HEADER HYDROLASE 30-JUL-09 3IHR
TITLE CRYSTAL STRUCTURE OF UCH37
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L5;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: UCH-L5, UBIQUITIN THIOESTERASE L5, UBIQUITIN C-TERMINAL
COMPND 5 HYDROLASE UCH37;
COMPND 6 EC: 3.4.19.12;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: AD-019, CGI-70, UCH37, UCHL5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834 PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PVP 16
KEYWDS CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS, UCH37, UCH-L5, UBIQUITIN
KEYWDS 2 HYDROLASE, HOMO SAPIENS, UBIQUITIN, PROTEASOME, INO80, SMAD7, RPN13,
KEYWDS 3 PSI, PROTEIN STRUCTURE INITIATIVE, CESG, STRUCTURAL GENOMICS,
KEYWDS 4 HYDROLASE, PROTEASE, THIOL PROTEASE, UBL CONJUGATION PATHWAY
EXPDTA X-RAY DIFFRACTION
AUTHOR E.S.BURGIE,C.A.BINGMAN,G.N.PHILLIPS JR.,CENTER FOR EUKARYOTIC
AUTHOR 2 STRUCTURAL GENOMICS (CESG)
REVDAT 8 26-JUL-23 3IHR 1 JRNL
REVDAT 7 13-OCT-21 3IHR 1 REMARK SEQADV LINK
REVDAT 6 01-NOV-17 3IHR 1 REMARK
REVDAT 5 19-JUN-13 3IHR 1 JRNL
REVDAT 4 23-JAN-13 3IHR 1 JRNL
REVDAT 3 09-JAN-13 3IHR 1 JRNL
REVDAT 2 10-OCT-12 3IHR 1 JRNL VERSN
REVDAT 1 11-AUG-09 3IHR 0
JRNL AUTH S.E.BURGIE,C.A.BINGMAN,A.B.SONI,G.N.PHILLIPS JR.
JRNL TITL STRUCTURAL CHARACTERIZATION OF HUMAN UCH37.
JRNL REF PROTEINS V. 80 649 2012
JRNL REFN ESSN 1097-0134
JRNL PMID 21953935
JRNL DOI 10.1002/PROT.23147
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.56
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 3 NUMBER OF REFLECTIONS : 13796
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 682
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 45.5650 - 5.0430 1.00 2947 143 0.2190 0.2500
REMARK 3 2 5.0430 - 4.0030 1.00 2837 137 0.1540 0.2130
REMARK 3 3 4.0030 - 3.4970 1.00 2796 134 0.1770 0.1990
REMARK 3 4 3.4970 - 3.1780 0.93 2575 141 0.2150 0.2670
REMARK 3 5 3.1780 - 2.9500 0.71 1959 127 0.2480 0.2780
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 68.34
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.000
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 107.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -16.61100
REMARK 3 B22 (A**2) : -14.27900
REMARK 3 B33 (A**2) : 26.32900
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 2331
REMARK 3 ANGLE : 1.092 3141
REMARK 3 CHIRALITY : 0.067 344
REMARK 3 PLANARITY : 0.004 409
REMARK 3 DIHEDRAL : 17.634 874
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 7:56)
REMARK 3 ORIGIN FOR THE GROUP (A): 82.3178 88.5944 35.0592
REMARK 3 T TENSOR
REMARK 3 T11: 0.7121 T22: 0.4488
REMARK 3 T33: 0.6875 T12: 0.0051
REMARK 3 T13: 0.0191 T23: 0.0338
REMARK 3 L TENSOR
REMARK 3 L11: 1.7883 L22: 1.1860
REMARK 3 L33: 2.3298 L12: 2.0547
REMARK 3 L13: 0.5806 L23: -0.5771
REMARK 3 S TENSOR
REMARK 3 S11: -0.6939 S12: 0.2496 S13: 0.2490
REMARK 3 S21: -0.5229 S22: 0.5125 S23: -0.1195
REMARK 3 S31: -0.6224 S32: 0.3153 S33: 0.2284
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 57:65)
REMARK 3 ORIGIN FOR THE GROUP (A): 94.9038 70.2357 34.4067
REMARK 3 T TENSOR
REMARK 3 T11: 1.1326 T22: 1.4816
REMARK 3 T33: 1.6309 T12: 0.0701
REMARK 3 T13: -0.0053 T23: -0.1505
REMARK 3 L TENSOR
REMARK 3 L11: 3.9588 L22: 2.3802
REMARK 3 L33: 6.2208 L12: -1.6068
REMARK 3 L13: 7.9351 L23: 0.0442
REMARK 3 S TENSOR
REMARK 3 S11: 2.6093 S12: -1.3310 S13: 1.2359
REMARK 3 S21: 0.0851 S22: 1.2132 S23: -2.2198
REMARK 3 S31: 1.5497 S32: 0.0178 S33: -3.9575
