HEADER HYDROLASE 07-OCT-18 6IIN
TITLE USP14 CATALYTIC DOMAIN WITH IU1-248
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: DEUBIQUITINATING ENZYME 14,UBIQUITIN THIOESTERASE 14,
COMPND 6 UBIQUITIN-SPECIFIC-PROCESSING PROTEASE 14;
COMPND 7 EC: 3.4.19.12;
COMPND 8 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: USP14, TGT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS USP14 INHIBITOR COMPLEX, STRUCTURAL PROTEIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.Q.MEI,J.W.WANG,F.WANG,Y.W.WANG
REVDAT 2 27-MAR-24 6IIN 1 REMARK
REVDAT 1 19-DEC-18 6IIN 0
JRNL AUTH Y.WANG,Y.JIANG,S.DING,J.LI,N.SONG,Y.REN,D.HONG,C.WU,B.LI,
JRNL AUTH 2 F.WANG,W.HE,J.WANG,Z.MEI
JRNL TITL SMALL MOLECULE INHIBITORS REVEAL ALLOSTERIC REGULATION OF
JRNL TITL 2 USP14 VIA STERIC BLOCKADE.
JRNL REF CELL RES. V. 28 1186 2018
JRNL REFN ISSN 1748-7838
JRNL PMID 30254335
JRNL DOI 10.1038/S41422-018-0091-X
REMARK 2
REMARK 2 RESOLUTION. 2.53 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8_1069
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.53
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.25
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 33924
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1713
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 38.0875 - 5.7766 0.97 2842 137 0.1947 0.2178
REMARK 3 2 5.7766 - 4.5875 0.99 2754 153 0.1861 0.2096
REMARK 3 3 4.5875 - 4.0084 0.98 2718 143 0.1786 0.2451
REMARK 3 4 4.0084 - 3.6422 0.99 2727 127 0.1975 0.2777
REMARK 3 5 3.6422 - 3.3813 0.98 2659 161 0.2151 0.2579
REMARK 3 6 3.3813 - 3.1820 0.99 2716 130 0.2313 0.3244
REMARK 3 7 3.1820 - 3.0228 0.99 2686 130 0.2411 0.3028
REMARK 3 8 3.0228 - 2.8912 0.99 2675 157 0.2357 0.3042
REMARK 3 9 2.8912 - 2.7800 0.99 2661 166 0.2387 0.2876
REMARK 3 10 2.7800 - 2.6841 1.00 2705 135 0.2746 0.3589
REMARK 3 11 2.6841 - 2.6001 0.99 2683 143 0.2741 0.3491
REMARK 3 12 2.6001 - 2.5258 0.89 2385 131 0.2955 0.3483
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.590
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.003 5543
REMARK 3 ANGLE : 0.886 7467
REMARK 3 CHIRALITY : 0.055 814
REMARK 3 PLANARITY : 0.003 953
REMARK 3 DIHEDRAL : 14.450 2096
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8793 -1.6952 -0.5431
REMARK 3 T TENSOR
REMARK 3 T11: 0.2601 T22: 0.3526
REMARK 3 T33: 0.2173 T12: -0.0145
REMARK 3 T13: 0.0018 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 3.3401 L22: 1.2227
REMARK 3 L33: 1.8394 L12: -0.2707
REMARK 3 L13: 0.1863 L23: -0.1595
REMARK 3 S TENSOR
REMARK 3 S11: -0.0627 S12: 0.3390 S13: 0.1260
