Header list of 1dfs.pdb file
Complete list - 16 202 Bytes
HEADER METAL BINDING PROTEIN 20-NOV-99 1DFS
TITLE SOLUTION STRUCTURE OF THE ALPHA-DOMAIN OF MOUSE METALLOTHIONEIN-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METALLOTHIONEIN-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (ALPHA);
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 BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3D
KEYWDS 3-10 HELIX, CD-S CLUSTER, HALF TURN, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR K.ZANGGER,G.OZ,J.D.OTVOS,I.M.ARMITAGE
REVDAT 4 16-FEB-22 1DFS 1 REMARK LINK
REVDAT 3 24-FEB-09 1DFS 1 VERSN
REVDAT 2 10-JAN-00 1DFS 1 JRNL COMPND
REVDAT 1 01-DEC-99 1DFS 0
JRNL AUTH K.ZANGGER,G.OZ,J.D.OTVOS,I.M.ARMITAGE
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF MOUSE
JRNL TITL 2 [CD7]-METALLOTHIONEIN-1 BY HOMONUCLEAR AND HETERONUCLEAR NMR
JRNL TITL 3 SPECTROSCOPY.
JRNL REF PROTEIN SCI. V. 8 2630 1999
JRNL REFN ISSN 0961-8368
JRNL PMID 10631978
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1A, X-PLOR 3.851
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: A TOTAL OF 278 NOE-DERIVED DISTANCE
REMARK 3 CONSTRAINTS AND 16 CD-S CONNECTIVITIES
REMARK 4
REMARK 4 1DFS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1000010045.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283; 298
REMARK 210 PH : 6.5; 6.5
REMARK 210 IONIC STRENGTH : 15MMKPI; 15MMKPI
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.7MM MOUSE-METALLOTHIONEIN-1,
REMARK 210 NATURAL ABUNDANCE, 15MM
REMARK 210 PHOSPHATE BUFFER NA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; ACCORDION CD
REMARK 210 -H HSQC
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 : X-PLOR 3.851
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 AN ACCORDION CD-H HSQC
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 LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 1 N LYS A 1 CA 0.160
REMARK 500 LYS A 1 CA LYS A 1 CB 0.162
REMARK 500 SER A 2 N SER A 2 CA 0.166
REMARK 500 SER A 2 CA SER A 2 CB 0.111
REMARK 500 SER A 2 C CYS A 3 N 0.143
REMARK 500 CYS A 3 N CYS A 3 CA 0.182
REMARK 500 CYS A 3 CA CYS A 3 CB 0.158
REMARK 500 CYS A 4 N CYS A 4 CA 0.157
REMARK 500 CYS A 4 CA CYS A 4 CB 0.166
REMARK 500 SER A 5 N SER A 5 CA 0.174
REMARK 500 SER A 5 CA SER A 5 CB 0.100
REMARK 500 SER A 5 CA SER A 5 C 0.177
REMARK 500 CYS A 6 N CYS A 6 CA 0.179
REMARK 500 CYS A 6 CA CYS A 6 CB 0.149
REMARK 500 CYS A 7 N CYS A 7 CA 0.155
REMARK 500 CYS A 7 CA CYS A 7 CB 0.136
REMARK 500 CYS A 7 C PRO A 8 N 0.153
REMARK 500 PRO A 8 N PRO A 8 CA 0.141
REMARK 500 PRO A 8 CD PRO A 8 N 0.089
REMARK 500 PRO A 8 CA PRO A 8 C 0.170
REMARK 500 PRO A 8 C VAL A 9 N 0.140
REMARK 500 VAL A 9 N VAL A 9 CA 0.192
REMARK 500 VAL A 9 CA VAL A 9 CB 0.176
REMARK 500 GLY A 10 N GLY A 10 CA 0.127
REMARK 500 GLY A 10 CA GLY A 10 C 0.142
REMARK 500 CYS A 11 N CYS A 11 CA 0.209
REMARK 500 CYS A 11 CA CYS A 11 CB 0.164
REMARK 500 CYS A 11 CA CYS A 11 C 0.179
REMARK 500 SER A 12 N SER A 12 CA 0.167
REMARK 500 SER A 12 CA SER A 12 CB 0.104
REMARK 500 LYS A 13 N LYS A 13 CA 0.154
REMARK 500 CYS A 14 N CYS A 14 CA 0.151
REMARK 500 CYS A 14 CA CYS A 14 CB 0.147
REMARK 500 CYS A 14 CA CYS A 14 C 0.175
REMARK 500 ALA A 15 N ALA A 15 CA 0.196
REMARK 500 GLN A 16 N GLN A 16 CA 0.172
REMARK 500 GLY A 17 N GLY A 17 CA 0.146
REMARK 500 GLY A 17 CA GLY A 17 C 0.098
REMARK 500 CYS A 18 N CYS A 18 CA 0.186
REMARK 500 CYS A 18 CA CYS A 18 CB 0.141
REMARK 500 CYS A 18 CA CYS A 18 C 0.166
REMARK 500 VAL A 19 N VAL A 19 CA 0.168
REMARK 500 VAL A 19 CA VAL A 19 CB 0.187
REMARK 500 VAL A 19 CB VAL A 19 CG1 0.148
REMARK 500 VAL A 19 CA VAL A 19 C 0.157
REMARK 500 CYS A 20 N CYS A 20 CA 0.161
REMARK 500 CYS A 20 CA CYS A 20 CB 0.149
REMARK 500 LYS A 21 N LYS A 21 CA 0.177
REMARK 500 LYS A 21 CD LYS A 21 CE 0.158
REMARK 500 GLY A 22 N GLY A 22 CA 0.162
REMARK 500
REMARK 500 THIS ENTRY HAS 66 BOND DEVIATIONS.