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 66:163)
REMARK 3 ORIGIN FOR THE GROUP (A): 73.6033 75.9128 31.4822
REMARK 3 T TENSOR
REMARK 3 T11: 0.6674 T22: 0.5093
REMARK 3 T33: 0.8691 T12: -0.0217
REMARK 3 T13: 0.0506 T23: 0.0441
REMARK 3 L TENSOR
REMARK 3 L11: 2.9147 L22: 2.5999
REMARK 3 L33: 4.5624 L12: 2.4722
REMARK 3 L13: -1.6635 L23: 1.4648
REMARK 3 S TENSOR
REMARK 3 S11: -0.4990 S12: 0.1507 S13: -0.6310
REMARK 3 S21: -0.1434 S22: 0.2680 S23: 0.5074
REMARK 3 S31: 0.6608 S32: -0.2054 S33: 0.2198
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 164:216)
REMARK 3 ORIGIN FOR THE GROUP (A): 86.5870 77.3443 43.3157
REMARK 3 T TENSOR
REMARK 3 T11: 0.7211 T22: 0.6220
REMARK 3 T33: 0.7618 T12: 0.0919
REMARK 3 T13: -0.0207 T23: 0.0577
REMARK 3 L TENSOR
REMARK 3 L11: 5.0393 L22: 5.7594
REMARK 3 L33: 1.6106 L12: 2.3673
REMARK 3 L13: 3.1857 L23: -0.5410
REMARK 3 S TENSOR
REMARK 3 S11: 0.0389 S12: -0.1860 S13: -1.0785
REMARK 3 S21: 0.7222 S22: -0.3258 S23: -0.5724
REMARK 3 S31: 0.3164 S32: -0.0464 S33: 0.2451
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 217:284)
REMARK 3 ORIGIN FOR THE GROUP (A): 78.1351 104.8118 42.3369
REMARK 3 T TENSOR
REMARK 3 T11: 0.4267 T22: 0.2971
REMARK 3 T33: 0.7031 T12: 0.0488
REMARK 3 T13: -0.0340 T23: 0.1315
REMARK 3 L TENSOR
REMARK 3 L11: 1.5159 L22: 2.5912
REMARK 3 L33: 1.9874 L12: -2.0645
REMARK 3 L13: -0.4583 L23: 2.2745
REMARK 3 S TENSOR
REMARK 3 S11: -0.2026 S12: 0.1313 S13: -0.5199
REMARK 3 S21: -0.4262 S22: -0.0332 S23: 0.2330
REMARK 3 S31: -0.3663 S32: -0.2436 S33: 0.1737
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 285:302)
REMARK 3 ORIGIN FOR THE GROUP (A): 91.9406 94.3099 7.2298
REMARK 3 T TENSOR
REMARK 3 T11: 1.8681 T22: 1.2575
REMARK 3 T33: 0.6433 T12: 0.4128
REMARK 3 T13: -0.1732 T23: 0.0539
REMARK 3 L TENSOR
REMARK 3 L11: 1.2854 L22: 3.6024
REMARK 3 L33: 7.3023 L12: -1.0548
REMARK 3 L13: -8.4898 L23: 2.1726
REMARK 3 S TENSOR
REMARK 3 S11: -0.3666 S12: -1.9274 S13: 0.5806
REMARK 3 S21: 1.5058 S22: 1.2902 S23: 0.6195
REMARK 3 S31: 1.2685 S32: 2.6499 S33: -0.7093
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 303:311)
REMARK 3 ORIGIN FOR THE GROUP (A): 104.6450 96.9035 -6.9620
REMARK 3 T TENSOR
REMARK 3 T11: 1.1739 T22: 2.5179
REMARK 3 T33: 0.6795 T12: 0.4765
REMARK 3 T13: 0.0125 T23: -0.2390
REMARK 3 L TENSOR
REMARK 3 L11: 8.0942 L22: 5.0016
REMARK 3 L33: -2.5461 L12: 1.4977
REMARK 3 L13: -3.7673 L23: -1.3714
REMARK 3 S TENSOR
REMARK 3 S11: 1.5581 S12: 1.4668 S13: 0.0368
REMARK 3 S21: -1.6392 S22: -2.0605 S23: -0.1713
REMARK 3 S31: 1.9378 S32: 3.6264 S33: 0.5745
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: TLS REFINEMENT WAS INCLUDED
REMARK 4
REMARK 4 3IHR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000054426.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949, 0.97973
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15698
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.1
REMARK 200 DATA REDUNDANCY : 11.40
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 52.7
REMARK 200 DATA REDUNDANCY IN SHELL : 8.70
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP, DM 5.0
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TOTAL VOLUME 4 UL; 5 MG/ML UCH37, 1.3
REMARK 280 M SODIUM FORMATE, 100 MM TRIS, 2.5 MM BISTRIS, 0.15 MM TCEP, PH
REMARK 280 8.5, HANGING DROP, BATCH, TEMPERATURE 277K, VAPOR DIFFUSION,
