Header list of 2gt5.pdb file
Complete list - r 9 2 Bytes
HEADER METAL TRANSPORT 27-APR-06 2GT5
TITLE SOLUTION STRUCTURE OF APO HUMAN 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 2GT5 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2GT5 1 VERSN
REVDAT 2 20-JUN-06 2GT5 1 JRNL
REVDAT 1 06-JUN-06 2GT5 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 2GT5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037517.
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 APO SCO1 U-15N, 13C,
REMARK 210 50 MM PHOSPHATE BUFFER NA, 1MM
REMARK 210 DTT, 90% H2O, 10% D2O; 1MM HUMAN
REMARK 210 APO SCO1 U-15N, 50 MM 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; CBCA(CO)NH;
REMARK 210 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 HG1 THR A 230 OE1 GLU A 233 1.55
REMARK 500 O GLU A 285 HG SER A 289 1.59
REMARK 500 OD1 ASP A 185 HG SER A 221 1.59
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 282 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 2 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 3 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 3 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 3 ARG A 282 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 3 ARG A 298 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 4 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 4 ARG A 207 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 4 ARG A 231 CD - NE - CZ ANGL. DEV. = 9.1 DEGREES
REMARK 500 4 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 4 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 4 ARG A 239 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 5 ARG A 298 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 6 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 6 TYR A 244 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 8 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 9 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 9 ARG A 298 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 10 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 11 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 11 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 12 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 12 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 12 ARG A 295 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 13 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 13 ARG A 242 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 14 PHE A 166 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 14 PHE A 166 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 16 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 17 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 17 ARG A 242 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 18 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 21 ARG A 207 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES
REMARK 500 21 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 22 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 22 ARG A 239 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 22 ARG A 282 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 22 ARG A 298 CD - NE - CZ ANGL. DEV. = 9.1 DEGREES
REMARK 500 22 ARG A 298 NE - CZ - NH1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 23 ARG A 149 NE - CZ - NH2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 23 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 23 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 24 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 26 ARG A 239 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 27 ARG A 149 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 27 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 27 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 27 VAL A 258 CG1 - CB - CG2 ANGL. DEV. = -10.4 DEGREES
