Header list of 2fj5.pdb file
Complete list - 9 20 Bytes
HEADER METAL BINDING PROTEIN 31-DEC-05 2FJ5 TITLE SOLUTION STRUCTURE OF SOLE 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 SOLE A-DOMAIN HUMAN METALLOTHIONEIN-3 MT-3 GIF, METAL BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR H.WU,Q.ZHANG REVDAT 3 09-MAR-22 2FJ5 1 REMARK LINK REVDAT 2 24-FEB-09 2FJ5 1 VERSN REVDAT 1 24-JAN-06 2FJ5 0 JRNL AUTH H.WU,Q.ZHANG JRNL TITL SOLUTION STRUCTURE OF SOLE A-DOMAIN OF HUMAN JRNL TITL 2 METALLOTHIONEIN-3 (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 2FJ5 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_1000035937. 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 : 3.7MM; 3.7MM 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 : SIMULATED 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 CYS A 35 CA - CB - SG ANGL. DEV. = 8.2 DEGREES REMARK 500 1 CYS A 49 CB - CA - C ANGL. DEV. = 8.4 DEGREES REMARK 500 2 CYS A 35 CA - CB - SG ANGL. DEV. = 8.3 DEGREES REMARK 500 5 CYS A 49 CB - CA - C ANGL. DEV. = 7.3 DEGREES REMARK 500 8 CYS A 35 CA - CB - SG ANGL. DEV. = 8.2 DEGREES REMARK 500 8 CYS A 49 CB - CA - C ANGL. DEV. = 7.8 DEGREES REMARK 500 9 CYS A 35 CA - CB - SG ANGL. DEV. = 7.8 DEGREES REMARK 500 10 CYS A 35 CA - CB - SG ANGL. DEV. = 8.3 DEGREES REMARK 500 13 CYS A 35 CA - CB - SG ANGL. DEV. = 6.8 DEGREES REMARK 500 13 CYS A 38 CB - CA - C ANGL. DEV. = 8.2 DEGREES REMARK 500 14 CYS A 35 CA - CB - SG ANGL. DEV. = 8.6 DEGREES REMARK 500 15 CYS A 35 CA - CB - SG ANGL. DEV. = 8.8 DEGREES REMARK 500 16 CYS A 35 CA - CB - SG ANGL. DEV. = 7.6 DEGREES REMARK 500 17 CYS A 35 CA - CB - SG ANGL. DEV. = 13.6 DEGREES REMARK 500 17 CYS A 38 CB - CA - C ANGL. DEV. = 7.9 DEGREES REMARK 500 18 CYS A 35 CA - CB - SG ANGL. DEV. = 7.8 DEGREES REMARK 500 19 CYS A 35 CA - CB - SG ANGL. DEV. = 9.2 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 -60.18 -178.31 REMARK 500 1 CYS A 37 0.17 -63.41 REMARK 500 1 PRO A 39 -73.61 -62.55 REMARK 500 1 ALA A 40 -40.65 -166.99 REMARK 500 1 CYS A 42 99.36 -53.39 REMARK 500 1 GLU A 43 -35.69 -37.10 REMARK 500 1 VAL A 50 -26.58 -33.02 REMARK 500 1 LYS A 52 38.70 35.95 REMARK 500 1 GLU A 55 -89.21 -91.69 REMARK 500 1 ALA A 56 49.01 -76.43 REMARK 500 1 ALA A 59 -21.25 59.76 REMARK 500 1 GLU A 60 -28.81 73.88 REMARK 500 1 GLU A 62 -16.26 65.75 REMARK 500 1 LYS A 63 73.60 -170.72 REMARK 500 2 SER A 33 -71.54 -74.65 REMARK 500 2 CYS A 34 -39.56 161.48 REMARK 500 2 ALA A 40 -35.79 160.49 REMARK 500 2 CYS A 42 103.46 -51.27 REMARK 500 2 ASP A 48 17.28 -173.98 REMARK 500 2 VAL A 50 -35.55 -26.13 REMARK 500 2 LYS A 52 11.49 40.00 REMARK 500 2 GLU A 60 -36.49 75.97 REMARK 500 2 CYS A 64 -100.72 -96.56 REMARK 500 2 SER A 65 -40.80 176.97 REMARK 500 3 SER A 33 -70.26 -67.16 REMARK 500 3 CYS A 34 17.07 -164.54 REMARK 500 3 CYS A 35 -177.56 -170.13 REMARK 500 3 SER A 36 44.24 -144.79 REMARK 500 3 PRO A 39 -96.08 -78.17 REMARK 500 3 GLU A 41 12.88 -142.11 REMARK 500 3 CYS A 42 106.81 -39.88 REMARK 500 3 ASP A 48 58.48 -175.63 REMARK 