REMARK 3 S21: -0.1858 S22: 0.0183 S23: 0.0458
REMARK 3 S31: 0.0732 S32: -0.0654 S33: 0.0471
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -19.8815 -3.3441 -35.5590
REMARK 3 T TENSOR
REMARK 3 T11: 0.3034 T22: 0.5832
REMARK 3 T33: 0.3154 T12: -0.0314
REMARK 3 T13: -0.0120 T23: 0.1222
REMARK 3 L TENSOR
REMARK 3 L11: 4.6379 L22: 1.3048
REMARK 3 L33: 2.4490 L12: -0.3563
REMARK 3 L13: 0.0796 L23: 0.2069
REMARK 3 S TENSOR
REMARK 3 S11: -0.1231 S12: -0.7019 S13: -0.4026
REMARK 3 S21: 0.1977 S22: 0.1094 S23: 0.0641
REMARK 3 S31: 0.1530 S32: -0.1861 S33: 0.0287
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6IIN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1300009270.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.984
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33924
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.530
REMARK 200 RESOLUTION RANGE LOW (A) : 36.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.9300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.53
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, NH4F, CSCL, GLYCINE, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 40.90450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.13550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.17550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.13550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.90450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.17550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 ASP A 220
REMARK 465 ASP A 221
REMARK 465 SER A 222
REMARK 465 VAL A 223
REMARK 465 LYS A 224
REMARK 465 GLU A 225
REMARK 465 THR A 226
REMARK 465 ASP A 227
REMARK 465 SER A 228
REMARK 465 SER A 229
REMARK 465 SER A 230
REMARK 465 ALA A 231
REMARK 465 SER A 232
REMARK 465 ALA A 233
REMARK 465 ALA A 234
REMARK 465 THR A 235
REMARK 465 PRO A 236
REMARK 465 SER A 237
REMARK 465 LYS A 238
REMARK 465 LYS A 239
REMARK 465 LYS A 334
REMARK 465 GLU A 335
REMARK 465 LYS A 336
REMARK 465 GLU A 337
REMARK 465 SER A 338
REMARK 465 VAL A 339
REMARK 465 GLU A 378
REMARK 465 ASP A 379
REMARK 465 LYS A 380
REMARK 465 LYS A 381
REMARK 465 VAL A 382
REMARK 465 ASN A 383
REMARK 465 GLN A 384
REMARK 465 GLN A 385
REMARK 465 PRO A 386
REMARK 465 ASN A 387
REMARK 465 THR A 388
REMARK 465 SER A 389
REMARK 465 ASP A 390
REMARK 465 LYS A 391
REMARK 465 LYS A 392
REMARK 465 SER A 393
REMARK 465 SER A 394
REMARK 465 PRO A 395
REMARK 465 GLN A 396
REMARK 465 LYS A 397
REMARK 465 GLU A 398
REMARK 465 VAL A 399
REMARK 465 LYS A 400
REMARK 465 ASP B 220
