HEADER HYDROLASE 06-APR-16 5J7T
TITLE MOLECULAR UNDERSTANDING OF USP7 SUBSTRATE RECOGNITION AND C-TERMINAL
TITLE 2 ACTIVATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: USP7;
COMPND 5 SYNONYM: DEUBIQUITINATING ENZYME 7,HERPESVIRUS-ASSOCIATED UBIQUITIN-
COMPND 6 SPECIFIC PROTEASE,UBIQUITIN THIOESTERASE 7,UBIQUITIN-SPECIFIC-
COMPND 7 PROCESSING PROTEASE 7;
COMPND 8 EC: 3.4.19.12;
COMPND 9 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: USP7, HAUSP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS USP7, HAUSP, DUB, ACTIVATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.MURRAY,L.ROUGE
REVDAT 2 27-SEP-23 5J7T 1 JRNL REMARK
REVDAT 1 10-AUG-16 5J7T 0
JRNL AUTH L.ROUGE,T.W.BAINBRIDGE,M.KWOK,R.TONG,P.DI LELLO,I.E.WERTZ,
JRNL AUTH 2 T.MAURER,J.A.ERNST,J.MURRAY
JRNL TITL MOLECULAR UNDERSTANDING OF USP7 SUBSTRATE RECOGNITION AND
JRNL TITL 2 C-TERMINAL ACTIVATION.
JRNL REF STRUCTURE V. 24 1335 2016
JRNL REFN ISSN 0969-2126
JRNL PMID 27452404
JRNL DOI 10.1016/J.STR.2016.05.020
REMARK 2
REMARK 2 RESOLUTION. 3.20 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 19201
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.252
REMARK 3 R VALUE (WORKING SET) : 0.250
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 971
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 47.3807 - 6.1179 0.96 2629 129 0.2003 0.2640
REMARK 3 2 6.1179 - 4.8575 1.00 2652 126 0.2361 0.2840
REMARK 3 3 4.8575 - 4.2439 1.00 2614 157 0.2358 0.2657
REMARK 3 4 4.2439 - 3.8561 1.00 2612 135 0.2665 0.3129
REMARK 3 5 3.8561 - 3.5798 0.99 2548 142 0.2874 0.2955
REMARK 3 6 3.5798 - 3.3688 0.99 2598 131 0.3435 0.3624
REMARK 3 7 3.3688 - 3.2001 1.00 2577 151 0.3617 0.3831
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) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.560
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 84.19
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 127.2
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 : 0.002 5559
REMARK 3 ANGLE : 0.579 7515
REMARK 3 CHIRALITY : 0.024 807
REMARK 3 PLANARITY : 0.003 992
REMARK 3 DIHEDRAL : 11.361 2118
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 211 THROUGH 243 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5946 16.0877 -30.2961
REMARK 3 T TENSOR
REMARK 3 T11: 0.6882 T22: 0.6255
REMARK 3 T33: 1.1056 T12: 0.0156
REMARK 3 T13: 0.1618 T23: 0.1941
REMARK 3 L TENSOR
REMARK 3 L11: 2.4908 L22: 6.9449
REMARK 3 L33: 9.5732 L12: -0.7234
REMARK 3 L13: 1.6282 L23: 2.4159
REMARK 3 S TENSOR
REMARK 3 S11: -0.6261 S12: 0.4868 S13: -0.3149
REMARK 3 S21: -0.1257 S22: 0.8486 S23: 0.1120
REMARK 3 S31: 0.0463 S32: -0.5635 S33: -0.2113
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 244 THROUGH 378 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.3797 15.6138 -16.2685
REMARK 3 T TENSOR
REMARK 3 T11: 0.9136 T22: 1.5167
