Header list of 2gqm.pdb file
Complete list - r 9 2 Bytes
HEADER METAL TRANSPORT 21-APR-06 2GQM
TITLE SOLUTION STRUCTURE OF HUMAN CU(I)-SCO1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SCO1 PROTEIN HOMOLOG, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (RESIDUES 132-301);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SCO1, SCOD1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3 GOLD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET6-30A
KEYWDS THIOREDOXIN-LIKE FOLD, METALLOPROTEIN, STRUCTURAL GENOMICS,
KEYWDS 2 STRUCTURAL PROTEOMICS IN EUROPE, SPINE, METAL TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR L.BANCI,I.BERTINI,V.CALDERONE,S.CIOFI-BAFFONI,S.MANGANI,P.PALUMAA,
AUTHOR 2 M.MARTINELLI,S.WANG,STRUCTURAL PROTEOMICS IN EUROPE (SPINE)
REVDAT 4 09-MAR-22 2GQM 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 2GQM 1 VERSN
REVDAT 2 20-JUN-06 2GQM 1 JRNL
REVDAT 1 06-JUN-06 2GQM 0
JRNL AUTH L.BANCI,I.BERTINI,V.CALDERONE,S.CIOFI-BAFFONI,S.MANGANI,
JRNL AUTH 2 M.MARTINELLI,P.PALUMAA,S.WANG
JRNL TITL A HINT FOR THE FUNCTION OF HUMAN SCO1 FROM DIFFERENT
JRNL TITL 2 STRUCTURES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 8595 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 16735468
JRNL DOI 10.1073/PNAS.0601375103
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, AMBER 8.0
REMARK 3 AUTHORS :
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH,
REMARK 3 WEINER,KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GQM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037434.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 50MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM HUMAN CU(I) SCO1 U-15N, 13C,
REMARK 210 50MM PHOSPHATE BUFFER NA, 1MM
REMARK 210 DTT, 90% H2O, 10% D2O; 1MM HUMAN
REMARK 210 CU(I) SCO1 U-15N, 50MM PHOSPHATE
REMARK 210 BUFFER NA, 1MM DTT, 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY;
REMARK 210 CBCA(CO)NH; HNCA; HN(CO)CA
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 900 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CARA 2.1, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 350
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 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 HG SER A 202 OD2 ASP A 208 1.57
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 1 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 1 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 1 ARG A 239 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 1 ARG A 282 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 THR A 191 CA - CB - CG2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 3 ARG A 239 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 3 ARG A 282 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 ARG A 298 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 5 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 5 ARG A 298 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 6 ARG A 298 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 7 ARG A 295 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 8 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 8 ARG A 295 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 10 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 10 ARG A 298 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 10 ARG A 298 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 11 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 11 ARG A 282 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 13 ARG A 282 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 13 TYR A 297 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 14 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 14 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 14 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 15 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 15 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 15 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 16 THR A 192 CA - CB - CG2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 16 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 16 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 16 ARG A 282 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 17 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 17 ARG A 282 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 17 ARG A 282 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 18 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 18 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 18 ARG A 282 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 19 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 19 ARG A 282 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 20 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 21 ARG A 282 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 22 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 22 ARG A 242 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 23 TYR A 216 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 23 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 23 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 23 ARG A 298 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 25 CYS A 173 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 25 ARG A 282 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 25 ARG A 298 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 60 ANGLE DEVIATIONS.
