Header list of 2gqk.pdb file
Complete list - r 9 2 Bytes
HEADER METAL TRANSPORT 21-APR-06 2GQK
TITLE SOLUTION STRUCTURE OF HUMAN NI(II)-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: PETG-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 2GQK 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 2GQK 1 VERSN
REVDAT 2 20-JUN-06 2GQK 1 JRNL
REVDAT 1 06-JUN-06 2GQK 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 2GQK 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_1000037432.
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 : 50 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM HUMAN NI(II) SCO1 U-15N,13C,
REMARK 210 50MM PHOSPHATE BUFFER NA, 1MM
REMARK 210 DTT, 90% H2O, 10% D2O; 1MM HUMAN
REMARK 210 NI(II) SCO1 U-15N, 50MM
REMARK 210 PHOSPHATE BUFFER NA, 1MM DTT, 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_ROESY; 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 : XWINNMR 3.5, 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
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. = 3.1 DEGREES
REMARK 500 1 ARG A 242 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 1 ARG A 295 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 1 ARG A 298 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 ARG A 282 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 3 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 CYS A 169 CB - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 3 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 3 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 5 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 5 ARG A 282 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 6 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 6 ARG A 298 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 7 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 7 ARG A 149 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 7 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 7 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 8 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 8 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 9 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 10 ARG A 282 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 10 ARG A 282 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 10 ARG A 298 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 11 TYR A 256 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 12 ARG A 207 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 12 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 12 ARG A 282 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 12 ARG A 298 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 12 ARG A 298 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 13 CYS A 173 CB - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 13 ARG A 239 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 14 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 15 CYS A 173 CB - CA - C ANGL. DEV. = 7.9 DEGREES
REMARK 500 16 ARG A 239 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 17 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 17 CYS A 173 CA - CB - SG ANGL. DEV. = 8.0 DEGREES
REMARK 500 17 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 17 TYR A 216 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 17 ARG A 242 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 17 ARG A 282 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 17 ARG A 295 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 17 ARG A 298 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 18 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 18 ARG A 298 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 19 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 20 ARG A 231 CD - NE - CZ ANGL. DEV. = 8.6 DEGREES
