HEADER HYDROLASE 28-MAR-14 4PYZ
TITLE CRYSTAL STRUCTURE OF THE FIRST TWO UBL DOMAINS OF DEUBIQUITYLASE USP7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 537-793;
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: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-V2R;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28-LIC
KEYWDS DEUBIQUITYLASE, UBIQUITIN-LIKE DOMAIN, STRUCTURAL GENOMICS,
KEYWDS 2 STRUCTURAL GENOMICS CONSORTIUM, SGC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.WALKER,A.DONG,M.S.ONG,S.DHE-PAGANON,J.KANIA,C.BOUNTRA,
AUTHOR 2 C.H.ARROWSMITH,A.M.EDWARDS,Y.TONG,STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 3 (SGC)
REVDAT 3 20-SEP-23 4PYZ 1 SEQADV
REVDAT 2 22-NOV-17 4PYZ 1 REMARK
REVDAT 1 16-APR-14 4PYZ 0
JRNL AUTH M.S.ONG,J.R.WALKER,A.DONG,S.DHE-PAGANON,J.KANIA,C.BOUNTRA,
JRNL AUTH 2 C.H.ARROWSMITH,A.M.EDWARDS,Y.TONG,
JRNL AUTH 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)
JRNL TITL CRYSTAL STRUCTURE OF THE FIRST TWO UBL DOMAINS OF
JRNL TITL 2 DEUBIQUITYLASE USP7
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 19769
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.245
REMARK 3 R VALUE (WORKING SET) : 0.244
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.180
REMARK 3 FREE R VALUE TEST SET COUNT : 629
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.84
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.99
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.34
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2659
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.3211
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2585
REMARK 3 BIN R VALUE (WORKING SET) : 0.3198
REMARK 3 BIN FREE R VALUE : 0.3722
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.78
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 74
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4062
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 12
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 82.16
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 80.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 37.23320
REMARK 3 B22 (A**2) : 5.63840
REMARK 3 B33 (A**2) : -42.87160
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.564
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.768
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.874
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.875
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4179 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5682 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1441 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 127 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 606 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4179 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 555 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 4427 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 0.91
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.82
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.54
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|531 - A|793 }
REMARK 3 ORIGIN FOR THE GROUP (A): 21.2636 -20.5670 -20.3683
REMARK 3 T TENSOR
REMARK 3 T11: 0.0918 T22: 0.1879
REMARK 3 T33: 0.1910 T12: -0.0712
REMARK 3 T13: 0.0409 T23: -0.0425
REMARK 3 L TENSOR
REMARK 3 L11: 1.3183 L22: 1.2423
REMARK 3 L33: 0.6303 L12: -0.2050
REMARK 3 L13: 0.0260 L23: -0.3117
REMARK 3 S TENSOR
REMARK 3 S11: -0.0707 S12: 0.3199 S13: -0.1038
REMARK 3 S21: -0.1195 S22: -0.0010 S23: -0.0973
REMARK 3 S31: 0.2187 S32: 0.0130 S33: 0.0717
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|533 - B|793 }
REMARK 3 ORIGIN FOR THE GROUP (A): 44.1291 -11.2558 -16.5863
REMARK 3 T TENSOR
REMARK 3 T11: 0.0680 T22: 0.0268
REMARK 3 T33: 0.2493 T12: -0.0485
REMARK 3 T13: -0.0825 T23: 0.1079
REMARK 3 L TENSOR