REMARK 280 HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 45.04600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.36800
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 77.03050
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.04600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.36800
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 77.03050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.04600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.36800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 77.03050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.04600
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 49.36800
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 77.03050
REMARK 290
REMARK 290 REMARK: NULL
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 300 REMARK: BIOLOGICAL UNIT IS A TETRAMER GENERATED FROM THE MONOMER IN
REMARK 300 THE ASYMMETRIC UNIT BY THE OPERATIONS 1; 2 X,0,0; 2 0,Y,0; 2 0,0,Z
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 55120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 180.18400
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 197.47200
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 180.18400
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 197.47200
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 1
REMARK 465 THR A 2
REMARK 465 GLY A 3
REMARK 465 ASN A 4
REMARK 465 ALA A 5
REMARK 465 GLY A 6
REMARK 465 ARG A 145
REMARK 465 GLN A 146
REMARK 465 GLN A 147
REMARK 465 MSE A 148
REMARK 465 PHE A 149
REMARK 465 GLU A 150
REMARK 465 PHE A 151
REMARK 465 ASP A 152
REMARK 465 THR A 153
REMARK 465 LYS A 154
REMARK 465 THR A 155
REMARK 465 SER A 156
REMARK 465 ALA A 157
REMARK 465 LYS A 158
REMARK 465 GLU A 159
REMARK 465 GLU A 160
REMARK 465 ASP A 161
REMARK 465 THR A 249
REMARK 465 ASP A 250
REMARK 465 GLN A 251
REMARK 465 GLY A 252
REMARK 465 ASN A 253
REMARK 465 SER A 254
REMARK 465 VAL A 312
REMARK 465 GLU A 313
REMARK 465 LYS A 314
REMARK 465 ALA A 315
REMARK 465 LYS A 316
REMARK 465 GLU A 317
REMARK 465 LYS A 318
REMARK 465 GLN A 319
REMARK 465 ASN A 320
REMARK 465 ALA A 321
REMARK 465 LYS A 322
REMARK 465 LYS A 323
REMARK 465 ALA A 324
REMARK 465 GLN A 325
REMARK 465 GLU A 326
REMARK 465 THR A 327
REMARK 465 LYS A 328
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 O TYR A 211 N GLU A 215 2.10
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 PHE A 56 -176.81 175.01
REMARK 500 PRO A 64 170.87 -49.99
REMARK 500 ALA A 65 8.41 -153.10
REMARK 500 VAL A 68 160.72 -48.89
REMARK 500 ASP A 71 -176.44 -62.20
REMARK 500 SER A 142 13.83 -69.80
REMARK 500 ARG A 182 -167.87 -117.95
REMARK 500 ASP A 195 86.40 -162.22
REMARK 500 SER A 212 -39.76 -31.04
REMARK 500 HIS A 289 56.56 -147.58
REMARK 500 GLU A 297 -3.26 -57.83
REMARK 500 LEU A 298 -64.47 -90.63
REMARK 500 THR A 301 44.61 -87.09
REMARK 500 LEU A 302 -4.23 -144.77
REMARK 500 HIS A 305 -76.98 -133.35
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 NA A 331 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 75 O
REMARK 620 2 GLN A 119 O 170.4
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 329
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 330
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 331
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: GO.41296 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE PROTEIN SEQUENCE MATCHES UNP ENTRY Q9Y5K5 ISOFORM 3 Q9Y5K5-3,
REMARK 999 AND DOES NOT MATCH THE ISOFORM 1.
