HEADER LIGASE 16-SEP-11 3TUG
TITLE CRYSTAL STRUCTURE OF THE HECT DOMAIN OF ITCH E3 UBIQUITIN LIGASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE ITCHY HOMOLOG;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ITCH, ATROPHIN-1-INTERACTING PROTEIN 4, AIP4, NFE2-
COMPND 5 ASSOCIATED POLYPEPTIDE 1, NAPP1;
COMPND 6 EC: 6.3.2.-;
COMPND 7 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: ITCH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-V2R;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28-MHL
KEYWDS STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, CATALYTIC
KEYWDS 2 DOMAIN, E3 LIGASE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DONG,E.DOBROVETSKY,S.XUE,C.BUTLER,A.WERNIMONT,J.R.WALKER,W.TEMPEL,
AUTHOR 2 S.DHE-PAGANON,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,Y.TONG,STRUCTURAL
AUTHOR 3 GENOMICS CONSORTIUM (SGC)
REVDAT 2 13-SEP-23 3TUG 1 REMARK SEQADV
REVDAT 1 12-OCT-11 3TUG 0
JRNL AUTH E.DOBROVETSKY,A.DONG,S.XUE,C.BUTLER,A.WERNIMONT,J.R.WALKER,
JRNL AUTH 2 W.TEMPEL,S.DHE-PAGANON,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,
JRNL AUTH 3 Y.TONG
JRNL TITL CRYSTAL STRUCTURE OF THE HECT DOMAIN OF ITCH E3 UBIQUITIN
JRNL TITL 2 LIGASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.27 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.8.0
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) : 2.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 20665
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.230
REMARK 3 FREE R VALUE TEST SET COUNT : 668
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) : 2.27
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.39
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2976
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2108
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2867
REMARK 3 BIN R VALUE (WORKING SET) : 0.2089
REMARK 3 BIN FREE R VALUE : 0.2587
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.66
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 109
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 : 2672
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 78
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.80860
REMARK 3 B22 (A**2) : -4.80860
REMARK 3 B33 (A**2) : 9.61720
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) : 0.317
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) : NULL
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 : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2760 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3746 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 910 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 64 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 409 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2760 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 348 ; 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 : 3184 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.94
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.69
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.81
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1384 -37.1045 -18.8237
REMARK 3 T TENSOR
REMARK 3 T11: -0.1570 T22: -0.1233
REMARK 3 T33: -0.1882 T12: -0.0475
REMARK 3 T13: 0.0051 T23: -0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 1.5333 L22: 1.7899
REMARK 3 L33: 2.4305 L12: -0.0886
REMARK 3 L13: -0.1021 L23: -0.6521
REMARK 3 S TENSOR
REMARK 3 S11: 0.0474 S12: 0.0785 S13: 0.2314
REMARK 3 S21: 0.0129 S22: -0.0551 S23: 0.0427
REMARK 3 S31: -0.0621 S32: 0.0227 S33: 0.0077
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3TUG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-SEP-11.