REMARK 3 T33: 1.2926 T12: 0.2713
REMARK 3 T13: 0.0023 T23: 0.3296
REMARK 3 L TENSOR
REMARK 3 L11: 6.8600 L22: 2.6534
REMARK 3 L33: 8.2468 L12: -0.2074
REMARK 3 L13: -0.5813 L23: 2.3010
REMARK 3 S TENSOR
REMARK 3 S11: -0.5368 S12: -2.0467 S13: -1.1355
REMARK 3 S21: 0.8961 S22: 0.6087 S23: -0.5705
REMARK 3 S31: 1.0149 S32: 1.0558 S33: -0.1978
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 379 THROUGH 426 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.3847 20.3357 -2.6692
REMARK 3 T TENSOR
REMARK 3 T11: 1.2593 T22: 1.7795
REMARK 3 T33: 1.1635 T12: 0.3152
REMARK 3 T13: -0.0668 T23: 0.4142
REMARK 3 L TENSOR
REMARK 3 L11: 3.5018 L22: 2.2757
REMARK 3 L33: 5.8970 L12: 1.4086
REMARK 3 L13: -0.9601 L23: 3.1463
REMARK 3 S TENSOR
REMARK 3 S11: 0.3247 S12: -1.6341 S13: -1.0614
REMARK 3 S21: 1.0918 S22: 0.3335 S23: -0.4153
REMARK 3 S31: 1.0444 S32: 0.7349 S33: -0.6660
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 427 THROUGH 469 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.6731 28.3384 -17.1754
REMARK 3 T TENSOR
REMARK 3 T11: 0.8238 T22: 0.7674
REMARK 3 T33: 1.0062 T12: 0.0815
REMARK 3 T13: 0.1007 T23: 0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 2.7795 L22: 6.9241
REMARK 3 L33: 7.3509 L12: 1.8677
REMARK 3 L13: 1.3176 L23: 0.8024
REMARK 3 S TENSOR
REMARK 3 S11: -0.0338 S12: -0.8448 S13: -0.4497
REMARK 3 S21: 0.9158 S22: 0.5196 S23: -1.0136
REMARK 3 S31: -0.4602 S32: 0.0124 S33: -0.4044
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 470 THROUGH 510 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.3731 25.2232 -24.5053
REMARK 3 T TENSOR
REMARK 3 T11: 0.8475 T22: 1.0962
REMARK 3 T33: 0.8524 T12: 0.1205
REMARK 3 T13: 0.0781 T23: 0.1890
REMARK 3 L TENSOR
REMARK 3 L11: 8.8015 L22: 5.6519
REMARK 3 L33: 3.8627 L12: -4.1781
REMARK 3 L13: -1.3054 L23: 3.2203
REMARK 3 S TENSOR
REMARK 3 S11: -0.3711 S12: -0.1738 S13: -0.3912
REMARK 3 S21: 0.0941 S22: -0.2681 S23: 0.2454
REMARK 3 S31: -1.1067 S32: -1.1778 S33: 0.9074
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 511 THROUGH 561 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.6643 13.4525 -36.8305
REMARK 3 T TENSOR
REMARK 3 T11: 0.6631 T22: 0.9017
REMARK 3 T33: 1.2543 T12: -0.0101
REMARK 3 T13: 0.0210 T23: -0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 2.0863 L22: 6.1813
REMARK 3 L33: 8.7076 L12: -1.4637
REMARK 3 L13: -2.2640 L23: 3.0368
REMARK 3 S TENSOR
REMARK 3 S11: 0.1330 S12: 0.0435 S13: -0.9368
REMARK 3 S21: -0.6748 S22: -0.0005 S23: -0.6116
REMARK 3 S31: 0.1428 S32: 0.0130 S33: -0.4015
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 563 THROUGH 627 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.8688 -27.4341 -52.0505
REMARK 3 T TENSOR
REMARK 3 T11: 1.2382 T22: 1.1048
REMARK 3 T33: 1.0528 T12: -0.3930
REMARK 3 T13: -0.0424 T23: 0.0581
REMARK 3 L TENSOR