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 PHE A 130 46.90 -81.53
REMARK 500 1 THR A 131 -161.54 -75.62
REMARK 500 1 LYS A 133 -32.64 107.83
REMARK 500 1 LEU A 136 -167.10 -118.70
REMARK 500 1 TYR A 155 40.83 -96.04
REMARK 500 1 HIS A 168 -48.81 173.79
REMARK 500 1 CYS A 169 -161.86 52.10
REMARK 500 1 PRO A 170 -74.87 -71.66
REMARK 500 1 ASP A 171 30.17 -163.68
REMARK 500 1 THR A 191 -36.72 76.85
REMARK 500 1 ASP A 204 74.71 -119.54
REMARK 500 1 GLU A 206 -51.44 77.53
REMARK 500 1 SER A 246 106.29 -162.69
REMARK 500 1 ASP A 251 -72.21 -115.90
REMARK 500 1 ASP A 253 -36.23 166.71
REMARK 500 1 GLU A 254 50.60 -91.42
REMARK 500 1 TYR A 256 49.70 -166.75
REMARK 500 1 ILE A 257 152.32 -49.86
REMARK 500 1 ILE A 262 44.28 -79.31
REMARK 500 1 ASP A 270 -69.17 -177.52
REMARK 500 1 LYS A 300 -134.02 58.21
REMARK 500 2 ASP A 152 -69.36 -28.04
REMARK 500 2 LYS A 153 0.04 -65.86
REMARK 500 2 THR A 167 23.41 -73.59
REMARK 500 2 HIS A 168 32.83 -165.66
REMARK 500 2 ASP A 171 -17.49 68.07
REMARK 500 2 THR A 191 60.54 -63.98
REMARK 500 2 THR A 192 -24.22 -173.18
REMARK 500 2 ASP A 204 77.06 -118.05
REMARK 500 2 GLU A 206 -124.18 -157.45
REMARK 500 2 ARG A 207 11.25 -54.99
REMARK 500 2 SER A 221 143.10 150.42
REMARK 500 2 ARG A 242 -41.72 65.71
REMARK 500 2 VAL A 243 103.13 18.85
REMARK 500 2 LYS A 250 156.43 115.86
REMARK 500 2 ASP A 251 -132.32 -95.00
REMARK 500 2 ASP A 253 -71.34 -164.41
REMARK 500 2 GLN A 279 3.29 -54.50
REMARK 500 2 ASN A 280 -45.35 -135.96
REMARK 500 2 ARG A 282 155.01 -48.07
REMARK 500 2 LYS A 283 -70.22 -41.70
REMARK 500 3 THR A 131 65.29 175.50
REMARK 500 3 SER A 141 22.07 -141.35
REMARK 500 3 ASP A 152 2.65 -63.96
REMARK 500 3 HIS A 168 -28.51 -174.91
REMARK 500 3 PRO A 170 -168.09 -76.96
REMARK 500 3 THR A 191 2.05 -176.82
REMARK 500 3 THR A 192 41.59 77.20
REMARK 500 3 LEU A 193 150.46 -40.20
REMARK 500 3 ASP A 195 154.45 161.34
REMARK 500
REMARK 500 THIS ENTRY HAS 633 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 CYS A 169 PRO A 170 1 120.35
REMARK 500 LYS A 299 LYS A 300 2 149.06
REMARK 500 PRO A 269 ASP A 270 3 -143.81
REMARK 500 PRO A 170 ASP A 171 4 -148.07
REMARK 500 THR A 192 LEU A 193 4 143.04
REMARK 500 LYS A 250 ASP A 251 4 -147.04
REMARK 500 LYS A 300 SER A 301 4 -135.37
REMARK 500 ASP A 251 GLU A 252 5 -148.97
REMARK 500 GLU A 254 ASP A 255 5 -147.23
REMARK 500 PRO A 269 ASP A 270 5 -149.02
REMARK 500 PRO A 194 ASP A 195 6 146.00
REMARK 500 VAL A 243 TYR A 244 6 148.97
REMARK 500 LYS A 300 SER A 301 7 134.97
REMARK 500 LYS A 300 SER A 301 8 147.38
REMARK 500 THR A 167 HIS A 168 9 -149.50
REMARK 500 PRO A 170 ASP A 171 9 136.17
REMARK 500 ASP A 251 GLU A 252 9 136.30
REMARK 500 GLU A 254 ASP A 255 9 149.91
REMARK 500 ASP A 255 TYR A 256 9 131.73
REMARK 500 GLY A 278 GLN A 279 9 147.99
REMARK 500 PRO A 296 TYR A 297 9 149.61