500 3 CYS A 49 59.88 38.87 REMARK 500 3 VAL A 50 -24.07 -37.66 REMARK 500 3 GLU A 55 -103.06 -99.19 REMARK 500 3 GLU A 58 119.07 72.91 REMARK 500 3 GLU A 60 -3.62 -54.12 REMARK 500 3 CYS A 64 -106.93 -90.73 REMARK 500 3 SER A 65 -43.15 -178.41 REMARK 500 4 SER A 33 -90.93 -69.90 REMARK 500 4 SER A 36 48.35 -140.26 REMARK 500 4 ALA A 40 -39.71 173.55 REMARK 500 4 CYS A 42 102.07 -51.74 REMARK 500 4 ALA A 46 -9.39 -58.86 REMARK 500 4 LYS A 47 -60.80 -90.21 REMARK 500 4 ASP A 48 47.04 -156.22 REMARK 500 4 VAL A 50 -23.50 -33.77 REMARK 500 4 GLU A 60 -33.73 72.52 REMARK 500 4 ALA A 61 21.73 -73.51 REMARK 500 4 GLU A 62 -17.12 67.16 REMARK 500 REMARK 500 THIS ENTRY HAS 263 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 LYS A 47 ASP A 48 2 -148.10 REMARK 500 CYS A 34 CYS A 35 4 -148.82 REMARK 500 CYS A 34 CYS A 35 5 143.43 REMARK 500 CYS A 38 PRO A 39 5 -143.63 REMARK 500 CYS A 38 PRO A 39 6 -147.41 REMARK 500 CYS A 38 PRO A 39 7 -145.39 REMARK 500 CYS A 38 PRO A 39 8 -139.94 REMARK 500 CYS A 38 PRO A 39 9 -145.52 REMARK 500 CYS A 38 PRO A 39 10 -141.80 REMARK 500 CYS A 38 PRO A 39 12 -147.01 REMARK 500 CYS A 38 PRO A 39 14 -143.25 REMARK 500 CYS A 38 PRO A 39 15 -141.49 REMARK 500 CYS A 38 PRO A 39 16 -148.41 REMARK 500 LYS A 47 ASP A 48 16 -147.31 REMARK 500 SER A 33 CYS A 34 17 -148.94 REMARK 500 CYS A 38 PRO A 39 17 -148.80 REMARK 500 LYS A 47 ASP A 48 17 -139.70 REMARK 500 CYS A 38 PRO A 39 18 -147.29 REMARK 500 CYS A 38 PRO A 39 19 -140.81 REMARK 500 CYS A 38 PRO A 39 20 -141.86 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 110.9 REMARK 620 3 CYS A 45 SG 108.5 115.9 REMARK 620 4 CYS A 49 SG 109.3 106.2 105.8 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 109.2 REMARK 620 3 CYS A 38 SG 105.8 111.7 REMARK 620 4 CYS A 51 SG 106.4 111.0 112.5 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 105.4 REMARK 620 3 CYS A 45 SG 113.6 109.5 REMARK 620 4 CYS A 67 SG 110.5 110.7 107.3 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 109.5 REMARK 620 3 CYS A 66 SG 108.5 109.3 REMARK 620 4 CYS A 67 SG 107.9 107.4 114.1 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: 2FJ4 RELATED DB: PDB REMARK 900 THE SAME PROTEIN DBREF 2FJ5 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 LINK SG CYS A 34 CD CD A 69 1555 1555 2.50 LINK SG CYS A 35 CD CD A 69 1555 1555 2.53 LINK SG CYS A 35 CD CD A 70 1555 1555 2.47 LINK SG CYS A 37 CD CD A 70 1555 1555 2.50 LINK SG CYS A 38 CD CD A 70 1555 1555 2.49 LINK SG CYS A 38 CD CD A 71 1555 1555 2.47 LINK SG CYS A 42 CD CD A 71 1555 1555 2.49 LINK SG CYS A 45 CD CD A 69 1555 1555 2.52 LINK SG CYS A 45 CD CD A 71 1555 1555 2.49 LINK SG CYS A 49 CD CD A 69 1555 1555 2.50 LINK SG CYS A 51 CD CD A 70 1555 1555 2.48 LINK SG CYS A 51 CD CD A 72 1555 1555 2.48 LINK SG CYS A 64 CD CD A 72 1555 1555 2.48 LINK SG CYS A 66 CD CD A 72 1555 1555 2.51 LINK SG CYS A 67 CD CD A 71 1555 1555 2.51 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 4 CYS A 51 CYS A 64 CYS A 66 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