HEADER METAL BINDING PROTEIN 13-JUN-02 1M0J
TITLE SOLUTION STRUCTURE OF THE BETA DOMAIN OF MT_NC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METALLOTHIONEIN MT_NC;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BETA DOMAIN;
COMPND 5 SYNONYM: METALLOTHIONEIN A;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOTOTHENIA CORIICEPS;
SOURCE 3 ORGANISM_COMMON: YELLOWBELLY ROCKCOD;
SOURCE 4 ORGANISM_TAXID: 8208;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEM-MT
KEYWDS CADMIUM THIOLATE-CLUSTER, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.CAPASSO,V.CARGINALE,O.CRESCENZI,D.DI MARO,E.PARISI,R.SPADACCINI,
AUTHOR 2 P.A.TEMUSSI
REVDAT 3 23-FEB-22 1M0J 1 REMARK LINK
REVDAT 2 24-FEB-09 1M0J 1 VERSN
REVDAT 1 06-MAY-03 1M0J 0
JRNL AUTH C.CAPASSO,V.CARGINALE,O.CRESCENZI,D.DI MARO,E.PARISI,
JRNL AUTH 2 R.SPADACCINI,P.A.TEMUSSI
JRNL TITL SOLUTION STRUCTURE OF MT_NC, A NOVEL METALLOTHIONEIN FROM
JRNL TITL 2 THE ANTARCTIC FISH NOTOTHENIA CORIICEPS.
JRNL REF STRUCTURE V. 11 435 2003
JRNL REFN ISSN 0969-2126
JRNL PMID 12679021
JRNL DOI 10.1016/S0969-2126(03)00044-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, DYANA 1.5
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), GUENTERT (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 253 NOES, 12 CD-S BONDS AND 63 DIHEDRAL ANGLE CONSTRAINTS
REMARK 4
REMARK 4 1M0J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JUN-02.
REMARK 100 THE DEPOSITION ID IS D_1000016446.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM METALLOTHIONEIN; 95% H2O, 5%
REMARK 210 D2O; METALLOTHIONEIN, U-113CD;
REMARK 210 95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; E-COSY; DQF
REMARK 210 -COSY; [113CD,1H]COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 4.0.3, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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
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 LYS A 14 -73.74 -64.38
REMARK 500 1 ASN A 19 54.41 -146.69
REMARK 500 1 THR A 25 -41.75 -132.91
REMARK 500 1 SER A 30 45.74 -170.45
REMARK 500 1 CYS A 34 -48.34 -144.28
REMARK 500 2 LYS A 14 -59.22 72.01
REMARK 500 2 SER A 15 -34.68 -38.70
REMARK 500 2 ASN A 19 52.45 -144.20
REMARK 500 2 CYS A 20 33.17 -88.12
REMARK 500 2 ASN A 28 67.63 -117.62
REMARK 500 2 SER A 30 53.29 -167.98
REMARK 500 2 CYS A 34 -49.18 -130.45
REMARK 500 3 LYS A 14 -54.98 85.24
REMARK 500 3 SER A 15 -31.62 -38.14
REMARK 500 3 ASN A 19 52.95 -146.19
REMARK 500 3 SER A 30 68.75 -175.15
REMARK 500 3 CYS A 31 -73.27 -121.11
REMARK 500 3 LYS A 32 137.12 -178.51
REMARK 500 3 SER A 33 9.31 81.09
REMARK 500 4 CYS A 12 -71.20 -67.77
REMARK 500 4 THR A 17 138.15 -178.92
REMARK 500 4 ASN A 19 52.40 -142.50
REMARK 500 4 SER A 23 94.85 -176.37
REMARK 500 4 SER A 30 49.79 -165.43
REMARK 500 4 CYS A 31 -91.75 -89.62
REMARK 500 4 LYS A 32 139.59 -178.99