REMARK 465 ASP B 221
REMARK 465 SER B 222
REMARK 465 VAL B 223
REMARK 465 LYS B 224
REMARK 465 GLU B 225
REMARK 465 THR B 226
REMARK 465 ASP B 227
REMARK 465 SER B 228
REMARK 465 SER B 229
REMARK 465 SER B 230
REMARK 465 ALA B 231
REMARK 465 SER B 232
REMARK 465 ALA B 233
REMARK 465 ALA B 234
REMARK 465 THR B 235
REMARK 465 PRO B 236
REMARK 465 SER B 237
REMARK 465 LYS B 238
REMARK 465 LYS B 239
REMARK 465 LYS B 334
REMARK 465 GLU B 335
REMARK 465 LYS B 336
REMARK 465 GLU B 337
REMARK 465 SER B 338
REMARK 465 VAL B 339
REMARK 465 GLU B 378
REMARK 465 ASP B 379
REMARK 465 LYS B 380
REMARK 465 LYS B 381
REMARK 465 VAL B 382
REMARK 465 ASN B 383
REMARK 465 GLN B 384
REMARK 465 GLN B 385
REMARK 465 PRO B 386
REMARK 465 ASN B 387
REMARK 465 THR B 388
REMARK 465 SER B 389
REMARK 465 ASP B 390
REMARK 465 LYS B 391
REMARK 465 LYS B 392
REMARK 465 SER B 393
REMARK 465 SER B 394
REMARK 465 PRO B 395
REMARK 465 GLN B 396
REMARK 465 LYS B 397
REMARK 465 GLU B 398
REMARK 465 VAL B 399
REMARK 465 LYS B 400
REMARK 465 TYR B 401
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 MET A 101 CG SD CE
REMARK 470 TYR A 333 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN A 340 CG OD1 ND2
REMARK 470 MET B 101 CG SD CE
REMARK 470 PHE B 332 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL B 485 CG1 CG2
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 OD2 ASP A 354 O HOH A 601 1.92
REMARK 500 OG SER A 276 O HOH A 602 2.05
REMARK 500 O HOH A 630 O HOH A 636 2.10
REMARK 500 OG SER B 456 O HOH B 601 2.10
REMARK 500 O HOH A 635 O HOH A 657 2.14
REMARK 500 OD1 ASP A 161 O HOH A 603 2.18
REMARK 500 O PRO B 321 OH TYR B 418 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 631 O HOH B 635 2455 2.16
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 GLU A 145 -72.00 -66.16
REMARK 500 SER A 168 -100.14 -101.01
REMARK 500 ARG A 330 59.32 -99.05
REMARK 500 GLU A 402 116.32 65.65
REMARK 500 ASP A 452 -113.42 55.34
REMARK 500 ALA B 139 130.88 -172.02
REMARK 500 SER B 168 -93.66 -96.61
REMARK 500 SER B 260 108.71 -166.09
REMARK 500 GLU B 282 -2.56 70.27
REMARK 500 LYS B 300 -86.10 -154.02
REMARK 500 ARG B 307 -155.52 -164.78
REMARK 500 SER B 433 -158.36 -155.46
REMARK 500 ASP B 451 74.76 -103.00
REMARK 500 ASP B 452 -113.40 56.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue A8O A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue A8O B 501
DBREF 6IIN A 101 485 UNP P54578 UBP14_HUMAN 101 485
DBREF 6IIN B 101 485 UNP P54578 UBP14_HUMAN 101 485
SEQRES 1 A 385 MET GLU LEU PRO CYS GLY LEU THR ASN LEU GLY ASN THR