REMARK 3 L11: 1.3112 L22: 0.8257
REMARK 3 L33: 1.1883 L12: -0.1888
REMARK 3 L13: -0.2238 L23: 0.5161
REMARK 3 S TENSOR
REMARK 3 S11: -0.0578 S12: 0.0949 S13: 0.3104
REMARK 3 S21: -0.0378 S22: 0.0616 S23: 0.0160
REMARK 3 S31: -0.1803 S32: 0.0028 S33: -0.0038
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4PYZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000085395.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97924
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19822
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.830
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 (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.93600
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: PDB ENTRY 2YLM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4000, 0.2 M NH4AC, 0.1 M
REMARK 280 NACITRATE PH5.6, VAPOR DIFFUSION HANGING DROP, TEMPERATURE 291K,
REMARK 280 VAPOR DIFFUSION, HANGING DROP
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 34.16400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.09850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.87750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.09850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.16400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.87750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: AS PER THE AUTHORS THE BIOLOGICAL ASSEMBLY IS UNKNOWN
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SER A 521
REMARK 465 HIS A 522
REMARK 465 HIS A 523
REMARK 465 HIS A 524
REMARK 465 HIS A 525
REMARK 465 HIS A 526
REMARK 465 HIS A 527
REMARK 465 SER A 528
REMARK 465 SER A 529
REMARK 465 GLY A 530
REMARK 465 SER B 521
REMARK 465 HIS B 522
REMARK 465 HIS B 523
REMARK 465 HIS B 524
REMARK 465 HIS B 525
REMARK 465 HIS B 526
REMARK 465 HIS B 527
REMARK 465 SER B 528
REMARK 465 SER B 529
REMARK 465 GLY B 530
REMARK 465 LEU B 531
REMARK 465 VAL B 532
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 GLU A 546 CG CD OE1 OE2
REMARK 470 GLU A 547 CD OE1 OE2
REMARK 470 LYS A 548 CE NZ
REMARK 470 ARG A 549 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 553 CG CD OE1 NE2
REMARK 470 LYS A 554 CD CE NZ
REMARK 470 LYS A 556 CD CE NZ
REMARK 470 GLU A 587 CD OE1 OE2
REMARK 470 LYS A 588 CD CE NZ
REMARK 470 LYS A 595 CD CE NZ
REMARK 470 LEU A 597 CG CD1 CD2
REMARK 470 GLN A 611 CG CD OE1 NE2
REMARK 470 MET A 613 CG SD CE
REMARK 470 ASN A 640 CG OD1 ND2
REMARK 470 GLU A 641 CG CD OE1 OE2
REMARK 470 ASP A 666 CG OD1 OD2
REMARK 470 GLU A 668 OE1 OE2
REMARK 470 THR A 675 OG1 CG2
REMARK 470 LYS A 678 CG CD CE NZ
REMARK 470 LYS A 681 CG CD CE NZ
REMARK 470 LYS A 695 CE NZ
REMARK 470 LYS A 712 CG CD CE NZ
REMARK 470 LEU A 753 CD1 CD2
REMARK 470 LYS A 755 CG CD CE NZ
REMARK 470 GLU A 759 CD OE1 OE2
REMARK 470 ARG A 788 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 543 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 547 CG CD OE1 OE2
REMARK 470 LYS B 548 CD CE NZ
REMARK 470 ILE B 550 CG1 CG2 CD1
REMARK 470 LYS B 554 CD CE NZ
REMARK 470 LYS B 556 CG CD CE NZ
REMARK 470 GLU B 587 CG CD OE1 OE2
REMARK 470 LYS B 588 CG CD CE NZ
REMARK 470 LYS B 595 CE NZ
REMARK 470 GLN B 611 OE1 NE2
REMARK 470 GLN B 619 CG CD OE1 NE2
REMARK 470 ARG B 621 NE CZ NH1 NH2
REMARK 470 SER B 629 OG
REMARK 470 GLU B 641 CG CD OE1 OE2
REMARK 470 ASN B 645 CG OD1 ND2
REMARK 470 LYS B 646 CG CD CE NZ
REMARK 470 ASP B 666 CG OD1 OD2
REMARK 470 LEU B 669 CG CD1 CD2
REMARK 470 SER B 672 OG
REMARK 470 LYS B 678 CG CD CE NZ
REMARK 470 LYS B 681 CG CD CE NZ
REMARK 470 HIS B 683 CG ND1 CD2 CE1 NE2
REMARK 470 LEU B 687 CD1 CD2
REMARK 470 LYS B 695 CG CD CE NZ
REMARK 470 SER B 710 OG
REMARK 470 GLN B 728 CG CD OE1 NE2
REMARK 470 ASP B 729 CG OD1 OD2
REMARK 470 GLU B 744 CD OE1 OE2
REMARK 470 LEU B 753 CG CD1 CD2
REMARK 470 LYS B 755 CG CD CE NZ
REMARK 470 GLU B 759 CD OE1 OE2
