Header list of 2fj4.pdb file
Complete list - 9 20 Bytes
HEADER METAL BINDING PROTEIN 31-DEC-05 2FJ4
TITLE SOLUTION STRUCTURE OF A-DOMAIN OF HUMAN METALLOTHIONEIN-3 (MT-3)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METALLOTHIONEIN-3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 32-68;
COMPND 5 SYNONYM: MT-3, METALLOTHIONEIN-III, MT-III, GROWTH INHIBITORY FACTOR,
COMPND 6 GIF, GIFB;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HUMAN METALLOTHIONEIN-3 A-DOMAIN MT-3 GIF, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.WU,Q.ZHANG
REVDAT 3 09-MAR-22 2FJ4 1 REMARK LINK
REVDAT 2 24-FEB-09 2FJ4 1 VERSN
REVDAT 1 24-JAN-06 2FJ4 0
JRNL AUTH H.WU,Q.ZHANG
JRNL TITL SOLUTION STRUCTURE OF A-DOMAIN OF HUMAN METALLOTHIONEIN-3
JRNL TITL 2 (MT-3)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, AMBER 6
REMARK 3 AUTHORS : PETER GUNTERT (DYANA), PETER KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FJ4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000035936.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 25MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 4.3MM; 4.3MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1B, XEASY
REMARK 210 METHOD USED : MOLECULAR DYNAMICS, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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: 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 VAL A 50 CA - CB - CG1 ANGL. DEV. = 11.7 DEGREES
REMARK 500 2 VAL A 50 CA - CB - CG1 ANGL. DEV. = 12.1 DEGREES
REMARK 500 2 CYS A 66 CB - CA - C ANGL. DEV. = 8.2 DEGREES
REMARK 500 3 VAL A 50 CA - CB - CG1 ANGL. DEV. = 12.0 DEGREES
REMARK 500 4 VAL A 50 CA - CB - CG1 ANGL. DEV. = 12.4 DEGREES
REMARK 500 5 VAL A 50 CG1 - CB - CG2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 5 VAL A 50 CA - CB - CG1 ANGL. DEV. = 9.9 DEGREES
REMARK 500 6 VAL A 50 CG1 - CB - CG2 ANGL. DEV. = -11.1 DEGREES
REMARK 500 6 VAL A 50 CA - CB - CG1 ANGL. DEV. = 10.1 DEGREES
REMARK 500 7 CYS A 37 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 7 VAL A 50 CA - CB - CG1 ANGL. DEV. = 12.2 DEGREES
REMARK 500 8 VAL A 50 CA - CB - CG1 ANGL. DEV. = 11.7 DEGREES
REMARK 500 8 CYS A 66 CB - CA - C ANGL. DEV. = 8.2 DEGREES
REMARK 500 9 VAL A 50 CG1 - CB - CG2 ANGL. DEV. = -11.2 DEGREES
REMARK 500 9 VAL A 50 CA - CB - CG1 ANGL. DEV. = 10.4 DEGREES
REMARK 500 10 VAL A 50 CG1 - CB - CG2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 10 VAL A 50 CA - CB - CG1 ANGL. DEV. = 10.5 DEGREES
REMARK 500 11 CYS A 37 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 11 VAL A 50 CG1 - CB - CG2 ANGL. DEV. = -11.5 DEGREES
REMARK 500 11 VAL A 50 CA - CB - CG1 ANGL. DEV. = 10.6 DEGREES