REMARK 3 L11: 6.4882 L22: 5.1151
REMARK 3 L33: 2.1674 L12: 0.4785
REMARK 3 L13: -0.1955 L23: -0.1939
REMARK 3 S TENSOR
REMARK 3 S11: -0.5954 S12: 1.1957 S13: 0.8046
REMARK 3 S21: -0.3822 S22: 0.4183 S23: -0.9095
REMARK 3 S31: -1.3409 S32: 1.0533 S33: 0.3791
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 628 THROUGH 647 )
REMARK 3 ORIGIN FOR THE GROUP (A): -57.8617 -22.6909 -51.6549
REMARK 3 T TENSOR
REMARK 3 T11: 1.3414 T22: 1.1014
REMARK 3 T33: 1.2556 T12: -0.2581
REMARK 3 T13: -0.5030 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 5.7499 L22: 7.1361
REMARK 3 L33: 0.6568 L12: 0.1115
REMARK 3 L13: 1.5812 L23: 0.1952
REMARK 3 S TENSOR
REMARK 3 S11: -0.6686 S12: 0.9997 S13: 1.4164
REMARK 3 S21: -0.4366 S22: 0.8681 S23: 0.6271
REMARK 3 S31: -0.5173 S32: 2.0214 S33: 0.3592
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 648 THROUGH 670 )
REMARK 3 ORIGIN FOR THE GROUP (A): -50.2910 -26.1915 -53.4820
REMARK 3 T TENSOR
REMARK 3 T11: 1.1660 T22: 1.5883
REMARK 3 T33: 1.1532 T12: -0.3152
REMARK 3 T13: -0.0928 T23: 0.0661
REMARK 3 L TENSOR
REMARK 3 L11: 4.5187 L22: 2.8147
REMARK 3 L33: 9.7672 L12: 2.4535
REMARK 3 L13: 3.1475 L23: -1.2661
REMARK 3 S TENSOR
REMARK 3 S11: -0.0052 S12: 1.4643 S13: 0.5901
REMARK 3 S21: 1.0395 S22: 0.0641 S23: -2.2173
REMARK 3 S31: -0.1814 S32: 1.0271 S33: 0.1501
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 671 THROUGH 770 )
REMARK 3 ORIGIN FOR THE GROUP (A): -64.8675 -41.8506 -47.9740
REMARK 3 T TENSOR
REMARK 3 T11: 0.9766 T22: 0.5248
REMARK 3 T33: 0.7009 T12: -0.0923
REMARK 3 T13: -0.0815 T23: -0.0994
REMARK 3 L TENSOR
REMARK 3 L11: 9.1363 L22: 4.7724
REMARK 3 L33: 7.7894 L12: -0.4113
REMARK 3 L13: 0.2648 L23: -0.9545
REMARK 3 S TENSOR
REMARK 3 S11: -0.4379 S12: 0.5008 S13: -0.3991
REMARK 3 S21: -0.6067 S22: 0.3976 S23: -0.0942
REMARK 3 S31: 0.0827 S32: -0.2955 S33: 0.0167
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 771 THROUGH 830 )
REMARK 3 ORIGIN FOR THE GROUP (A): -52.0691 -42.0791 -20.3857
REMARK 3 T TENSOR
REMARK 3 T11: 1.3421 T22: 1.2357
REMARK 3 T33: 0.9836 T12: 0.2571
REMARK 3 T13: -0.2641 T23: -0.0366
REMARK 3 L TENSOR
REMARK 3 L11: 1.7516 L22: 2.7138
REMARK 3 L33: 5.1267 L12: -0.0025
REMARK 3 L13: -1.2754 L23: 0.5106
REMARK 3 S TENSOR
REMARK 3 S11: 0.4058 S12: -0.5487 S13: -0.7715
REMARK 3 S21: 0.0376 S22: 0.2111 S23: -0.3670
REMARK 3 S31: 1.0284 S32: 1.4252 S33: -0.8026
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 831 THROUGH 850 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.2439 -31.6571 -8.0448
REMARK 3 T TENSOR
REMARK 3 T11: 1.2070 T22: 1.7880
REMARK 3 T33: 1.1699 T12: -0.2803
REMARK 3 T13: -0.4639 T23: 0.0668
REMARK 3 L TENSOR
REMARK 3 L11: 2.8292 L22: 2.2078
REMARK 3 L33: 7.8500 L12: 1.5484
REMARK 3 L13: -1.7419 L23: -3.0909
REMARK 3 S TENSOR
REMARK 3 S11: -0.0944 S12: 1.2769 S13: 0.4377