SEQRES 2 A 385 CYS TYR MET ASN ALA THR VAL GLN CYS ILE ARG SER VAL
SEQRES 3 A 385 PRO GLU LEU LYS ASP ALA LEU LYS ARG TYR ALA GLY ALA
SEQRES 4 A 385 LEU ARG ALA SER GLY GLU MET ALA SER ALA GLN TYR ILE
SEQRES 5 A 385 THR ALA ALA LEU ARG ASP LEU PHE ASP SER MET ASP LYS
SEQRES 6 A 385 THR SER SER SER ILE PRO PRO ILE ILE LEU LEU GLN PHE
SEQRES 7 A 385 LEU HIS MET ALA PHE PRO GLN PHE ALA GLU LYS GLY GLU
SEQRES 8 A 385 GLN GLY GLN TYR LEU GLN GLN ASP ALA ASN GLU CYS TRP
SEQRES 9 A 385 ILE GLN MET MET ARG VAL LEU GLN GLN LYS LEU GLU ALA
SEQRES 10 A 385 ILE GLU ASP ASP SER VAL LYS GLU THR ASP SER SER SER
SEQRES 11 A 385 ALA SER ALA ALA THR PRO SER LYS LYS LYS SER LEU ILE
SEQRES 12 A 385 ASP GLN PHE PHE GLY VAL GLU PHE GLU THR THR MET LYS
SEQRES 13 A 385 CYS THR GLU SER GLU GLU GLU GLU VAL THR LYS GLY LYS
SEQRES 14 A 385 GLU ASN GLN LEU GLN LEU SER CYS PHE ILE ASN GLN GLU
SEQRES 15 A 385 VAL LYS TYR LEU PHE THR GLY LEU LYS LEU ARG LEU GLN
SEQRES 16 A 385 GLU GLU ILE THR LYS GLN SER PRO THR LEU GLN ARG ASN
SEQRES 17 A 385 ALA LEU TYR ILE LYS SER SER LYS ILE SER ARG LEU PRO
SEQRES 18 A 385 ALA TYR LEU THR ILE GLN MET VAL ARG PHE PHE TYR LYS
SEQRES 19 A 385 GLU LYS GLU SER VAL ASN ALA LYS VAL LEU LYS ASP VAL
SEQRES 20 A 385 LYS PHE PRO LEU MET LEU ASP MET TYR GLU LEU CYS THR
SEQRES 21 A 385 PRO GLU LEU GLN GLU LYS MET VAL SER PHE ARG SER LYS
SEQRES 22 A 385 PHE LYS ASP LEU GLU ASP LYS LYS VAL ASN GLN GLN PRO
SEQRES 23 A 385 ASN THR SER ASP LYS LYS SER SER PRO GLN LYS GLU VAL
SEQRES 24 A 385 LYS TYR GLU PRO PHE SER PHE ALA ASP ASP ILE GLY SER
SEQRES 25 A 385 ASN ASN CYS GLY TYR TYR ASP LEU GLN ALA VAL LEU THR
SEQRES 26 A 385 HIS GLN GLY ARG SER SER SER SER GLY HIS TYR VAL SER
SEQRES 27 A 385 TRP VAL LYS ARG LYS GLN ASP GLU TRP ILE LYS PHE ASP
SEQRES 28 A 385 ASP ASP LYS VAL SER ILE VAL THR PRO GLU ASP ILE LEU
SEQRES 29 A 385 ARG LEU SER GLY GLY GLY ASP TRP HIS ILE ALA TYR VAL
SEQRES 30 A 385 LEU LEU TYR GLY PRO ARG ARG VAL
SEQRES 1 B 385 MET GLU LEU PRO CYS GLY LEU THR ASN LEU GLY ASN THR
SEQRES 2 B 385 CYS TYR MET ASN ALA THR VAL GLN CYS ILE ARG SER VAL
SEQRES 3 B 385 PRO GLU LEU LYS ASP ALA LEU LYS ARG TYR ALA GLY ALA
SEQRES 4 B 385 LEU ARG ALA SER GLY GLU MET ALA SER ALA GLN TYR ILE
SEQRES 5 B 385 THR ALA ALA LEU ARG ASP LEU PHE ASP SER MET ASP LYS
SEQRES 6 B 385 THR SER SER SER ILE PRO PRO ILE ILE LEU LEU GLN PHE
SEQRES 7 B 385 LEU HIS MET ALA PHE PRO GLN PHE ALA GLU LYS GLY GLU
SEQRES 8 B 385 GLN GLY GLN TYR LEU GLN GLN ASP ALA ASN GLU CYS TRP
SEQRES 9 B 385 ILE GLN MET MET ARG VAL LEU GLN GLN LYS LEU GLU ALA