REMARK 500 12 VAL A 50 CA - CB - CG1 ANGL. DEV. = 12.8 DEGREES
REMARK 500 13 VAL A 50 CG1 - CB - CG2 ANGL. DEV. = -11.1 DEGREES
REMARK 500 13 VAL A 50 CA - CB - CG1 ANGL. DEV. = 10.3 DEGREES
REMARK 500 14 VAL A 50 CA - CB - CG1 ANGL. DEV. = 12.7 DEGREES
REMARK 500 14 CYS A 66 CB - CA - C ANGL. DEV. = 8.7 DEGREES
REMARK 500 14 CYS A 66 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 15 VAL A 50 CG1 - CB - CG2 ANGL. DEV. = -10.7 DEGREES
REMARK 500 15 VAL A 50 CA - CB - CG1 ANGL. DEV. = 9.9 DEGREES
REMARK 500 16 VAL A 50 CA - CB - CG1 ANGL. DEV. = 12.1 DEGREES
REMARK 500 17 VAL A 50 CA - CB - CG1 ANGL. DEV. = 13.0 DEGREES
REMARK 500 17 CYS A 66 CB - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 17 CYS A 66 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 18 CYS A 37 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 18 VAL A 50 CA - CB - CG1 ANGL. DEV. = 13.0 DEGREES
REMARK 500 19 VAL A 50 CG1 - CB - CG2 ANGL. DEV. = -11.2 DEGREES
REMARK 500 19 VAL A 50 CA - CB - CG1 ANGL. DEV. = 10.2 DEGREES
REMARK 500 20 VAL A 50 CG1 - CB - CG2 ANGL. DEV. = -10.8 DEGREES
REMARK 500 20 VAL A 50 CA - CB - CG1 ANGL. DEV. = 10.0 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 1 CYS A 34 8.81 -66.08
REMARK 500 1 ALA A 40 -10.68 -44.65
REMARK 500 1 CYS A 42 82.91 -58.26
REMARK 500 1 GLU A 43 -52.47 -15.86
REMARK 500 1 LYS A 47 -74.36 -59.79
REMARK 500 1 ASP A 48 48.41 -166.34
REMARK 500 1 CYS A 49 70.78 48.42
REMARK 500 1 VAL A 50 -50.44 -22.52
REMARK 500 1 GLU A 55 -76.42 -52.53
REMARK 500 1 ALA A 57 -139.77 -92.45
REMARK 500 1 ALA A 61 45.16 -82.63
REMARK 500 1 GLU A 62 -12.52 59.82
REMARK 500 1 LYS A 63 135.31 -173.25
REMARK 500 2 CYS A 34 1.10 -64.69
REMARK 500 2 CYS A 42 80.23 -59.12
REMARK 500 2 GLU A 43 -36.20 -32.82
REMARK 500 2 ASP A 48 64.01 174.92
REMARK 500 2 CYS A 49 57.68 33.36
REMARK 500 2 VAL A 50 -55.52 -5.87
REMARK 500 2 LYS A 52 -16.78 -21.28
REMARK 500 2 GLU A 55 -78.14 -69.92
REMARK 500 2 ALA A 57 -136.67 -166.10
REMARK 500 2 ALA A 61 42.94 -77.52
REMARK 500 2 GLU A 62 -17.35 61.21
REMARK 500 2 LYS A 63 138.13 -172.73
REMARK 500 2 CYS A 66 -51.19 -131.20
REMARK 500 3 CYS A 34 1.18 -63.09
REMARK 500 3 CYS A 35 -158.56 -142.45
REMARK 500 3 SER A 36 -33.58 -142.29
REMARK 500 3 ALA A 40 -9.19 -47.03
REMARK 500 3 CYS A 42 78.06 -60.36
REMARK 500 3 GLU A 43 -54.27 -16.51
REMARK 500 3 ASP A 48 44.00 -168.82
REMARK 500 3 CYS A 49 51.14 38.46
REMARK 500 3 VAL A 50 -54.71 -6.18
REMARK 500 3 LYS A 52 -59.10 16.25
REMARK 500 3 GLU A 55 -97.45 -75.02
REMARK 500 3 ALA A 57 -121.04 -159.94
REMARK 500 3 ALA A 59 -49.82 -155.25
REMARK 500 3 ALA A 61 37.25 -65.02