REMARK 500 20 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 21 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 77 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 THR A 131 -144.04 -167.49
REMARK 500 1 LYS A 133 44.67 -157.79
REMARK 500 1 PHE A 166 166.14 65.59
REMARK 500 1 HIS A 168 -1.42 -150.99
REMARK 500 1 ASP A 171 -57.09 -120.81
REMARK 500 1 ILE A 190 57.61 -97.82
REMARK 500 1 THR A 191 6.12 -61.91
REMARK 500 1 ASP A 204 89.73 -164.25
REMARK 500 1 GLU A 206 5.70 -69.82
REMARK 500 1 ARG A 207 20.40 -156.05
REMARK 500 1 ALA A 240 -98.70 -74.33
REMARK 500 1 TYR A 241 31.93 -81.29
REMARK 500 1 ARG A 242 -57.86 68.12
REMARK 500 1 VAL A 243 158.19 63.96
REMARK 500 1 TYR A 244 32.67 -164.22
REMARK 500 1 LYS A 250 -63.54 -123.49
REMARK 500 1 GLU A 252 -50.50 -150.71
REMARK 500 1 GLU A 254 -74.69 63.91
REMARK 500 1 LEU A 274 -53.83 -130.48
REMARK 500 1 GLN A 279 -92.64 49.81
REMARK 500 1 LYS A 281 161.75 176.98
REMARK 500 1 ARG A 298 -142.54 93.90
REMARK 500 1 LYS A 299 -60.09 57.33
REMARK 500 1 LYS A 300 -41.59 79.02
REMARK 500 2 THR A 131 59.46 -178.86
REMARK 500 2 LEU A 136 -134.54 -95.70
REMARK 500 2 GLU A 148 -145.90 -81.38
REMARK 500 2 PHE A 166 -70.05 -89.29
REMARK 500 2 THR A 167 -81.56 171.63
REMARK 500 2 HIS A 168 46.57 -84.34
REMARK 500 2 ASP A 171 -87.28 -131.01
REMARK 500 2 THR A 191 -24.85 71.67
REMARK 500 2 SER A 221 149.68 171.47
REMARK 500 2 THR A 230 -160.78 -119.56
REMARK 500 2 ASP A 251 -88.49 -77.38
REMARK 500 2 GLU A 252 -14.28 -170.28
REMARK 500 2 GLU A 254 -53.10 -173.97
REMARK 500 2 ILE A 257 166.17 54.05
REMARK 500 2 THR A 261 28.05 -70.08
REMARK 500 2 LEU A 274 -60.63 -147.95
REMARK 500 2 ASN A 280 86.85 -164.96
REMARK 500 2 ARG A 298 75.57 -65.60
REMARK 500 2 LYS A 299 148.24 55.84
REMARK 500 2 LYS A 300 5.70 109.85
REMARK 500 3 PRO A 139 55.32 -98.44
REMARK 500 3 THR A 167 -55.67 76.43
REMARK 500 3 CYS A 169 75.11 -110.20
REMARK 500 3 ASP A 171 -87.34 -126.25
REMARK 500 3 THR A 191 -19.44 68.80
REMARK 500 3 THR A 230 160.59 179.82
REMARK 500
REMARK 500 THIS ENTRY HAS 606 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 -106.69
REMARK 500 ILE A 203 ASP A 204 1 -149.91
REMARK 500 ASP A 154 TYR A 155 2 145.00
REMARK 500 GLY A 165 PHE A 166 2 148.67
REMARK 500 LYS A 299 LYS A 300 2 -135.95
REMARK 500 SER A 129 PHE A 130 5 144.16
REMARK 500 LEU A 136 GLY A 137 5 -147.20
REMARK 500 CYS A 169 PRO A 170 5 142.29
REMARK 500 ILE A 190 THR A 191 5 149.25
REMARK 500 ASP A 208 THR A 209 5 146.68
REMARK 500 ASP A 253 GLU A 254 6 132.27
REMARK 500 LYS A 299 LYS A 300 6 141.32
REMARK 500 PRO A 249 LYS A 250 7 127.43
REMARK 500 LYS A 299 LYS A 300 7 129.69
REMARK 500 CYS A 169 PRO A 170 8 -143.80
REMARK 500 GLU A 254 ASP A 255 8 147.34
REMARK 500 PRO A 170 ASP A 171 9 -128.94
REMARK 500 ARG A 207 ASP A 208 9 -141.33
REMARK 500 LYS A 153 ASP A 154 10 149.10
REMARK 500 LYS A 300 SER A 301 10 134.88
REMARK 500 LYS A 153 ASP A 154 11 142.73
REMARK 500 GLY A 157 GLN A 158 11 144.69
REMARK 500 GLY A 229 THR A 230 11 123.53
REMARK 500 LYS A 300 SER A 301 11 -146.77
REMARK 500 GLU A 252 ASP A 253 12 136.61
REMARK 500 THR A 167 HIS A 168 14 -134.72
REMARK 500 PRO A 170 ASP A 171 14 134.69
REMARK 500 PHE A 130 THR A 131 16 140.70
REMARK 500 CYS A 169 PRO A 170 17 -142.14
REMARK 500 ARG A 207 ASP A 208 17 146.46
REMARK 500 ASP A 255 TYR A 256 17 -145.16
