Header list of 1ji9.pdb file
Complete list - 23 202 Bytes
HEADER METAL BINDING PROTEIN 01-JUL-01 1JI9
TITLE SOLUTION STRUCTURE OF THE ALPHA-DOMAIN OF MOUSE METALLOTHIONEIN-3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METALLOTHIONEIN-III;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL (ALPHA) DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET3D
KEYWDS 3-10 HELIX, CD-S CLUSTER, HALF TURN, TYPE II TURN, METAL BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR G.OZ,K.ZANGGER,I.M.ARMITAGE
REVDAT 3 23-FEB-22 1JI9 1 REMARK LINK
REVDAT 2 24-FEB-09 1JI9 1 VERSN
REVDAT 1 03-OCT-01 1JI9 0
JRNL AUTH G.OZ,K.ZANGGER,I.M.ARMITAGE
JRNL TITL THREE-DIMENSIONAL STRUCTURE AND DYNAMICS OF A BRAIN SPECIFIC
JRNL TITL 2 GROWTH INHIBITORY FACTOR: METALLOTHIONEIN-3.
JRNL REF BIOCHEMISTRY V. 40 11433 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11560491
JRNL DOI 10.1021/BI010827L
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 A TOTAL OF 377 NOE-DERIVED DISTANCE CONSTRAINTS
REMARK 3 AND 16 CADMIUM-TO-CYSTEINE CONNECTIVITIES
REMARK 3 WERE USED IN THE STRUCTURE CALCULATIONS.
REMARK 4
REMARK 4 1JI9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013803.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283; 303
REMARK 210 PH : 6.5; 6.5
REMARK 210 IONIC STRENGTH : 20MM TRIS-HCL; 20MM TRIS-HCL
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.6 MM MOUSE METALLOTHIONEIN-3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 1H-113CD
REMARK 210 HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY
REMARK 210 -DYNAMICAL SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED AVERAGE STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES AND 2D 1H-113CD HMQC SPECTROSCOPY.
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: 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 O GLU A 55 HZ3 LYS A 58 1.45
REMARK 500 HG CYS A 51 CD CD A 69 1.55
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 ALA A 46 N - CA - CB ANGL. DEV. = -8.6 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 CYS A 34 26.23 35.46
REMARK 500 CYS A 42 107.49 -48.95
REMARK 500 ASP A 48 41.43 178.51
REMARK 500 CYS A 49 88.05 55.02
REMARK 500 GLU A 54 45.94 -86.36
REMARK 500 GLU A 55 -99.25 -94.81
REMARK 500 ALA A 57 40.09 -88.19
REMARK 500 LYS A 58 132.69 -38.74
REMARK 500 ALA A 61 -25.93 -38.54
REMARK 500 GLU A 62 -21.06 89.79
REMARK 500 CYS A 64 -165.93 -118.51
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 70 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 34 O
REMARK 620 2 CYS A 34 SG 65.3
REMARK 620 3 CYS A 35 SG 58.0 110.0
REMARK 620 4 CYS A 45 SG 169.2 107.7 120.6
REMARK 620 5 CYS A 49 SG 83.2 109.4 101.3 107.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 72 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 35 SG
REMARK 620 2 CYS A 37 SG 100.9
REMARK 620 3 CYS A 38 SG 110.1 107.0
REMARK 620 4 CYS A 51 SG 106.8 122.2 109.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 71 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 38 SG
REMARK 620 2 CYS A 42 SG 96.5
REMARK 620 3 CYS A 45 SG 117.5 114.1
REMARK 620 4 CYS A 67 SG 109.8 99.1 116.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 69 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 51 SG
REMARK 620 2 CYS A 64 SG 113.4
REMARK 620 3 CYS A 66 SG 108.7 106.2
REMARK 620 4 CYS A 67 SG 102.2 110.2 116.3
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 69
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 70
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 71
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 72
DBREF 1JI9 A 32 68 UNP P28184 MT3_MOUSE 1 37
SEQRES 1 A 37 LYS SER CYS CYS SER CYS CYS PRO ALA GLY CYS GLU LYS
SEQRES 2 A 37 CYS ALA LYS ASP CYS VAL CYS LYS GLY GLU GLU GLY ALA
SEQRES 3 A 37 LYS ALA GLU ALA GLU LYS CYS SER CYS CYS GLN
HET CD A 69 1
HET CD A 70 1
HET CD A 71 1
HET CD A 72 1
HETNAM CD CADMIUM ION
FORMUL 2 CD 4(CD 2+)
LINK O CYS A 34 CD CD A 70 1555 1555 2.90
LINK SG CYS A 34 CD CD A 70 1555 1555 2.52
LINK SG CYS A 35 CD CD A 70 1555 1555 2.51
LINK SG CYS A 35 CD CD A 72 1555 1555 2.49
LINK SG CYS A 37 CD CD A 72 1555 1555 2.51
LINK SG CYS A 38 CD CD A 71 1555 1555 2.49
LINK SG CYS A 38 CD CD A 72 1555 1555 2.50
LINK SG CYS A 42 CD CD A 71 1555 1555 2.50
LINK SG CYS A 45 CD CD A 70 1555 1555 2.52
LINK SG CYS A 45 CD CD A 71 1555 1555 2.53
LINK SG CYS A 49 CD CD A 70 1555 1555 2.51
LINK SG CYS A 51 CD CD A 69 1555 1555 2.51
LINK SG CYS A 51 CD CD A 72 1555 1555 2.51
LINK SG CYS A 64 CD CD A 69 1555 1555 2.51
LINK SG CYS A 66 CD CD A 69 1555 1555 2.51
LINK SG CYS A 67 CD CD A 69 1555 1555 2.51
LINK SG CYS A 67 CD CD A 71 1555 1555 2.51
SITE 1 AC1 6 CYS A 51 CYS A 64 CYS A 66 CYS A 67
SITE 2 AC1 6 CD A 71 CD A 72
SITE 1 AC2 4 CYS A 34 CYS A 35 CYS A 45 CYS A 49
SITE 1 AC3 7 CYS A 38 CYS A 42 CYS A 45 CYS A 51
SITE 2 AC3 7 CYS A 67 CD A 69 CD A 72
SITE 1 AC4 7 CYS A 35 CYS A 37 CYS A 38 CYS A 51
SITE 2 AC4 7 CYS A 64 CD A 69 CD A 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
Complete list - 23 202 Bytes