DBREF 3IHR A 1 328 UNP Q9Y5K5 UCHL5_HUMAN 1 328
SEQADV 3IHR SER A 1 UNP Q9Y5K5 MET 1 ENGINEERED MUTATION
SEQRES 1 A 328 SER THR GLY ASN ALA GLY GLU TRP CYS LEU MSE GLU SER
SEQRES 2 A 328 ASP PRO GLY VAL PHE THR GLU LEU ILE LYS GLY PHE GLY
SEQRES 3 A 328 CYS ARG GLY ALA GLN VAL GLU GLU ILE TRP SER LEU GLU
SEQRES 4 A 328 PRO GLU ASN PHE GLU LYS LEU LYS PRO VAL HIS GLY LEU
SEQRES 5 A 328 ILE PHE LEU PHE LYS TRP GLN PRO GLY GLU GLU PRO ALA
SEQRES 6 A 328 GLY SER VAL VAL GLN ASP SER ARG LEU ASP THR ILE PHE
SEQRES 7 A 328 PHE ALA LYS GLN VAL ILE ASN ASN ALA CYS ALA THR GLN
SEQRES 8 A 328 ALA ILE VAL SER VAL LEU LEU ASN CYS THR HIS GLN ASP
SEQRES 9 A 328 VAL HIS LEU GLY GLU THR LEU SER GLU PHE LYS GLU PHE
SEQRES 10 A 328 SER GLN SER PHE ASP ALA ALA MSE LYS GLY LEU ALA LEU
SEQRES 11 A 328 SER ASN SER ASP VAL ILE ARG GLN VAL HIS ASN SER PHE
SEQRES 12 A 328 ALA ARG GLN GLN MSE PHE GLU PHE ASP THR LYS THR SER
SEQRES 13 A 328 ALA LYS GLU GLU ASP ALA PHE HIS PHE VAL SER TYR VAL
SEQRES 14 A 328 PRO VAL ASN GLY ARG LEU TYR GLU LEU ASP GLY LEU ARG
SEQRES 15 A 328 GLU GLY PRO ILE ASP LEU GLY ALA CYS ASN GLN ASP ASP
SEQRES 16 A 328 TRP ILE SER ALA VAL ARG PRO VAL ILE GLU LYS ARG ILE
SEQRES 17 A 328 GLN LYS TYR SER GLU GLY GLU ILE ARG PHE ASN LEU MSE
SEQRES 18 A 328 ALA ILE VAL SER ASP ARG LYS MSE ILE TYR GLU GLN LYS
SEQRES 19 A 328 ILE ALA GLU LEU GLN ARG GLN LEU ALA GLU GLU PRO MSE
SEQRES 20 A 328 ASP THR ASP GLN GLY ASN SER MSE LEU SER ALA ILE GLN
SEQRES 21 A 328 SER GLU VAL ALA LYS ASN GLN MSE LEU ILE GLU GLU GLU
SEQRES 22 A 328 VAL GLN LYS LEU LYS ARG TYR LYS ILE GLU ASN ILE ARG
SEQRES 23 A 328 ARG LYS HIS ASN TYR LEU PRO PHE ILE MSE GLU LEU LEU
SEQRES 24 A 328 LYS THR LEU ALA GLU HIS GLN GLN LEU ILE PRO LEU VAL
SEQRES 25 A 328 GLU LYS ALA LYS GLU LYS GLN ASN ALA LYS LYS ALA GLN
SEQRES 26 A 328 GLU THR LYS
MODRES 3IHR MSE A 11 MET SELENOMETHIONINE
MODRES 3IHR MSE A 125 MET SELENOMETHIONINE
MODRES 3IHR MSE A 221 MET SELENOMETHIONINE
MODRES 3IHR MSE A 229 MET SELENOMETHIONINE
MODRES 3IHR MSE A 247 MET SELENOMETHIONINE
MODRES 3IHR MSE A 255 MET SELENOMETHIONINE
MODRES 3IHR MSE A 268 MET SELENOMETHIONINE
MODRES 3IHR MSE A 296 MET SELENOMETHIONINE
HET MSE A 11 8
HET MSE A 125 8
HET MSE A 221 8
HET MSE A 229 8
HET MSE A 247 8
HET MSE A 255 8
HET MSE A 268 8