REMARK 500 3 GLU A 62 -16.17 72.49
REMARK 500 3 LYS A 63 148.96 -172.27
REMARK 500 3 CYS A 64 -154.40 -117.83
REMARK 500 3 SER A 65 46.53 -147.55
REMARK 500 3 CYS A 66 -57.91 -129.03
REMARK 500 4 ALA A 40 -61.13 -21.61
REMARK 500 4 CYS A 42 87.22 -22.39
REMARK 500 4 GLU A 43 -52.38 -16.29
REMARK 500 4 LYS A 47 -74.10 -59.94
REMARK 500 4 ASP A 48 47.12 -159.08
REMARK 500
REMARK 500 THIS ENTRY HAS 281 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 69 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 34 SG
REMARK 620 2 CYS A 35 SG 108.4
REMARK 620 3 CYS A 45 SG 108.0 119.9
REMARK 620 4 CYS A 49 SG 106.2 107.2 106.4
REMARK 620 N 1 2 3
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 35 SG
REMARK 620 2 CYS A 37 SG 108.6
REMARK 620 3 CYS A 38 SG 107.0 109.7
REMARK 620 4 CYS A 51 SG 108.1 111.7 111.5
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 107.5
REMARK 620 3 CYS A 45 SG 115.0 108.8
REMARK 620 4 CYS A 67 SG 108.9 106.5 109.8
REMARK 620 N 1 2 3
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 51 SG
REMARK 620 2 CYS A 64 SG 110.4
REMARK 620 3 CYS A 66 SG 109.4 109.8
REMARK 620 4 CYS A 67 SG 109.0 106.3 111.9
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 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
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FJ5 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN
DBREF 2FJ4 A 32 68 UNP P25713 MT3_HUMAN 32 68
SEQRES 1 A 37 LYS SER CYS CYS SER CYS CYS PRO ALA GLU CYS GLU LYS
SEQRES 2 A 37 CYS ALA LYS ASP CYS VAL CYS LYS GLY GLY GLU ALA ALA
SEQRES 3 A 37 GLU 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+)
HELIX 1 1 CYS A 42 CYS A 49 1 8
HELIX 2 2 VAL A 50 GLY A 54 5 5
LINK SG CYS A 34 CD CD A 69 1555 1555 2.49
LINK SG CYS A 35 CD CD A 69 1555 1555 2.50
LINK SG CYS A 35 CD CD A 70 1555 1555 2.46
LINK SG CYS A 37 CD CD A 70 1555 1555 2.49
LINK SG CYS A 38 CD CD A 70 1555 1555 2.48
LINK SG CYS A 38 CD CD A 71 1555 1555 2.48
LINK SG CYS A 42 CD CD A 71 1555 1555 2.50
LINK SG CYS A 45 CD CD A 69 1555 1555 2.53
LINK SG CYS A 45 CD CD A 71 1555 1555 2.52
LINK SG CYS A 49 CD CD A 69 1555 1555 2.49
LINK SG CYS A 51 CD CD A 70 1555 1555 2.49
LINK SG CYS A 51 CD CD A 72 1555 1555 2.50
LINK SG CYS A 64 CD CD A 72 1555 1555 2.49
LINK SG CYS A 66 CD CD A 72 1555 1555 2.50
LINK SG CYS A 67 CD CD A 71 1555 1555 2.50
LINK SG CYS A 67 CD CD A 72 1555 1555 2.50
SITE 1 AC1 4 CYS A 34 CYS A 35 CYS A 45 CYS A 49
SITE 1 AC2 4 CYS A 35 CYS A 37 CYS A 38 CYS A 51
SITE 1 AC3 4 CYS A 38 CYS A 42 CYS A 45 CYS A 67
SITE 1 AC4 5 VAL A 50 CYS A 51 CYS A 64 CYS A 66
SITE 2 AC4 5 CYS A 67
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 - 9 20 Bytes