REMARK 500 PHE A 140 SER A 141 10 148.95
REMARK 500 CYS A 169 PRO A 170 10 143.02
REMARK 500 ILE A 190 THR A 191 10 144.20
REMARK 500 ASP A 195 LEU A 196 10 143.70
REMARK 500 ASP A 255 TYR A 256 10 148.23
REMARK 500 ASN A 280 LYS A 281 10 -139.58
REMARK 500 GLU A 254 ASP A 255 11 148.08
REMARK 500 ASP A 255 TYR A 256 12 145.57
REMARK 500 PRO A 205 GLU A 206 13 -147.23
REMARK 500 GLU A 254 ASP A 255 13 132.31
REMARK 500 ASP A 255 TYR A 256 13 140.64
REMARK 500 ASN A 280 LYS A 281 13 -143.58
REMARK 500 PRO A 269 ASP A 270 14 -149.01
REMARK 500 ARG A 298 LYS A 299 14 -146.87
REMARK 500 LYS A 300 SER A 301 14 -138.86
REMARK 500 PRO A 269 ASP A 270 15 -135.81
REMARK 500 CYS A 169 PRO A 170 16 139.98
REMARK 500 THR A 191 THR A 192 16 -121.30
REMARK 500 THR A 192 LEU A 193 16 136.47
REMARK 500 ASN A 280 LYS A 281 16 -143.83
REMARK 500 LYS A 300 SER A 301 16 139.32
REMARK 500 SER A 129 PHE A 130 17 142.93
REMARK 500 ILE A 190 THR A 191 17 147.01
REMARK 500 GLY A 229 THR A 230 17 136.48
REMARK 500 SER A 129 PHE A 130 18 138.48
REMARK 500 GLY A 157 GLN A 158 18 149.57
REMARK 500 VAL A 172 CYS A 173 18 -147.77
REMARK 500 GLN A 182 VAL A 183 18 147.42
REMARK 500 ASP A 255 TYR A 256 18 149.65
REMARK 500
REMARK 500 THIS ENTRY HAS 84 NON CIS, NON-TRANS OMEGA OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 2 ARG A 207 0.10 SIDE CHAIN
REMARK 500 4 TYR A 216 0.10 SIDE CHAIN
REMARK 500 4 ARG A 231 0.16 SIDE CHAIN
REMARK 500 5 ARG A 207 0.10 SIDE CHAIN
REMARK 500 5 TYR A 241 0.07 SIDE CHAIN
REMARK 500 6 ARG A 207 0.10 SIDE CHAIN
REMARK 500 6 TYR A 244 0.07 SIDE CHAIN
REMARK 500 7 TYR A 245 0.07 SIDE CHAIN
REMARK 500 9 TYR A 216 0.07 SIDE CHAIN
REMARK 500 9 TYR A 241 0.08 SIDE CHAIN
REMARK 500 11 TYR A 163 0.08 SIDE CHAIN
REMARK 500 13 ARG A 207 0.08 SIDE CHAIN
REMARK 500 14 ARG A 149 0.10 SIDE CHAIN
REMARK 500 14 TYR A 244 0.07 SIDE CHAIN
REMARK 500 16 ARG A 231 0.09 SIDE CHAIN
REMARK 500 17 ARG A 231 0.10 SIDE CHAIN
REMARK 500 17 ARG A 282 0.08 SIDE CHAIN
REMARK 500 18 ARG A 149 0.10 SIDE CHAIN
REMARK 500 18 TYR A 216 0.07 SIDE CHAIN
REMARK 500 18 TYR A 244 0.08 SIDE CHAIN
REMARK 500 19 TYR A 163 0.09 SIDE CHAIN
REMARK 500 19 ARG A 242 0.10 SIDE CHAIN
REMARK 500 23 TYR A 163 0.07 SIDE CHAIN
REMARK 500 26 ARG A 149 0.08 SIDE CHAIN
REMARK 500 26 TYR A 216 0.07 SIDE CHAIN
REMARK 500 27 TYR A 216 0.07 SIDE CHAIN
REMARK 500 29 ARG A 149 0.08 SIDE CHAIN
REMARK 500 30 ARG A 295 0.11 SIDE CHAIN
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 CU1 A 302 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 169 SG
REMARK 620 2 CYS A 173 SG 111.0
REMARK 620 3 HIS A 260 NE2 125.0 110.4
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GQK RELATED DB: PDB
REMARK 900 THE FAMILY STRUCTURES OF THE SAME PROTEIN METALIZED WITH NI(II)
REMARK 900 IONS.