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 CYS A 3 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 CYS A 6 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 CYS A 27 CA - CB - SG ANGL. DEV. = 7.7 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 SER A 2 -92.99 -119.00
REMARK 500 CYS A 3 -45.26 -145.51
REMARK 500 PRO A 8 38.59 -85.59
REMARK 500 VAL A 9 -64.17 70.59
REMARK 500 CYS A 11 171.01 -49.28
REMARK 500 ALA A 23 -48.03 72.73
REMARK 500 ASP A 25 -64.83 -135.90
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 33 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 3 SG
REMARK 620 2 CYS A 4 SG 112.7
REMARK 620 3 CYS A 14 SG 115.0 120.1
REMARK 620 4 CYS A 18 SG 94.1 100.6 109.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 35 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 4 SG
REMARK 620 2 CYS A 6 SG 105.5
REMARK 620 3 CYS A 7 SG 119.1 121.4
REMARK 620 4 CYS A 20 SG 97.2 99.7 109.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 34 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 7 SG
REMARK 620 2 CYS A 11 SG 100.7
REMARK 620 3 CYS A 14 SG 115.0 121.4
REMARK 620 4 CYS A 30 SG 101.4 102.7 112.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 32 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 20 SG
REMARK 620 2 CYS A 27 SG 95.5
REMARK 620 3 CYS A 29 SG 103.1 115.5
REMARK 620 4 CYS A 30 SG 117.3 112.6 111.7
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 32
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 33
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 34
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 35
DBREF 1DFS A 1 31 UNP P02802 MT1_MOUSE 31 61
SEQRES 1 A 31 LYS SER CYS CYS SER CYS CYS PRO VAL GLY CYS SER LYS
SEQRES 2 A 31 CYS ALA GLN GLY CYS VAL CYS LYS GLY ALA ALA ASP LYS
SEQRES 3 A 31 CYS THR CYS CYS ALA
HET CD A 32 1
HET CD A 33 1
HET CD A 34 1
HET CD A 35 1
HETNAM CD CADMIUM ION
FORMUL 2 CD 4(CD 2+)
LINK SG CYS A 3 CD CD A 33 1555 1555 2.55
LINK SG CYS A 4 CD CD A 33 1555 1555 2.53
LINK SG CYS A 4 CD CD A 35 1555 1555 2.52
LINK SG CYS A 6 CD CD A 35 1555 1555 2.53
LINK SG CYS A 7 CD CD A 34 1555 1555 2.52
LINK SG CYS A 7 CD CD A 35 1555 1555 2.53
LINK SG CYS A 11 CD CD A 34 1555 1555 2.57
LINK SG CYS A 14 CD CD A 33 1555 1555 2.56
LINK SG CYS A 14 CD CD A 34 1555 1555 2.58
LINK SG CYS A 18 CD CD A 33 1555 1555 2.52
LINK SG CYS A 20 CD CD A 32 1555 1555 2.52
LINK SG CYS A 20 CD CD A 35 1555 1555 2.49
LINK SG CYS A 27 CD CD A 32 1555 1555 2.52
LINK SG CYS A 29 CD CD A 32 1555 1555 2.53
LINK SG CYS A 30 CD CD A 32 1555 1555 2.54
LINK SG CYS A 30 CD CD A 34 1555 1555 2.55
SITE 1 AC1 4 CYS A 20 CYS A 27 CYS A 29 CYS A 30
SITE 1 AC2 4 CYS A 3 CYS A 4 CYS A 14 CYS A 18
SITE 1 AC3 4 CYS A 7 CYS A 11 CYS A 14 CYS A 30
SITE 1 AC4 4 CYS A 4 CYS A 6 CYS A 7 CYS A 20
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 - 16 202 Bytes