REMARK 500 5 CYS A 12 -72.47 -70.75
REMARK 500 5 THR A 17 126.38 179.40
REMARK 500 5 SER A 30 34.51 -157.78
REMARK 500 5 CYS A 31 -90.02 -78.10
REMARK 500 6 CYS A 10 141.59 63.25
REMARK 500 6 LYS A 14 -91.91 -73.43
REMARK 500 6 CYS A 20 42.60 -107.53
REMARK 500 6 SER A 30 -27.90 -176.69
REMARK 500 6 CYS A 31 134.54 -35.90
REMARK 500 6 CYS A 34 -63.43 -108.69
REMARK 500 7 CYS A 18 100.03 -47.39
REMARK 500 7 THR A 25 -41.68 -161.47
REMARK 500 7 SER A 30 34.22 -175.04
REMARK 500 7 CYS A 31 -98.79 -68.95
REMARK 500 7 LYS A 32 -30.79 166.33
REMARK 500 7 CYS A 34 -51.62 -133.89
REMARK 500 8 CYS A 10 164.61 56.94
REMARK 500 8 CYS A 12 -75.74 -91.05
REMARK 500 8 LYS A 14 -43.31 -29.03
REMARK 500 8 SER A 15 -31.90 -36.37
REMARK 500 8 THR A 17 137.47 82.96
REMARK 500 8 CYS A 18 154.28 -41.08
REMARK 500 8 ASN A 19 57.01 -147.19
REMARK 500 8 CYS A 20 31.78 -87.12
REMARK 500
REMARK 500 THIS ENTRY HAS 142 RAMACHANDRAN OUTLIERS.
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 10 SG
REMARK 620 2 CYS A 12 SG 131.0
REMARK 620 3 CYS A 26 SG 106.4 106.9
REMARK 620 4 CYS A 29 SG 105.4 104.6 97.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 101 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 12 SG
REMARK 620 2 CYS A 18 SG 109.9
REMARK 620 3 CYS A 20 SG 97.6 101.7
REMARK 620 4 CYS A 31 SG 105.4 120.8 119.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 102 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 20 SG
REMARK 620 2 CYS A 24 SG 115.9
REMARK 620 3 CYS A 29 SG 100.0 112.7
REMARK 620 4 CYS A 34 SG 110.2 116.2 99.3
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 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 103
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M0G RELATED DB: PDB
REMARK 900 1M0G CONTAINS ALPHA DOMAIN OF THE SAME PROTEIN
DBREF 1M0J A 8 35 UNP P62339 MTA_NOTCO 2 29
SEQRES 1 A 28 ASP PRO CYS GLU CYS SER LYS SER GLY THR CYS ASN CYS
SEQRES 2 A 28 GLY GLY SER CYS THR CYS THR ASN CYS SER CYS LYS SER
SEQRES 3 A 28 CYS LYS
HET CD A 101 1
HET CD A 102 1
HET CD A 103 1
HETNAM CD CADMIUM ION
FORMUL 2 CD 3(CD 2+)
HELIX 1 1 CYS A 10 GLY A 16 1 7
LINK SG CYS A 10 CD CD A 103 1555 1555 2.30
LINK SG CYS A 12 CD CD A 101 1555 1555 2.60
LINK SG CYS A 12 CD CD A 103 1555 1555 2.32
LINK SG CYS A 18 CD CD A 101 1555 1555 2.54
LINK SG CYS A 20 CD CD A 101 1555 1555 2.58
LINK SG CYS A 20 CD CD A 102 1555 1555 2.60
LINK SG CYS A 24 CD CD A 102 1555 1555 2.29
LINK SG CYS A 26 CD CD A 103 1555 1555 2.57
LINK SG CYS A 29 CD CD A 102 1555 1555 2.60
LINK SG CYS A 29 CD CD A 103 1555 1555 2.60
LINK SG CYS A 31 CD CD A 101 1555 1555 2.30
LINK SG CYS A 34 CD CD A 102 1555 1555 2.52
SITE 1 AC1 4 CYS A 12 CYS A 18 CYS A 20 CYS A 31
SITE 1 AC2 4 CYS A 20 CYS A 24 CYS A 29 CYS A 34
SITE 1 AC3 4 CYS A 10 CYS A 12 CYS A 26 CYS A 29
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
(ATOM LINES ARE NOT SHOWN.)
END