REMARK 3 S21: 0.8481 S22: 0.3719 S23: -0.5041
REMARK 3 S31: -0.0691 S32: 1.7928 S33: -0.1143
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 851 THROUGH 881 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.5252 -29.2958 -13.9768
REMARK 3 T TENSOR
REMARK 3 T11: 1.2040 T22: 1.7783
REMARK 3 T33: 0.8843 T12: 0.1540
REMARK 3 T13: -0.2982 T23: -0.0345
REMARK 3 L TENSOR
REMARK 3 L11: 6.4960 L22: 4.8357
REMARK 3 L33: 2.1500 L12: 1.1533
REMARK 3 L13: -2.3020 L23: 0.6988
REMARK 3 S TENSOR
REMARK 3 S11: 0.0564 S12: 0.7279 S13: 0.3415
REMARK 3 S21: -0.4372 S22: 0.0625 S23: 0.0612
REMARK 3 S31: -0.8288 S32: 0.6666 S33: 0.2354
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 5J7T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220095.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19259
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 74.245
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.12800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.67000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1NB8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, 0.2M TRI-POTASSIUM CITRATE,
REMARK 280 PH 8.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 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,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z+1/2
REMARK 290 7555 -X,Y+1/2,-Z+1/2
REMARK 290 8555 X,-Y+1/2,-Z+1/2
REMARK 290 9555 X+1/2,Y,Z+1/2
REMARK 290 10555 -X+1/2,-Y,Z+1/2
REMARK 290 11555 -X+1/2,Y,-Z+1/2
REMARK 290 12555 X+1/2,-Y,-Z+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z
REMARK 290 14555 -X+1/2,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y+1/2,-Z
REMARK 290 16555 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 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 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 98.36500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 113.18500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 98.36500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 113.18500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 98.36500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 113.18500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 98.36500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 113.18500
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 52.16500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 113.18500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 52.16500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 113.18500
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 52.16500
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 113.18500
REMARK 290 SMTRY1 12 1.000000 0.000000 0.000000 52.16500
REMARK 290 SMTRY2 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 113.18500
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 52.16500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 98.36500