REMARK 470 LYS B 770 CD CE NZ
REMARK 470 GLU B 774 CG CD OE1 OE2
REMARK 470 ASN B 777 CG OD1 ND2
REMARK 470 GLU B 785 OE1 OE2
REMARK 470 ARG B 788 CG CD NE CZ NH1 NH2
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 ASP A 582 -165.27 67.92
REMARK 500 ASN A 741 -12.92 86.18
REMARK 500 ASP B 582 -158.86 66.45
REMARK 500 ASP B 729 68.73 63.62
REMARK 500 ASN B 741 -7.36 83.73
REMARK 500 HIS B 792 30.72 -90.05
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4PYZ A 537 793 UNP Q93009 UBP7_HUMAN 537 793
DBREF 4PYZ B 537 793 UNP Q93009 UBP7_HUMAN 537 793
SEQADV 4PYZ SER A 521 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ HIS A 522 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ HIS A 523 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ HIS A 524 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ HIS A 525 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ HIS A 526 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ HIS A 527 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ SER A 528 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ SER A 529 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ GLY A 530 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ LEU A 531 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ VAL A 532 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ PRO A 533 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ ARG A 534 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ GLY A 535 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ SER A 536 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ SER B 521 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ HIS B 522 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ HIS B 523 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ HIS B 524 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ HIS B 525 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ HIS B 526 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ HIS B 527 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ SER B 528 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ SER B 529 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ GLY B 530 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ LEU B 531 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ VAL B 532 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ PRO B 533 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ ARG B 534 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ GLY B 535 UNP Q93009 EXPRESSION TAG
SEQADV 4PYZ SER B 536 UNP Q93009 EXPRESSION TAG
SEQRES 1 A 273 SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES 2 A 273 ARG GLY SER PRO GLN GLN LEU VAL GLU ARG LEU GLN GLU
SEQRES 3 A 273 GLU LYS ARG ILE GLU ALA GLN LYS ARG LYS GLU ARG GLN
SEQRES 4 A 273 GLU ALA HIS LEU TYR MET GLN VAL GLN ILE VAL ALA GLU
SEQRES 5 A 273 ASP GLN PHE CYS GLY HIS GLN GLY ASN ASP MET TYR ASP
SEQRES 6 A 273 GLU GLU LYS VAL LYS TYR THR VAL PHE LYS VAL LEU LYS
SEQRES 7 A 273 ASN SER SER LEU ALA GLU PHE VAL GLN SER LEU SER GLN
SEQRES 8 A 273 THR MET GLY PHE PRO GLN ASP GLN ILE ARG LEU TRP PRO
SEQRES 9 A 273 MET GLN ALA ARG SER ASN GLY THR LYS ARG PRO ALA MET
SEQRES 10 A 273 LEU ASP ASN GLU ALA ASP GLY ASN LYS THR MET ILE GLU
SEQRES 11 A 273 LEU SER ASP ASN GLU ASN PRO TRP THR ILE PHE LEU GLU
SEQRES 12 A 273 THR VAL ASP PRO GLU LEU ALA ALA SER GLY ALA THR LEU
SEQRES 13 A 273 PRO LYS PHE ASP LYS ASP HIS ASP VAL MET LEU PHE LEU
SEQRES 14 A 273 LYS MET TYR ASP PRO LYS THR ARG SER LEU ASN TYR CYS
SEQRES 15 A 273 GLY HIS ILE TYR THR PRO ILE SER CYS LYS ILE ARG ASP
SEQRES 16 A 273 LEU LEU PRO VAL MET CYS ASP ARG ALA GLY PHE ILE GLN
SEQRES 17 A 273 ASP THR SER LEU ILE LEU TYR GLU GLU VAL LYS PRO ASN
SEQRES 18 A 273 LEU THR GLU ARG ILE GLN ASP TYR ASP VAL SER LEU ASP
SEQRES 19 A 273 LYS ALA LEU ASP GLU LEU MET ASP GLY ASP ILE ILE VAL
