL BINDING
KEYWDS 3 PROTEIN
EXPDTA SOLUTION NMR
AUTHOR A.MUNOZ,F.H.FORSTERLING,C.F.SHAW III,D.H.PETERING
REVDAT 6 14-JUN-23 1J5M 1 REMARK LINK
REVDAT 5 05-FEB-20 1J5M 1 REMARK ATOM
REVDAT 4 24-FEB-09 1J5M 1 VERSN
REVDAT 3 01-APR-03 1J5M 1 JRNL
REVDAT 2 23-DEC-02 1J5M 1 EXPDTA JRNL REMARK
REVDAT 1 22-MAY-02 1J5M 0
SPRSDE 22-MAY-02 1J5M 1HZR
JRNL AUTH A.MUNOZ,F.H.FORSTERLING,C.F.SHAW III,D.H.PETERING
JRNL TITL STRUCTURE OF THE (113)CD(3)BETA DOMAINS FROM HOMARUS
JRNL TITL 2 AMERICANUS METALLOTHIONEIN-1: HYDROGEN BONDING AND SOLVENT
JRNL TITL 3 ACCESSIBILITY OF SULFUR ATOMS
JRNL REF J.BIOL.INORG.CHEM. V. 7 713 2002
JRNL REFN ISSN 0949-8257
JRNL PMID 12203008
JRNL DOI 10.1007/S00775-002-0345-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER (XWINNMR), AXEL BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURE IS BASED ON 276 DISTANCE RESTRAINTS, 240 DERIVED
REMARK 3 FROM NOE, 33 METAL CLUSTER
REMARK 3 RESTRAINTS FROM 113CD HSQC TOCSY AND 6 RESTRAINTS FROM HN-S
REMARK 3 HYDROGEN BONDS. A TOTAL OF 27
REMARK 3 DIHEDRAL ANGLE RESTRAINTS WAS APPLIED, 13 PHI, 10 CHI1 AND 4 CYS-
REMARK 3 CD CHI2 ANGLES. METHYLENE
REMARK 3 PROTONS FOR WHICH NO STEREOSPECIFIC ASSIGNMENT COULD BE OBTAINED
REMARK 3 WERE TREATED WITH THE
REMARK 3 FLOATING CHIRALITY PROCEDURE IN XPLOR.
REMARK 4
REMARK 4 1J5M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-02.
REMARK 100 THE DEPOSITION ID IS D_1000001641.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278; 298
REMARK 210 PH : 7.4; 7.4
REMARK 210 IONIC STRENGTH : 5MM TRIS-HCL; 5MM TRIS-HCL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 5MM (113CD)3-BETA_N, 5MM D-TRIS
REMARK 210 -HCL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-TOCSY; 2D-NOESY; DQF-COSY; PE
REMARK 210 -COSY; 2D-113CD-HSQC-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 300 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DPX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.5, FELIX 2000, X-PLOR
REMARK 210 3.851, MOLMOL 2K.1
REMARK 210 METHOD USED : AB INITIO SIMULATED ANNEALING
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: HN-S HYDROGEN BONDS WERE DETERMINED USING A 2D LONG RANGE
REMARK 210 1H{113CD} HMQC EXPERIMENT
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 CYS A 4 -171.75 -174.43
REMARK 500 CYS A 5 29.10 40.27
REMARK 500 ASP A 7 -35.18 -133.08
REMARK 500 LYS A 8 -103.78 -135.78
REMARK 500 CYS A 9 149.20 175.33
REMARK 500 GLU A 10 -77.84 -137.61
REMARK 500 CYS A 11 19.05 50.37
REMARK 500 GLU A 13 31.78 -97.41
REMARK 500 LYS A 17 -62.48 -128.26
REMARK 500 THR A 18 -75.33 -163.23
REMARK 500 CYS A 20 113.13 -29.69
REMARK 500 THR A 23 38.44 -87.46
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 A 26 0.32 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 30 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 4 SG
REMARK 620 2 CYS A 5 SG 117.1
REMARK 620 3 CYS A 16 SG 110.3 100.1
REMARK 620 4 CYS A 20 SG 109.4 111.2 108.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 29 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 5 SG
REMARK 620 2 CYS A 9 SG 108.3
REMARK 620 3 CYS A 22 SG 106.7 111.4
REMARK 620 4 CYS A 25 SG 116.0 107.8 106.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 31 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 11 SG
REMARK 620 2 CYS A 16 SG 107.0
REMARK 620 3 CYS A 25 SG 107.1 111.8
REMARK 620 4 CYS A 27 SG 110.7 109.5 110.6
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 29
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 30
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 31
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4725 RELATED DB: BMRB
REMARK 900 CONTAINS 1H, 13C CHEMICAL SHIFTS AND 3JHNHA AND 3JHAHB COUPLING
REMARK 900 CONSTANTS
REMARK 900 RELATED ID: 1J5L RELATED DB: PDB
REMARK 900 CONTAINS THE MINIMIZED AVERAGE STRUCTURE OF THE BETA_C DOMAIN OF
REMARK 900 THIS PROTEIN
DBREF 1J5M A 1 28 UNP P29499 MT1_HOMAM 1 28
SEQRES 1 A 28 PRO GLY PRO CYS CYS LYS ASP LYS CYS GLU CYS ALA GLU
SEQRES 2 A 28 GLY GLY CYS LYS THR GLY CYS LYS CYS THR SER CYS ARG
SEQRES 3 A 28 CYS ALA
HET CD A 29 1
HET CD A 30 1
HET CD A 31 1
HETNAM CD CADMIUM ION
FORMUL 2 CD 3(CD 2+)
LINK SG CYS A 4 CD CD A 30 1555 1555 2.57
LINK SG CYS A 5 CD CD A 29 1555 1555 2.56
LINK SG CYS A 5 CD CD A 30 1555 1555 2.54
LINK SG CYS A 9 CD CD A 29 1555 1555 2.56
LINK SG CYS A 11 CD CD A 31 1555 1555 2.54
LINK SG CYS A 16 CD CD A 30 1555 1555 2.53
LINK SG CYS A 16 CD CD A 31 1555 1555 2.53
LINK SG CYS A 20 CD CD A 30 1555 1555 2.55
LINK SG CYS A 22 CD CD A 29 1555 1555 2.56
LINK SG CYS A 25 CD CD A 29 1555 1555 2.58
LINK SG CYS A 25 CD CD A 31 1555 1555 2.58
LINK SG CYS A 27 CD CD A 31 1555 1555 2.56
SITE 1 AC1 4 CYS A 5 CYS A 9 CYS A 22 CYS A 25
SITE 1 AC2 4 CYS A 4 CYS A 5 CYS A 16 CYS A 20
SITE 1 AC3 4 CYS A 11 CYS A 16 CYS A 25 CYS A 27
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 - 9 202 Bytes