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 52.16500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 98.36500
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 52.16500
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 98.36500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 52.16500
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 98.36500
REMARK 290 SMTRY3 16 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 LYS A 335 CG CD CE NZ
REMARK 470 TYR A 845 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 846 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 847 CG OD1 OD2
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 OD1 ASP A 503 NZ LYS A 841 2455 1.93
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 ALA A 221 18.41 56.38
REMARK 500 CYS A 223 -138.06 63.05
REMARK 500 MET A 244 42.81 -93.09
REMARK 500 SER A 253 26.12 -142.55
REMARK 500 LYS A 254 20.33 -154.25
REMARK 500 PHE A 283 27.71 -145.76
REMARK 500 PHE A 291 -45.59 -137.08
REMARK 500 HIS A 294 -165.35 -114.62
REMARK 500 LYS A 391 65.44 -156.48
REMARK 500 PHE A 409 47.35 -109.68
REMARK 500 ASP A 444 67.42 -164.14
REMARK 500 ALA A 446 49.61 -88.92
REMARK 500 HIS A 451 -57.08 -121.27
REMARK 500 HIS A 461 50.06 -94.38
REMARK 500 ASN A 470 75.12 -116.29
REMARK 500 ASP A 482 -122.83 53.77
REMARK 500 ILE A 494 -72.09 -113.44
REMARK 500 ASP A 502 52.56 -143.22
REMARK 500 VAL A 507 -118.14 54.49
REMARK 500 LEU A 528 42.20 -87.88
REMARK 500 LEU A 563 34.12 39.93
REMARK 500 ASP A 582 -174.76 70.18
REMARK 500 ASN A 645 39.74 -88.85
REMARK 500 ASN A 741 -1.45 75.76
REMARK 500 ASP A 750 45.36 -99.03
REMARK 500 GLU A 759 72.46 48.67
REMARK 500 ASN A 777 47.55 -87.39
REMARK 500 ASP A 847 7.00 59.07
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5J7T A 211 881 UNP Q93009 UBP7_HUMAN 195 865
SEQRES 1 A 671 THR GLY TYR VAL GLY LEU LYS ASN GLN GLY ALA THR CYS
SEQRES 2 A 671 TYR MET ASN SER LEU LEU GLN THR LEU PHE PHE THR ASN
SEQRES 3 A 671 GLN LEU ARG LYS ALA VAL TYR MET MET PRO THR GLU GLY
SEQRES 4 A 671 ASP ASP SER SER LYS SER VAL PRO LEU ALA LEU GLN ARG
SEQRES 5 A 671 VAL PHE TYR GLU LEU GLN HIS SER ASP LYS PRO VAL GLY
SEQRES 6 A 671 THR LYS LYS LEU THR LYS SER PHE GLY TRP GLU THR LEU
SEQRES 7 A 671 ASP SER PHE MET GLN HIS ASP VAL GLN GLU LEU CYS ARG
SEQRES 8 A 671 VAL LEU LEU ASP ASN VAL GLU ASN LYS MET LYS GLY THR
SEQRES 9 A 671 CYS VAL GLU GLY THR ILE PRO LYS LEU PHE ARG GLY LYS
SEQRES 10 A 671 MET VAL SER TYR ILE GLN CYS LYS GLU VAL ASP TYR ARG
SEQRES 11 A 671 SER ASP ARG ARG GLU ASP TYR TYR ASP ILE GLN LEU SER
SEQRES 12 A 671 ILE LYS GLY LYS LYS ASN ILE PHE GLU SER PHE VAL ASP
SEQRES 13 A 671 TYR VAL ALA VAL GLU GLN LEU ASP GLY ASP ASN LYS TYR
SEQRES 14 A 671 ASP ALA GLY GLU HIS GLY LEU GLN GLU ALA GLU LYS GLY