HET MSE A 296 8
HET FMT A 329 3
HET FMT A 330 3
HET NA A 331 1
HETNAM MSE SELENOMETHIONINE
HETNAM FMT FORMIC ACID
HETNAM NA SODIUM ION
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 2 FMT 2(C H2 O2)
FORMUL 4 NA NA 1+
FORMUL 5 HOH *10(H2 O)
HELIX 1 1 ASP A 14 GLY A 26 1 13
HELIX 2 2 GLU A 39 LYS A 45 1 7
HELIX 3 3 ILE A 84 ASN A 86 5 3
HELIX 4 4 ALA A 87 ASN A 99 1 13
HELIX 5 5 LEU A 107 GLN A 119 1 13
HELIX 6 6 ASP A 122 ASN A 132 1 11
HELIX 7 7 SER A 133 SER A 142 1 10
HELIX 8 8 TRP A 196 GLU A 215 1 20
HELIX 9 9 ASP A 226 GLU A 245 1 20
HELIX 10 10 MSE A 255 LYS A 288 1 34
HELIX 11 11 TYR A 291 LYS A 300 1 10
HELIX 12 12 THR A 301 ALA A 303 5 3
SHEET 1 A 7 ALA A 30 GLU A 34 0
SHEET 2 A 7 PHE A 218 SER A 225 -1 O ALA A 222 N GLU A 33
SHEET 3 A 7 VAL A 49 LYS A 57 -1 N HIS A 50 O ILE A 223
SHEET 4 A 7 PHE A 163 VAL A 171 -1 O VAL A 166 N PHE A 54
SHEET 5 A 7 ARG A 174 LEU A 178 -1 O LEU A 178 N SER A 167
SHEET 6 A 7 ILE A 186 ALA A 190 -1 O LEU A 188 N LEU A 175
SHEET 7 A 7 SER A 67 VAL A 68 -1 N SER A 67 O ASP A 187
LINK C LEU A 10 N MSE A 11 1555 1555 1.33
LINK C MSE A 11 N GLU A 12 1555 1555 1.33
LINK C ALA A 124 N MSE A 125 1555 1555 1.33
LINK C MSE A 125 N LYS A 126 1555 1555 1.33
LINK C LEU A 220 N MSE A 221 1555 1555 1.33
LINK C MSE A 221 N ALA A 222 1555 1555 1.33
LINK C LYS A 228 N MSE A 229 1555 1555 1.32
LINK C MSE A 229 N ILE A 230 1555 1555 1.32
LINK C PRO A 246 N MSE A 247 1555 1555 1.33
LINK C MSE A 247 N ASP A 248 1555 1555 1.33
LINK C MSE A 255 N LEU A 256 1555 1555 1.33
LINK C GLN A 267 N MSE A 268 1555 1555 1.33
LINK C MSE A 268 N LEU A 269 1555 1555 1.33
LINK C ILE A 295 N MSE A 296 1555 1555 1.33
LINK C MSE A 296 N GLU A 297 1555 1555 1.33
LINK O ASP A 75 NA NA A 331 1555 1555 2.00
LINK O GLN A 119 NA NA A 331 1555 1555 2.32
CISPEP 1 LYS A 47 PRO A 48 0 0.42
CISPEP 2 PRO A 64 ALA A 65 0 -3.45
SITE 1 AC1 2 ALA A 80 SER A 95
SITE 1 AC2 5 TRP A 36 SER A 37 LEU A 38 LYS A 265
SITE 2 AC2 5 MSE A 268
SITE 1 AC3 2 ASP A 75 GLN A 119
CRYST1 90.092 98.736 154.061 90.00 90.00 90.00 I 2 2 2 8
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 0.011100 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010128 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006491 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