REMARK 900 RELATED ID: 2GQL RELATED DB: PDB
REMARK 900 THE MINIMIZED AVERAGE STRUCTURE OF THE SAME PROTEIN METALIZED WITH
REMARK 900 NI(II) IONS.
REMARK 900 RELATED ID: CIRMMP13 RELATED DB: TARGETDB
DBREF 2GQM A 132 301 UNP O75880 SCO1_HUMAN 132 301
SEQADV 2GQM SER A 129 UNP O75880 CLONING ARTIFACT
SEQADV 2GQM PHE A 130 UNP O75880 CLONING ARTIFACT
SEQADV 2GQM THR A 131 UNP O75880 CLONING ARTIFACT
SEQRES 1 A 173 SER PHE THR GLY LYS PRO LEU LEU GLY GLY PRO PHE SER
SEQRES 2 A 173 LEU THR THR HIS THR GLY GLU ARG LYS THR ASP LYS ASP
SEQRES 3 A 173 TYR LEU GLY GLN TRP LEU LEU ILE TYR PHE GLY PHE THR
SEQRES 4 A 173 HIS CYS PRO ASP VAL CYS PRO GLU GLU LEU GLU LYS MET
SEQRES 5 A 173 ILE GLN VAL VAL ASP GLU ILE ASP SER ILE THR THR LEU
SEQRES 6 A 173 PRO ASP LEU THR PRO LEU PHE ILE SER ILE ASP PRO GLU
SEQRES 7 A 173 ARG ASP THR LYS GLU ALA ILE ALA ASN TYR VAL LYS GLU
SEQRES 8 A 173 PHE SER PRO LYS LEU VAL GLY LEU THR GLY THR ARG GLU
SEQRES 9 A 173 GLU VAL ASP GLN VAL ALA ARG ALA TYR ARG VAL TYR TYR
SEQRES 10 A 173 SER PRO GLY PRO LYS ASP GLU ASP GLU ASP TYR ILE VAL
SEQRES 11 A 173 ASP HIS THR ILE ILE MET TYR LEU ILE GLY PRO ASP GLY
SEQRES 12 A 173 GLU PHE LEU ASP TYR PHE GLY GLN ASN LYS ARG LYS GLY
SEQRES 13 A 173 GLU ILE ALA ALA SER ILE ALA THR HIS MET ARG PRO TYR
SEQRES 14 A 173 ARG LYS LYS SER
HET CU1 A 302 1
HETNAM CU1 COPPER (I) ION
FORMUL 2 CU1 CU 1+
HELIX 1 1 VAL A 172 SER A 189 1 18
HELIX 2 2 THR A 209 SER A 221 1 13
HELIX 3 3 THR A 230 TYR A 241 1 12
HELIX 4 4 ARG A 282 MET A 294 1 13
SHEET 1 A 6 THR A 143 THR A 144 0
SHEET 2 A 6 VAL A 225 THR A 228 -1 O THR A 228 N THR A 143
SHEET 3 A 6 LEU A 196 SER A 202 1 N PHE A 200 O VAL A 225
SHEET 4 A 6 TRP A 159 GLY A 165 1 N LEU A 161 O LEU A 199
SHEET 5 A 6 ILE A 263 ILE A 267 -1 O ILE A 267 N LEU A 160
SHEET 6 A 6 PHE A 273 GLY A 278 -1 O ASP A 275 N LEU A 266
SHEET 1 B 2 TYR A 245 PRO A 247 0
SHEET 2 B 2 VAL A 258 HIS A 260 -1 O ASP A 259 N SER A 246
LINK SG CYS A 169 CU CU1 A 302 1555 1555 2.41
LINK SG CYS A 173 CU CU1 A 302 1555 1555 2.40
LINK NE2 HIS A 260 CU CU1 A 302 1555 1555 2.08
SITE 1 AC1 4 PHE A 166 CYS A 169 CYS A 173 HIS A 260
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 - r 9 2 Bytes