REMARK 500 27 ARG A 298 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 28 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 54 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 -176.67 63.45
REMARK 500 1 LEU A 136 -138.26 -90.42
REMARK 500 1 SER A 141 38.00 -140.88
REMARK 500 1 TYR A 155 -40.66 -131.93
REMARK 500 1 LEU A 156 -36.69 135.53
REMARK 500 1 GLN A 158 79.18 -57.05
REMARK 500 1 HIS A 168 -70.16 -151.82
REMARK 500 1 PRO A 170 43.25 -87.32
REMARK 500 1 ASP A 171 -144.56 -160.24
REMARK 500 1 CYS A 173 -69.27 175.82
REMARK 500 1 PRO A 194 34.87 -77.00
REMARK 500 1 ASP A 195 165.82 67.71
REMARK 500 1 ASP A 204 -56.44 145.96
REMARK 500 1 GLU A 206 -93.09 54.83
REMARK 500 1 ARG A 207 -48.88 -170.51
REMARK 500 1 ASP A 208 -140.20 48.48
REMARK 500 1 PHE A 220 46.06 -74.54
REMARK 500 1 SER A 221 137.07 102.25
REMARK 500 1 TYR A 245 -136.55 -73.70
REMARK 500 1 ASP A 251 -105.73 -92.01
REMARK 500 1 TYR A 256 33.89 -149.14
REMARK 500 1 ILE A 257 46.95 -70.18
REMARK 500 1 VAL A 258 30.08 -70.96
REMARK 500 1 ASP A 259 157.19 57.99
REMARK 500 1 PRO A 269 45.76 -75.49
REMARK 500 1 ASP A 270 -49.46 -138.83
REMARK 500 1 LEU A 274 -35.95 -140.71
REMARK 500 1 ASN A 280 131.00 -171.49
REMARK 500 1 LYS A 281 131.37 128.49
REMARK 500 1 LYS A 299 -177.94 -65.25
REMARK 500 2 PHE A 130 88.57 -157.44
REMARK 500 2 THR A 131 -165.02 62.58
REMARK 500 2 PRO A 134 -167.91 -74.69
REMARK 500 2 LEU A 136 45.72 -86.91
REMARK 500 2 SER A 141 55.07 -142.45
REMARK 500 2 HIS A 145 1.33 57.74
REMARK 500 2 THR A 146 -86.62 -135.43
REMARK 500 2 LEU A 156 103.93 -51.11
REMARK 500 2 THR A 167 136.06 -172.14
REMARK 500 2 ILE A 190 51.67 -110.08
REMARK 500 2 THR A 191 -2.52 -47.26
REMARK 500 2 LEU A 193 172.06 -59.81
REMARK 500 2 ILE A 203 34.55 -99.12
REMARK 500 2 ARG A 207 133.20 -177.18
REMARK 500 2 ASP A 208 -166.21 -162.04
REMARK 500 2 SER A 221 144.41 -171.29
REMARK 500 2 ASP A 251 95.74 -62.23
REMARK 500 2 GLU A 252 -175.22 64.94
REMARK 500 2 GLU A 254 -178.52 66.32
REMARK 500 2 ASP A 255 -163.99 86.44
REMARK 500
REMARK 500 THIS ENTRY HAS 798 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 PRO A 194 ASP A 195 1 -149.91
REMARK 500 VAL A 243 TYR A 244 1 -139.44
REMARK 500 PRO A 249 LYS A 250 1 -143.77
REMARK 500 PHE A 220 SER A 221 2 135.79
REMARK 500 PRO A 249 LYS A 250 2 -144.93
REMARK 500 VAL A 258 ASP A 259 2 -143.32
REMARK 500 GLY A 278 GLN A 279 2 -148.18
REMARK 500 LYS A 300 SER A 301 2 -136.63
REMARK 500 ILE A 203 ASP A 204 3 148.02
REMARK 500 TYR A 245 SER A 246 3 140.78
REMARK 500 LYS A 300 SER A 301 3 135.15
REMARK 500 ARG A 149 LYS A 150 4 -148.82
REMARK 500 VAL A 172 CYS A 173 4 -147.61
REMARK 500 ILE A 203 ASP A 204 4 146.98
REMARK 500 GLU A 206 ARG A 207 4 -144.04
REMARK 500 TYR A 245 SER A 246 4 143.09
REMARK 500 THR A 167 HIS A 168 5 146.11
REMARK 500 THR A 228 GLY A 229 5 149.67
REMARK 500 ASP A 235 GLN A 236 5 146.94
REMARK 500 ASP A 251 GLU A 252 5 111.73
REMARK 500 LYS A 300 SER A 301 5 -125.93
REMARK 500 SER A 129 PHE A 130 6 145.28
REMARK 500 GLU A 206 ARG A 207 6 148.53
REMARK 500 PHE A 220 SER A 221 6 -145.96
REMARK 500 THR A 167 HIS A 168 7 -144.29
REMARK 500 SER A 202 ILE A 203 7 133.69
REMARK 500 ILE A 203 ASP A 204 7 -149.19
REMARK 500 ASP A 251 GLU A 252 7 138.97
REMARK 500 ASP A 275 TYR A 276 7 149.56
REMARK 500 PRO A 139 PHE A 140 8 146.76