SEQRES 10 B 385 ILE GLU ASP ASP SER VAL LYS GLU THR ASP SER SER SER
SEQRES 11 B 385 ALA SER ALA ALA THR PRO SER LYS LYS LYS SER LEU ILE
SEQRES 12 B 385 ASP GLN PHE PHE GLY VAL GLU PHE GLU THR THR MET LYS
SEQRES 13 B 385 CYS THR GLU SER GLU GLU GLU GLU VAL THR LYS GLY LYS
SEQRES 14 B 385 GLU ASN GLN LEU GLN LEU SER CYS PHE ILE ASN GLN GLU
SEQRES 15 B 385 VAL LYS TYR LEU PHE THR GLY LEU LYS LEU ARG LEU GLN
SEQRES 16 B 385 GLU GLU ILE THR LYS GLN SER PRO THR LEU GLN ARG ASN
SEQRES 17 B 385 ALA LEU TYR ILE LYS SER SER LYS ILE SER ARG LEU PRO
SEQRES 18 B 385 ALA TYR LEU THR ILE GLN MET VAL ARG PHE PHE TYR LYS
SEQRES 19 B 385 GLU LYS GLU SER VAL ASN ALA LYS VAL LEU LYS ASP VAL
SEQRES 20 B 385 LYS PHE PRO LEU MET LEU ASP MET TYR GLU LEU CYS THR
SEQRES 21 B 385 PRO GLU LEU GLN GLU LYS MET VAL SER PHE ARG SER LYS
SEQRES 22 B 385 PHE LYS ASP LEU GLU ASP LYS LYS VAL ASN GLN GLN PRO
SEQRES 23 B 385 ASN THR SER ASP LYS LYS SER SER PRO GLN LYS GLU VAL
SEQRES 24 B 385 LYS TYR GLU PRO PHE SER PHE ALA ASP ASP ILE GLY SER
SEQRES 25 B 385 ASN ASN CYS GLY TYR TYR ASP LEU GLN ALA VAL LEU THR
SEQRES 26 B 385 HIS GLN GLY ARG SER SER SER SER GLY HIS TYR VAL SER
SEQRES 27 B 385 TRP VAL LYS ARG LYS GLN ASP GLU TRP ILE LYS PHE ASP
SEQRES 28 B 385 ASP ASP LYS VAL SER ILE VAL THR PRO GLU ASP ILE LEU
SEQRES 29 B 385 ARG LEU SER GLY GLY GLY ASP TRP HIS ILE ALA TYR VAL
SEQRES 30 B 385 LEU LEU TYR GLY PRO ARG ARG VAL
HET A8O A 501 25
HET A8O B 501 25
HETNAM A8O 4-{3-[(4-HYDROXYPIPERIDIN-1-YL)ACETYL]-2,5-DIMETHYL-1H-
HETNAM 2 A8O PYRROL-1-YL}BENZONITRILE
FORMUL 3 A8O 2(C20 H23 N3 O2)
FORMUL 5 HOH *104(H2 O)
HELIX 1 AA1 THR A 113 SER A 125 1 13
HELIX 2 AA2 VAL A 126 ARG A 135 1 10
HELIX 3 AA3 MET A 146 THR A 166 1 21
HELIX 4 AA4 PRO A 172 PHE A 183 1 12
HELIX 5 AA5 ASP A 199 LEU A 215 1 17
HELIX 6 AA6 SER A 241 GLY A 248 1 8
HELIX 7 AA7 TYR A 285 LEU A 294 1 10
HELIX 8 AA8 TYR A 356 CYS A 359 5 4
HELIX 9 AA9 THR A 360 SER A 372 1 13
HELIX 10 AB1 THR A 459 ARG A 465 1 7
HELIX 11 AB2 LEU A 466 GLY A 468 5 3
HELIX 12 AB3 THR B 113 SER B 125 1 13
HELIX 13 AB4 VAL B 126 TYR B 136 1 11
HELIX 14 AB5 MET B 146 THR B 166 1 21
HELIX 15 AB6 PRO B 172 PHE B 183 1 12
HELIX 16 AB7 PRO B 184 GLU B 188 5 5
HELIX 17 AB8 ASP B 199 LEU B 215 1 17
HELIX 18 AB9 SER B 241 GLY B 248 1 8
HELIX 19 AC1 TYR B 285 LEU B 294 1 10
HELIX 20 AC2 TYR B 356 CYS B 359 5 4
HELIX 21 AC3 THR B 360 LYS B 375 1 16
HELIX 22 AC4 THR B 459 ARG B 465 1 7
SHEET 1 AA1 2 GLY A 106 LEU A 107 0
SHEET 2 AA1 2 SER A 169 ILE A 170 1 O ILE A 170 N GLY A 106
SHEET 1 AA2 4 THR A 266 GLN A 272 0