SEQRES 15 A 671 VAL LYS PHE LEU THR LEU PRO PRO VAL LEU HIS LEU GLN
SEQRES 16 A 671 LEU MET ARG PHE MET TYR ASP PRO GLN THR ASP GLN ASN
SEQRES 17 A 671 ILE LYS ILE ASN ASP ARG PHE GLU PHE PRO GLU GLN LEU
SEQRES 18 A 671 PRO LEU ASP GLU PHE LEU GLN LYS THR ASP PRO LYS ASP
SEQRES 19 A 671 PRO ALA ASN TYR ILE LEU HIS ALA VAL LEU VAL HIS SER
SEQRES 20 A 671 GLY ASP ASN HIS GLY GLY HIS TYR VAL VAL TYR LEU ASN
SEQRES 21 A 671 PRO LYS GLY ASP GLY LYS TRP CYS LYS PHE ASP ASP ASP
SEQRES 22 A 671 VAL VAL SER ARG CYS THR LYS GLU GLU ALA ILE GLU HIS
SEQRES 23 A 671 ASN TYR GLY GLY HIS ASP ASP ASP LEU SER VAL ARG HIS
SEQRES 24 A 671 CYS THR ASN ALA TYR MET LEU VAL TYR ILE ARG GLU SER
SEQRES 25 A 671 LYS LEU SER GLU VAL LEU GLN ALA VAL THR ASP HIS ASP
SEQRES 26 A 671 ILE PRO GLN GLN LEU VAL GLU ARG LEU GLN GLU GLU LYS
SEQRES 27 A 671 ARG ILE GLU ALA GLN LYS ARG LYS GLU ARG GLN GLU ALA
SEQRES 28 A 671 HIS LEU TYR MET GLN VAL GLN ILE VAL ALA GLU ASP GLN
SEQRES 29 A 671 PHE CYS GLY HIS GLN GLY ASN ASP MET TYR ASP GLU GLU
SEQRES 30 A 671 LYS VAL LYS TYR THR VAL PHE LYS VAL LEU LYS ASN SER
SEQRES 31 A 671 SER LEU ALA GLU PHE VAL GLN SER LEU SER GLN THR MET
SEQRES 32 A 671 GLY PHE PRO GLN ASP GLN ILE ARG LEU TRP PRO MET GLN
SEQRES 33 A 671 ALA ARG SER ASN GLY THR LYS ARG PRO ALA MET LEU ASP
SEQRES 34 A 671 ASN GLU ALA ASP GLY ASN LYS THR MET ILE GLU LEU SER
SEQRES 35 A 671 ASP ASN GLU ASN PRO TRP THR ILE PHE LEU GLU THR VAL
SEQRES 36 A 671 ASP PRO GLU LEU ALA ALA SER GLY ALA THR LEU PRO LYS
SEQRES 37 A 671 PHE ASP LYS ASP HIS ASP VAL MET LEU PHE LEU LYS MET
SEQRES 38 A 671 TYR ASP PRO LYS THR ARG SER LEU ASN TYR CYS GLY HIS
SEQRES 39 A 671 ILE TYR THR PRO ILE SER CYS LYS ILE ARG ASP LEU LEU
SEQRES 40 A 671 PRO VAL MET CYS ASP ARG ALA GLY PHE ILE GLN ASP THR
SEQRES 41 A 671 SER LEU ILE LEU TYR GLU GLU VAL LYS PRO ASN LEU THR
SEQRES 42 A 671 GLU ARG ILE GLN ASP TYR ASP VAL SER LEU ASP LYS ALA
SEQRES 43 A 671 LEU ASP GLU LEU MET ASP GLY ASP ILE ILE VAL PHE GLN
SEQRES 44 A 671 LYS ASP ASP PRO GLU ASN ASP ASN SER GLU LEU PRO THR
SEQRES 45 A 671 ALA LYS GLU TYR PHE ARG ASP LEU TYR HIS ARG VAL ASP
SEQRES 46 A 671 VAL ILE PHE CYS ASP LYS THR ILE PRO ASN ASP PRO GLY
SEQRES 47 A 671 PHE VAL VAL THR LEU SER ASN ARG MET ASN TYR PHE GLN
SEQRES 48 A 671 VAL ALA LYS THR VAL ALA GLN ARG LEU ASN THR ASP PRO
SEQRES 49 A 671 MET LEU LEU GLN PHE PHE LYS SER GLN GLY TYR ARG ASP
SEQRES 50 A 671 GLY PRO GLY ASN PRO LEU ARG HIS ASN TYR GLU GLY THR
SEQRES 51 A 671 LEU ARG ASP LEU LEU GLN PHE PHE LYS PRO ARG GLN PRO
SEQRES 52 A 671 LYS LYS LEU TYR TYR GLN GLN LEU
HELIX 1 AA1 TYR A 224 PHE A 234 1 11
HELIX 2 AA2 THR A 235 MET A 244 1 10
HELIX 3 AA3 SER A 255 SER A 270 1 16
HELIX 4 AA4 THR A 276 SER A 282 1 7
HELIX 5 AA5 ASP A 295 LYS A 312 1 18
HELIX 6 AA6 GLY A 318 ARG A 325 1 8
HELIX 7 AA7 ASN A 359 VAL A 368 1 10
HELIX 8 AA8 THR A 489 ILE A 494 1 6