SEQRES 20 A 273 PHE GLN LYS ASP ASP PRO GLU ASN ASP ASN SER GLU LEU
SEQRES 21 A 273 PRO THR ALA LYS GLU TYR PHE ARG ASP LEU TYR HIS ARG
SEQRES 1 B 273 SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES 2 B 273 ARG GLY SER PRO GLN GLN LEU VAL GLU ARG LEU GLN GLU
SEQRES 3 B 273 GLU LYS ARG ILE GLU ALA GLN LYS ARG LYS GLU ARG GLN
SEQRES 4 B 273 GLU ALA HIS LEU TYR MET GLN VAL GLN ILE VAL ALA GLU
SEQRES 5 B 273 ASP GLN PHE CYS GLY HIS GLN GLY ASN ASP MET TYR ASP
SEQRES 6 B 273 GLU GLU LYS VAL LYS TYR THR VAL PHE LYS VAL LEU LYS
SEQRES 7 B 273 ASN SER SER LEU ALA GLU PHE VAL GLN SER LEU SER GLN
SEQRES 8 B 273 THR MET GLY PHE PRO GLN ASP GLN ILE ARG LEU TRP PRO
SEQRES 9 B 273 MET GLN ALA ARG SER ASN GLY THR LYS ARG PRO ALA MET
SEQRES 10 B 273 LEU ASP ASN GLU ALA ASP GLY ASN LYS THR MET ILE GLU
SEQRES 11 B 273 LEU SER ASP ASN GLU ASN PRO TRP THR ILE PHE LEU GLU
SEQRES 12 B 273 THR VAL ASP PRO GLU LEU ALA ALA SER GLY ALA THR LEU
SEQRES 13 B 273 PRO LYS PHE ASP LYS ASP HIS ASP VAL MET LEU PHE LEU
SEQRES 14 B 273 LYS MET TYR ASP PRO LYS THR ARG SER LEU ASN TYR CYS
SEQRES 15 B 273 GLY HIS ILE TYR THR PRO ILE SER CYS LYS ILE ARG ASP
SEQRES 16 B 273 LEU LEU PRO VAL MET CYS ASP ARG ALA GLY PHE ILE GLN
SEQRES 17 B 273 ASP THR SER LEU ILE LEU TYR GLU GLU VAL LYS PRO ASN
SEQRES 18 B 273 LEU THR GLU ARG ILE GLN ASP TYR ASP VAL SER LEU ASP
SEQRES 19 B 273 LYS ALA LEU ASP GLU LEU MET ASP GLY ASP ILE ILE VAL
SEQRES 20 B 273 PHE GLN LYS ASP ASP PRO GLU ASN ASP ASN SER GLU LEU
SEQRES 21 B 273 PRO THR ALA LYS GLU TYR PHE ARG ASP LEU TYR HIS ARG
HET UNX B1000 1
HET UNX B1001 1
HETNAM UNX UNKNOWN ATOM OR ION
FORMUL 3 UNX 2(X)
FORMUL 5 HOH *12(H2 O)
HELIX 1 1 SER A 536 GLU A 560 1 25
HELIX 2 2 ASP A 573 PHE A 575 5 3
HELIX 3 3 SER A 601 GLY A 614 1 14
HELIX 4 4 PRO A 616 ASP A 618 5 3
HELIX 5 5 THR A 647 ASP A 653 1 7
HELIX 6 6 ASP A 666 SER A 672 1 7
HELIX 7 7 ILE A 713 ASP A 715 5 3
HELIX 8 8 LEU A 716 GLY A 725 1 10
HELIX 9 9 SER A 752 LEU A 757 1 6
HELIX 10 10 ASP A 772 SER A 778 5 7
HELIX 11 11 THR A 782 HIS A 792 1 11
HELIX 12 12 SER B 536 ALA B 561 1 26
HELIX 13 13 ASP B 573 PHE B 575 5 3
HELIX 14 14 SER B 601 GLY B 614 1 14
HELIX 15 15 PRO B 616 ASP B 618 5 3
HELIX 16 16 THR B 647 ASP B 653 1 7
HELIX 17 17 LEU B 716 GLY B 725 1 10
HELIX 18 18 SER B 752 LEU B 757 1 6
HELIX 19 19 ASP B 772 SER B 778 5 7
HELIX 20 20 THR B 782 HIS B 792 1 11
SHEET 1 A 5 THR A 592 LEU A 597 0
SHEET 2 A 5 TYR A 564 ALA A 571 -1 N MET A 565 O VAL A 596
SHEET 3 A 5 TRP A 658 THR A 664 1 O TRP A 658 N GLN A 568
SHEET 4 A 5 ILE A 620 ALA A 627 -1 N TRP A 623 O PHE A 661
SHEET 5 A 5 LYS A 633 PRO A 635 -1 O ARG A 634 N GLN A 626
SHEET 1 B 5 SER A 698 PRO A 708 0
SHEET 2 B 5 ASP A 684 ASP A 693 -1 N MET A 691 O ASN A 700
SHEET 3 B 5 ILE A 765 LYS A 770 1 O PHE A 768 N TYR A 692
SHEET 4 B 5 LEU A 732 LYS A 739 -1 N TYR A 735 O VAL A 767
SHEET 5 B 5 LEU A 742 ARG A 745 -1 O LEU A 742 N LYS A 739
SHEET 1 C 5 THR B 592 LEU B 597 0
SHEET 2 C 5 TYR B 564 ALA B 571 -1 N MET B 565 O VAL B 596
SHEET 3 C 5 TRP B 658 THR B 664 1 O LEU B 662 N VAL B 570
SHEET 4 C 5 ILE B 620 ALA B 627 -1 N TRP B 623 O PHE B 661
SHEET 5 C 5 LYS B 633 PRO B 635 -1 O ARG B 634 N GLN B 626
SHEET 1 D 5 SER B 698 PRO B 708 0
SHEET 2 D 5 ASP B 684 ASP B 693 -1 N LEU B 689 O GLY B 703
SHEET 3 D 5 ASP B 764 LYS B 770 1 O ASP B 764 N PHE B 688
SHEET 4 D 5 LEU B 732 LYS B 739 -1 N ILE B 733 O GLN B 769
SHEET 5 D 5 LEU B 742 ARG B 745 -1 O GLU B 744 N GLU B 736
SSBOND 1 CYS A 576 CYS B 576 1555 1555 2.04
CISPEP 1 ASN A 656 PRO A 657 0 2.75
CISPEP 2 ASN B 656 PRO B 657 0 2.29
CRYST1 68.328 103.755 116.197 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 0.014635 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009638 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008606 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