REMARK 100 THE DEPOSITION ID IS D_1000067933.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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) : 0.97934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20717
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.270
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.80
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : 0.09100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 38.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.80
REMARK 200 R MERGE FOR SHELL (I) : 0.89000
REMARK 200 R SYM FOR SHELL (I) : 0.89000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
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: 3OML
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG1500, 0.2M NACL 0.1M HEPES PH
REMARK 280 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.64767
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 73.29533
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 73.29533
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 36.64767
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 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 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 MET A 506
REMARK 465 HIS A 507
REMARK 465 HIS A 508
REMARK 465 HIS A 509
REMARK 465 HIS A 510
REMARK 465 HIS A 511
REMARK 465 HIS A 512
REMARK 465 SER A 513
REMARK 465 SER A 514
REMARK 465 GLY A 515
REMARK 465 ARG A 516
REMARK 465 GLU A 517
REMARK 465 ASN A 518
REMARK 465 LEU A 519
REMARK 465 TYR A 520
REMARK 465 PHE A 521
REMARK 465 GLN A 522
REMARK 465 GLY A 523
REMARK 465 TYR A 524
REMARK 465 GLY A 616
REMARK 465 LYS A 617
REMARK 465 ASP A 618
REMARK 465 ASN A 619
REMARK 465 ILE A 696
REMARK 465 GLU A 697
REMARK 465 GLU A 698
REMARK 465 CYS A 699
REMARK 465 ASP A 700
REMARK 465 LEU A 701
REMARK 465 GLU A 702
REMARK 465 MET A 703
REMARK 465 VAL A 707
REMARK 465 ASP A 708
REMARK 465 LYS A 709
REMARK 465 GLU A 710
REMARK 465 ILE A 711
REMARK 465 LEU A 712
REMARK 465 GLY A 713
REMARK 465 GLU A 714
REMARK 465 ILE A 715
REMARK 465 LYS A 716
REMARK 465 SER A 717
REMARK 465 HIS A 718
REMARK 465 ASP A 719
REMARK 465 LEU A 720
REMARK 465 LYS A 721
REMARK 465 PRO A 722
REMARK 465 ASN A 723
REMARK 465 GLY A 724
REMARK 465 GLY A 725
REMARK 465 ASN A 726
REMARK 465 ILE A 727
REMARK 465 LEU A 728
REMARK 465 VAL A 729
REMARK 465 THR A 730
REMARK 465 GLU A 731
REMARK 465 GLU A 732
REMARK 465 ASN A 733
REMARK 465 GLU A 898
REMARK 465 GLY A 899
REMARK 465 PHE A 900
REMARK 465 GLY A 901
REMARK 465 GLN A 902
REMARK 465 GLU A 903
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 VAL A 525 CG1 CG2
REMARK 470 LYS A 529 CG CD CE NZ
REMARK 470 GLN A 540 CD OE1 NE2
REMARK 470 LYS A 555 CG CD CE NZ
REMARK 470 GLU A 585 CG CD OE1 OE2
REMARK 470 TYR A 589 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET A 608 CG SD CE
REMARK 470 TYR A 620 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 674 CD1 CD2
REMARK 470 LYS A 675 CG CD CE NZ
REMARK 470 GLU A 678 CG CD OE1 OE2
REMARK 470 SER A 679 OG
REMARK 470 GLU A 683 CD OE1 OE2
REMARK 470 LEU A 688 CG CD1 CD2
REMARK 470 VAL A 691 CG1 CG2
REMARK 470 LYS A 692 CG CD CE NZ
REMARK 470 GLU A 693 CG CD OE1 OE2
REMARK 470 ASN A 694 CG OD1 ND2