SHEET 2 AA2 4 VAL A 249 CYS A 257 -1 N VAL A 249 O GLN A 272
SHEET 3 AA2 4 ARG A 307 ARG A 319 -1 O SER A 318 N GLU A 250
SHEET 4 AA2 4 GLN A 295 SER A 302 -1 N GLU A 296 O LYS A 313
SHEET 1 AA3 5 LEU A 275 PHE A 278 0
SHEET 2 AA3 5 LEU A 324 VAL A 329 1 O THR A 325 N LEU A 275
SHEET 3 AA3 5 ILE A 474 PRO A 482 -1 O TYR A 480 N LEU A 324
SHEET 4 AA3 5 TYR A 417 GLN A 427 -1 N ASP A 419 O GLY A 481
SHEET 5 AA3 5 MET A 352 ASP A 354 -1 N LEU A 353 O TYR A 418
SHEET 1 AA4 7 LEU A 275 PHE A 278 0
SHEET 2 AA4 7 LEU A 324 VAL A 329 1 O THR A 325 N LEU A 275
SHEET 3 AA4 7 ILE A 474 PRO A 482 -1 O TYR A 480 N LEU A 324
SHEET 4 AA4 7 TYR A 417 GLN A 427 -1 N ASP A 419 O GLY A 481
SHEET 5 AA4 7 HIS A 435 LYS A 443 -1 O HIS A 435 N GLN A 427
SHEET 6 AA4 7 GLU A 446 ASP A 451 -1 O PHE A 450 N SER A 438
SHEET 7 AA4 7 LYS A 454 VAL A 458 -1 O SER A 456 N LYS A 449
SHEET 1 AA5 2 GLY B 106 LEU B 107 0
SHEET 2 AA5 2 SER B 169 ILE B 170 1 O ILE B 170 N GLY B 106
SHEET 1 AA6 4 THR B 266 GLN B 272 0
SHEET 2 AA6 4 VAL B 249 CYS B 257 -1 N VAL B 249 O GLN B 272
SHEET 3 AA6 4 TYR B 311 ARG B 319 -1 O SER B 318 N GLU B 250
SHEET 4 AA6 4 GLN B 295 ILE B 298 -1 N GLU B 296 O LYS B 313
SHEET 1 AA7 5 LEU B 275 PHE B 278 0
SHEET 2 AA7 5 LEU B 324 VAL B 329 1 O THR B 325 N LEU B 275
SHEET 3 AA7 5 ILE B 474 PRO B 482 -1 O LEU B 478 N ILE B 326
SHEET 4 AA7 5 TYR B 417 GLN B 427 -1 N ASP B 419 O GLY B 481
SHEET 5 AA7 5 MET B 352 ASP B 354 -1 N LEU B 353 O TYR B 418
SHEET 1 AA8 7 LEU B 275 PHE B 278 0
SHEET 2 AA8 7 LEU B 324 VAL B 329 1 O THR B 325 N LEU B 275
SHEET 3 AA8 7 ILE B 474 PRO B 482 -1 O LEU B 478 N ILE B 326
SHEET 4 AA8 7 TYR B 417 GLN B 427 -1 N ASP B 419 O GLY B 481
SHEET 5 AA8 7 HIS B 435 LYS B 443 -1 O VAL B 437 N THR B 425
SHEET 6 AA8 7 GLU B 446 ASP B 451 -1 O GLU B 446 N ARG B 442
SHEET 7 AA8 7 LYS B 454 VAL B 458 -1 O VAL B 458 N TRP B 447
CISPEP 1 ALA B 137 GLY B 138 0 -5.68
CISPEP 2 PHE B 332 TYR B 333 0 0.44
SITE 1 AC1 10 GLN A 197 GLN A 198 ASP A 199 ARG A 330
SITE 2 AC1 10 PHE A 331 SER A 431 SER A 432 SER A 433
SITE 3 AC1 10 TYR A 436 TYR A 476
SITE 1 AC2 12 LEU B 196 GLN B 197 GLN B 198 ASP B 199
SITE 2 AC2 12 ARG B 330 LYS B 342 HIS B 426 SER B 431
SITE 3 AC2 12 SER B 432 SER B 433 TYR B 436 TYR B 476
CRYST1 81.809 104.351 118.271 90.00 90.00 90.00 P 21 21 21 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 0.012224 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009583 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008455 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