HELIX 9 AA9 GLU A 495 TYR A 498 5 4
HELIX 10 AB1 LYS A 523 LEU A 528 1 6
HELIX 11 AB2 THR A 532 ILE A 536 5 5
HELIX 12 AB3 PRO A 537 HIS A 562 1 26
HELIX 13 AB4 ALA A 571 PHE A 575 5 5
HELIX 14 AB5 SER A 601 GLY A 614 1 14
HELIX 15 AB6 THR A 647 SER A 652 1 6
HELIX 16 AB7 ASP A 666 ALA A 674 1 9
HELIX 17 AB8 LYS A 712 ASP A 715 5 4
HELIX 18 AB9 LEU A 716 GLY A 725 1 10
HELIX 19 AC1 SER A 752 LEU A 757 1 6
HELIX 20 AC2 ASP A 772 ASN A 777 5 6
HELIX 21 AC3 THR A 782 HIS A 792 1 11
HELIX 22 AC4 ASN A 818 LEU A 830 1 13
HELIX 23 AC5 ASP A 833 MET A 835 5 3
HELIX 24 AC6 THR A 860 LEU A 865 1 6
SHEET 1 AA1 3 ARG A 343 TYR A 347 0
SHEET 2 AA1 3 GLY A 326 SER A 330 -1 N MET A 328 O GLU A 345
SHEET 3 AA1 3 VAL A 393 PHE A 395 -1 O LYS A 394 N VAL A 329
SHEET 1 AA2 5 ASP A 349 LEU A 352 0
SHEET 2 AA2 5 VAL A 401 LEU A 406 1 O HIS A 403 N ILE A 350
SHEET 3 AA2 5 THR A 511 ARG A 520 -1 O TYR A 514 N LEU A 406
SHEET 4 AA2 5 ASN A 447 ASP A 459 -1 N ILE A 449 O ILE A 519
SHEET 5 AA2 5 GLN A 430 PRO A 432 -1 N LEU A 431 O TYR A 448
SHEET 1 AA3 7 ASP A 349 LEU A 352 0
SHEET 2 AA3 7 VAL A 401 LEU A 406 1 O HIS A 403 N ILE A 350
SHEET 3 AA3 7 THR A 511 ARG A 520 -1 O TYR A 514 N LEU A 406
SHEET 4 AA3 7 ASN A 447 ASP A 459 -1 N ILE A 449 O ILE A 519
SHEET 5 AA3 7 GLY A 462 LEU A 469 -1 O VAL A 466 N VAL A 455
SHEET 6 AA3 7 CYS A 478 ASP A 481 -1 O PHE A 480 N VAL A 467
SHEET 7 AA3 7 VAL A 484 ARG A 487 -1 O VAL A 484 N ASP A 481
SHEET 1 AA4 2 TYR A 379 GLY A 382 0
SHEET 2 AA4 2 GLY A 385 GLN A 387 -1 O GLY A 385 N ALA A 381
SHEET 1 AA5 5 THR A 592 LEU A 597 0
SHEET 2 AA5 5 TYR A 564 VAL A 570 -1 N MET A 565 O VAL A 596
SHEET 3 AA5 5 TRP A 658 THR A 664 1 O TRP A 658 N GLN A 568
SHEET 4 AA5 5 ILE A 620 ALA A 627 -1 N TRP A 623 O PHE A 661
SHEET 5 AA5 5 LYS A 633 PRO A 635 -1 O ARG A 634 N GLN A 626
SHEET 1 AA6 5 SER A 698 PRO A 708 0
SHEET 2 AA6 5 ASP A 684 ASP A 693 -1 N MET A 691 O ASN A 700
SHEET 3 AA6 5 ASP A 764 LYS A 770 1 O ASP A 764 N PHE A 688
SHEET 4 AA6 5 LEU A 732 LYS A 739 -1 N TYR A 735 O VAL A 767
SHEET 5 AA6 5 LEU A 742 ARG A 745 -1 O GLU A 744 N GLU A 736
SHEET 1 AA7 4 PHE A 809 SER A 814 0
SHEET 2 AA7 4 ARG A 793 ASP A 800 -1 N VAL A 796 O VAL A 811
SHEET 3 AA7 4 LYS A 875 GLN A 880 1 O TYR A 878 N CYS A 799
SHEET 4 AA7 4 LEU A 837 PHE A 840 -1 N PHE A 840 O TYR A 877
CISPEP 1 PRO A 413 GLN A 414 0 -0.57
CISPEP 2 GLN A 414 THR A 415 0 0.76
CISPEP 3 THR A 415 ASP A 416 0 -4.99
CISPEP 4 ASP A 416 GLN A 417 0 -4.15
CISPEP 5 ARG A 508 HIS A 509 0 1.14
CISPEP 6 ASN A 656 PRO A 657 0 2.66
CRYST1 104.330 196.730 226.370 90.00 90.00 90.00 F 2 2 2 16
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 0.009585 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005083 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004418 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