REMARK 470 ASN A 695 CG OD1 ND2
REMARK 470 TYR A 704 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE A 705 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER A 706 OG
REMARK 470 LYS A 734 CG CD CE NZ
REMARK 470 GLU A 735 CG CD OE1 OE2
REMARK 470 GLU A 736 CG CD OE1 OE2
REMARK 470 ILE A 738 CD1
REMARK 470 ARG A 739 CD NE CZ NH1 NH2
REMARK 470 LEU A 790 CD1 CD2
REMARK 470 ARG A 800 NH1 NH2
REMARK 470 ARG A 801 NE CZ NH1 NH2
REMARK 470 ARG A 804 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 807 CG CD CE NZ
REMARK 470 LYS A 817 CG CD CE NZ
REMARK 470 LYS A 823 CE NZ
REMARK 470 VAL A 839 CG1 CG2
REMARK 470 MET A 846 CE
REMARK 470 LYS A 853 NZ
REMARK 470 LYS A 858 CG CD CE NZ
REMARK 470 VAL A 859 CG1 CG2
REMARK 470 LYS A 861 CG CD CE NZ
REMARK 470 GLU A 862 CG CD OE1 OE2
REMARK 470 ARG A 867 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 881 CD CE NZ
REMARK 470 SER A 882 OG
REMARK 470 LEU A 886 CG CD1 CD2
REMARK 470 LYS A 887 CD CE NZ
REMARK 470 GLU A 888 CG CD OE1 OE2
REMARK 470 LYS A 889 CG CD CE NZ
REMARK 470 THR A 897 OG1 CG2
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 GLN A 546 -153.32 57.75
REMARK 500 GLU A 585 46.56 -96.71
REMARK 500 ASP A 656 46.85 -109.52
REMARK 500 GLU A 693 31.76 -87.96
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 CL A 100
DBREF 3TUG A 524 903 UNP Q96J02 ITCH_HUMAN 524 903
SEQADV 3TUG MET A 506 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG HIS A 507 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG HIS A 508 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG HIS A 509 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG HIS A 510 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG HIS A 511 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG HIS A 512 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG SER A 513 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG SER A 514 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG GLY A 515 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG ARG A 516 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG GLU A 517 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG ASN A 518 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG LEU A 519 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG TYR A 520 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG PHE A 521 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG GLN A 522 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG GLY A 523 UNP Q96J02 EXPRESSION TAG
SEQADV 3TUG SER A 605 UNP Q96J02 LEU 605 ENGINEERED MUTATION
SEQADV 3TUG ARG A 801 UNP Q96J02 HIS 801 ENGINEERED MUTATION
SEQRES 1 A 398 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 A 398 LEU TYR PHE GLN GLY TYR VAL ARG ASP PHE LYS ALA LYS
SEQRES 3 A 398 VAL GLN TYR PHE ARG PHE TRP CYS GLN GLN LEU ALA MET
SEQRES 4 A 398 PRO GLN HIS ILE LYS ILE THR VAL THR ARG LYS THR LEU
SEQRES 5 A 398 PHE GLU ASP SER PHE GLN GLN ILE MET SER PHE SER PRO
SEQRES 6 A 398 GLN ASP LEU ARG ARG ARG LEU TRP VAL ILE PHE PRO GLY
SEQRES 7 A 398 GLU GLU GLY LEU ASP TYR GLY GLY VAL ALA ARG GLU TRP
SEQRES 8 A 398 PHE PHE LEU LEU SER HIS GLU VAL SER ASN PRO MET TYR
SEQRES 9 A 398 CYS LEU PHE GLU TYR ALA GLY LYS ASP ASN TYR CYS LEU