REMARK 500 ASP A 204 PRO A 205 8 -67.14
REMARK 500 PRO A 222 LYS A 223 8 -147.15
REMARK 500 ASP A 251 GLU A 252 8 142.15
REMARK 500 ILE A 262 ILE A 263 8 136.65
REMARK 500 LYS A 133 PRO A 134 9 145.94
REMARK 500 THR A 151 ASP A 152 9 -143.90
REMARK 500 GLN A 182 VAL A 183 9 142.51
REMARK 500 THR A 191 THR A 192 9 147.12
REMARK 500 ASP A 204 PRO A 205 9 -146.11
REMARK 500 ASP A 251 GLU A 252 9 -139.58
REMARK 500 VAL A 258 ASP A 259 9 145.20
REMARK 500 ASP A 259 HIS A 260 9 -118.32
REMARK 500 PRO A 205 GLU A 206 10 -149.87
REMARK 500 SER A 246 PRO A 247 10 142.98
REMARK 500 ASP A 251 GLU A 252 10 -145.45
REMARK 500 ASP A 204 PRO A 205 11 -142.05
REMARK 500 GLY A 229 THR A 230 11 143.22
REMARK 500 GLU A 252 ASP A 253 11 134.30
REMARK 500 ILE A 257 VAL A 258 11 -136.53
REMARK 500 THR A 261 ILE A 262 11 144.27
REMARK 500
REMARK 500 THIS ENTRY HAS 146 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 1 TYR A 163 0.08 SIDE CHAIN
REMARK 500 1 ARG A 207 0.12 SIDE CHAIN
REMARK 500 1 ARG A 231 0.16 SIDE CHAIN
REMARK 500 2 ARG A 207 0.08 SIDE CHAIN
REMARK 500 3 TYR A 216 0.08 SIDE CHAIN
REMARK 500 3 TYR A 241 0.07 SIDE CHAIN
REMARK 500 4 TYR A 256 0.09 SIDE CHAIN
REMARK 500 6 ARG A 239 0.09 SIDE CHAIN
REMARK 500 7 TYR A 297 0.07 SIDE CHAIN
REMARK 500 7 ARG A 298 0.08 SIDE CHAIN
REMARK 500 8 ARG A 207 0.11 SIDE CHAIN
REMARK 500 8 ARG A 298 0.10 SIDE CHAIN
REMARK 500 12 ARG A 231 0.14 SIDE CHAIN
REMARK 500 13 ARG A 239 0.09 SIDE CHAIN
REMARK 500 13 HIS A 260 0.10 SIDE CHAIN
REMARK 500 13 TYR A 265 0.07 SIDE CHAIN
REMARK 500 14 ARG A 207 0.09 SIDE CHAIN
REMARK 500 15 ARG A 242 0.13 SIDE CHAIN
REMARK 500 15 TYR A 256 0.12 SIDE CHAIN
REMARK 500 17 ARG A 231 0.14 SIDE CHAIN
REMARK 500 18 ARG A 149 0.09 SIDE CHAIN
REMARK 500 18 PHE A 220 0.08 SIDE CHAIN
REMARK 500 23 PHE A 220 0.14 SIDE CHAIN
REMARK 500 23 TYR A 256 0.09 SIDE CHAIN
REMARK 500 24 ARG A 231 0.16 SIDE CHAIN
REMARK 500 26 ARG A 298 0.10 SIDE CHAIN
REMARK 500 27 TYR A 163 0.07 SIDE CHAIN
REMARK 500 27 ARG A 239 0.08 SIDE CHAIN
REMARK 500 27 TYR A 256 0.07 SIDE CHAIN
REMARK 500 28 PHE A 164 0.09 SIDE CHAIN
REMARK 500 28 ARG A 239 0.08 SIDE CHAIN
REMARK 500 28 ARG A 242 0.09 SIDE CHAIN
REMARK 500 28 TYR A 256 0.07 SIDE CHAIN
REMARK 500 28 ARG A 295 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GQK RELATED DB: PDB
REMARK 900 RELATED ID: 2GQL RELATED DB: PDB
REMARK 900 RELATED ID: 2GQM RELATED DB: PDB
REMARK 900 RELATED ID: 2GT6 RELATED DB: PDB
REMARK 900 RELATED ID: CIRMMP13 RELATED DB: TARGETDB
DBREF 2GT5 A 132 301 UNP O75880 SCO1_HUMAN 132 301
SEQADV 2GT5 SER A 129 UNP O75880 CLONING ARTIFACT
SEQADV 2GT5 PHE A 130 UNP O75880 CLONING ARTIFACT
SEQADV 2GT5 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
HELIX 1 1 THR A 151 TYR A 155 5 5
HELIX 2 2 CYS A 173 GLN A 182 1 10
HELIX 3 3 VAL A 184 SER A 189 1 6
HELIX 4 4 THR A 209 PHE A 220 1 12
HELIX 5 5 THR A 230 ARG A 242 1 13
HELIX 6 6 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 PRO A 198 SER A 202 1 N PHE A 200 O LEU A 227
SHEET 4 A 6 LEU A 160 GLY A 165 1 N GLY A 165 O ILE A 201
SHEET 5 A 6 MET A 264 ILE A 267 -1 O TYR A 265 N ILE A 162
SHEET 6 A 6 PHE A 273 PHE A 277 -1 O PHE A 277 N MET A 264
CISPEP 1 ASP A 204 PRO A 205 1 -12.18
CISPEP 2 VAL A 258 ASP A 259 6 -6.19
CISPEP 3 CYS A 169 PRO A 170 9 11.26
CISPEP 4 ASP A 204 PRO A 205 10 -24.66
CISPEP 5 HIS A 260 THR A 261 15 12.94
CISPEP 6 SER A 246 PRO A 247 17 -8.44
CISPEP 7 VAL A 258 ASP A 259 17 12.79
CISPEP 8 ILE A 203 ASP A 204 19 -13.91
CISPEP 9 TYR A 245 SER A 246 22 -3.68
CISPEP 10 SER A 246 PRO A 247 22 -7.34
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