REMARK 500 THR A 228 GLY A 229 18 149.83
REMARK 500 HIS A 260 THR A 261 18 149.29
REMARK 500 CYS A 169 PRO A 170 19 148.52
REMARK 500 LYS A 250 ASP A 251 19 -142.11
REMARK 500 LYS A 300 SER A 301 19 -139.57
REMARK 500 CYS A 169 PRO A 170 20 -137.45
REMARK 500 LYS A 300 SER A 301 20 -138.75
REMARK 500 PRO A 139 PHE A 140 21 148.77
REMARK 500 ASP A 195 LEU A 196 21 135.92
REMARK 500 LYS A 300 SER A 301 22 -149.42
REMARK 500 SER A 141 LEU A 142 23 -147.64
REMARK 500 THR A 151 ASP A 152 23 -143.95
REMARK 500 HIS A 168 CYS A 169 24 -106.31
REMARK 500 CYS A 169 PRO A 170 24 121.12
REMARK 500 ASP A 171 VAL A 172 24 -149.00
REMARK 500 ARG A 282 LYS A 283 24 -149.58
REMARK 500 LYS A 300 SER A 301 24 130.35
REMARK 500 PRO A 170 ASP A 171 26 148.40
REMARK 500 GLU A 254 ASP A 255 26 149.27
REMARK 500
REMARK 500 THIS ENTRY HAS 57 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 3 ARG A 242 0.08 SIDE CHAIN
REMARK 500 4 ARG A 207 0.11 SIDE CHAIN
REMARK 500 5 HIS A 168 0.10 SIDE CHAIN
REMARK 500 6 ARG A 298 0.09 SIDE CHAIN
REMARK 500 7 TYR A 241 0.08 SIDE CHAIN
REMARK 500 8 TYR A 241 0.11 SIDE CHAIN
REMARK 500 10 ARG A 207 0.20 SIDE CHAIN
REMARK 500 11 ARG A 149 0.09 SIDE CHAIN
REMARK 500 11 ARG A 207 0.11 SIDE CHAIN
REMARK 500 11 TYR A 241 0.09 SIDE CHAIN
REMARK 500 11 HIS A 260 0.14 SIDE CHAIN
REMARK 500 12 ARG A 231 0.14 SIDE CHAIN
REMARK 500 13 ARG A 149 0.12 SIDE CHAIN
REMARK 500 13 ARG A 231 0.09 SIDE CHAIN
REMARK 500 15 HIS A 260 0.17 SIDE CHAIN
REMARK 500 15 ARG A 295 0.10 SIDE CHAIN
REMARK 500 16 ARG A 295 0.09 SIDE CHAIN
REMARK 500 16 ARG A 298 0.13 SIDE CHAIN
REMARK 500 17 HIS A 260 0.09 SIDE CHAIN
REMARK 500 18 ARG A 207 0.10 SIDE CHAIN
REMARK 500 22 ARG A 207 0.10 SIDE CHAIN
REMARK 500 22 ARG A 231 0.12 SIDE CHAIN
REMARK 500 22 TYR A 244 0.08 SIDE CHAIN
REMARK 500 22 ARG A 298 0.09 SIDE CHAIN
REMARK 500 24 ARG A 207 0.08 SIDE CHAIN
REMARK 500 26 TYR A 241 0.08 SIDE CHAIN
REMARK 500 27 ARG A 231 0.15 SIDE CHAIN
REMARK 500 28 ARG A 231 0.10 SIDE CHAIN
REMARK 500 29 TYR A 244 0.07 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 NI A 302 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 165 O
REMARK 620 2 CYS A 169 O 140.2
REMARK 620 3 CYS A 169 SG 98.4 84.9
REMARK 620 4 CYS A 173 SG 80.0 97.3 177.8
REMARK 620 5 HIS A 260 NE2 82.5 137.4 88.6 89.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CIRMMP13 RELATED DB: TARGETDB
REMARK 900 RELATED ID: 2GQL RELATED DB: PDB
REMARK 900 RELATED ID: 2GQM RELATED DB: PDB
DBREF 2GQK A 132 301 UNP O75880 SCO1_HUMAN 132 301
SEQADV 2GQK SER A 129 UNP O75880 CLONING ARTIFACT
SEQADV 2GQK PHE A 130 UNP O75880 CLONING ARTIFACT
SEQADV 2GQK 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 NI A 302 1
HETNAM NI NICKEL (II) ION
FORMUL 2 NI NI 2+
HELIX 1 1 ASP A 152 LEU A 156 1 5
HELIX 2 2 ASP A 171 ILE A 190 1 20
HELIX 3 3 THR A 209 SER A 221 1 13
HELIX 4 4 THR A 230 TYR A 241 1 12
HELIX 5 5 ARG A 282 MET A 294 1 13
SHEET 1 A 7 ARG A 149 THR A 151 0
SHEET 2 A 7 SER A 141 THR A 144 -1 N LEU A 142 O LYS A 150
SHEET 3 A 7 VAL A 225 THR A 228 -1 O THR A 228 N THR A 143
SHEET 4 A 7 LEU A 196 ILE A 201 1 N PHE A 200 O VAL A 225
SHEET 5 A 7 TRP A 159 PHE A 164 1 N TYR A 163 O ILE A 201
SHEET 6 A 7 ILE A 263 ILE A 267 -1 O TYR A 265 N ILE A 162
SHEET 7 A 7 ASP A 275 GLY A 278 -1 O ASP A 275 N LEU A 266
LINK O GLY A 165 NI NI A 302 1555 1555 2.09
LINK O CYS A 169 NI NI A 302 1555 1555 1.96
LINK SG CYS A 169 NI NI A 302 1555 1555 2.50
LINK SG CYS A 173 NI NI A 302 1555 1555 2.54
LINK NE2 HIS A 260 NI NI A 302 1555 1555 2.18
SITE 1 AC1 4 GLY A 165 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