SEQRES 10 A 398 GLN ILE ASN PRO ALA SER TYR ILE ASN PRO ASP HIS LEU
SEQRES 11 A 398 LYS TYR PHE ARG PHE ILE GLY ARG PHE ILE ALA MET ALA
SEQRES 12 A 398 LEU PHE HIS GLY LYS PHE ILE ASP THR GLY PHE SER LEU
SEQRES 13 A 398 PRO PHE TYR LYS ARG ILE LEU ASN LYS PRO VAL GLY LEU
SEQRES 14 A 398 LYS ASP LEU GLU SER ILE ASP PRO GLU PHE TYR ASN SER
SEQRES 15 A 398 LEU ILE TRP VAL LYS GLU ASN ASN ILE GLU GLU CYS ASP
SEQRES 16 A 398 LEU GLU MET TYR PHE SER VAL ASP LYS GLU ILE LEU GLY
SEQRES 17 A 398 GLU ILE LYS SER HIS ASP LEU LYS PRO ASN GLY GLY ASN
SEQRES 18 A 398 ILE LEU VAL THR GLU GLU ASN LYS GLU GLU TYR ILE ARG
SEQRES 19 A 398 MET VAL ALA GLU TRP ARG LEU SER ARG GLY VAL GLU GLU
SEQRES 20 A 398 GLN THR GLN ALA PHE PHE GLU GLY PHE ASN GLU ILE LEU
SEQRES 21 A 398 PRO GLN GLN TYR LEU GLN TYR PHE ASP ALA LYS GLU LEU
SEQRES 22 A 398 GLU VAL LEU LEU CYS GLY MET GLN GLU ILE ASP LEU ASN
SEQRES 23 A 398 ASP TRP GLN ARG HIS ALA ILE TYR ARG ARG TYR ALA ARG
SEQRES 24 A 398 THR SER LYS GLN ILE MET TRP PHE TRP GLN PHE VAL LYS
SEQRES 25 A 398 GLU ILE ASP ASN GLU LYS ARG MET ARG LEU LEU GLN PHE
SEQRES 26 A 398 VAL THR GLY THR CYS ARG LEU PRO VAL GLY GLY PHE ALA
SEQRES 27 A 398 ASP LEU MET GLY SER ASN GLY PRO GLN LYS PHE CYS ILE
SEQRES 28 A 398 GLU LYS VAL GLY LYS GLU ASN TRP LEU PRO ARG SER HIS
SEQRES 29 A 398 THR CYS PHE ASN ARG LEU ASP LEU PRO PRO TYR LYS SER
SEQRES 30 A 398 TYR GLU GLN LEU LYS GLU LYS LEU LEU PHE ALA ILE GLU
SEQRES 31 A 398 GLU THR GLU GLY PHE GLY GLN GLU
HET CL A 100 1
HET UNX A1001 1
HET UNX A1002 1
HET UNX A1003 1
HET UNX A1004 1
HET UNX A1006 1
HET UNX A1007 1
HET UNX A1008 1
HET UNX A1009 1
HET UNX A1010 1
HETNAM CL CHLORIDE ION
HETNAM UNX UNKNOWN ATOM OR ION
FORMUL 2 CL CL 1-
FORMUL 3 UNX 9(X)
FORMUL 12 HOH *78(H2 O)
HELIX 1 1 ASP A 527 GLN A 540 1 14
HELIX 2 2 THR A 556 PHE A 568 1 13
HELIX 3 3 GLN A 571 ARG A 575 5 5
HELIX 4 4 ASP A 588 VAL A 604 1 17
HELIX 5 5 PRO A 626 ASN A 631 5 6
HELIX 6 6 ASP A 633 HIS A 651 1 19
HELIX 7 7 SER A 660 LEU A 668 1 9
HELIX 8 8 LEU A 674 GLU A 678 5 5
HELIX 9 9 ASP A 681 GLU A 693 1 13
HELIX 10 10 GLU A 735 ARG A 748 1 14
HELIX 11 11 VAL A 750 LEU A 765 1 16
HELIX 12 12 PRO A 766 GLN A 771 5 6
HELIX 13 13 ASP A 774 GLY A 784 1 11
HELIX 14 14 ASP A 789 HIS A 796 1 8
HELIX 15 15 SER A 806 ILE A 819 1 14
HELIX 16 16 ASP A 820 GLY A 833 1 14
HELIX 17 17 GLY A 841 LEU A 845 5 5
HELIX 18 18 THR A 870 PHE A 872 5 3
HELIX 19 19 SER A 882 GLU A 896 1 15
SHEET 1 A 2 HIS A 547 THR A 551 0
SHEET 2 A 2 ARG A 576 ILE A 580 1 O ILE A 580 N ILE A 550
SHEET 1 B 3 PHE A 612 TYR A 614 0
SHEET 2 B 3 CYS A 621 ILE A 624 -1 O GLN A 623 N GLU A 613
SHEET 3 B 3 GLY A 658 PHE A 659 1 O GLY A 658 N LEU A 622
SHEET 1 C 4 ILE A 798 ARG A 800 0
SHEET 2 C 4 CYS A 855 LYS A 858 1 O ILE A 856 N ARG A 800
SHEET 3 C 4 ARG A 874 LEU A 877 1 O LEU A 877 N GLU A 857
SHEET 4 C 4 ARG A 867 HIS A 869 -1 N ARG A 867 O ASP A 876
SITE 1 AC1 1 ALA A 775
CRYST1 82.779 82.779 109.943 90.00 90.00 120.00 P 31 2 1 6
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 0.012080 0.006975 0.000000 0.00000
SCALE2 0.000000 0.013949 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009096 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
