HEADER HYDROLASE 16-JUN-11 3ZRH
TITLE CRYSTAL STRUCTURE OF THE LYS29, LYS33-LINKAGE-SPECIFIC TRABID OTU
TITLE 2 DEUBIQUITINASE DOMAIN REVEALS AN ANKYRIN-REPEAT UBIQUITIN BINDING
TITLE 3 DOMAIN (ANKUBD)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN THIOESTERASE ZRANB1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ANKUBD, OTU, RESIUDES 245-697;
COMPND 5 SYNONYM: TRABID, ZINC FINGER RAN-BINDING DOMAIN-CONTAINING PROTEIN
COMPND 6 1, HTRABID;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: POPINK;
SOURCE 10 OTHER_DETAILS: ARCTICEXPRESS COMPETENT CELLS
KEYWDS HYDROLASE, DEUBIQUITINATING ENZYME, WNT SIGNALING, OVARIAN TUMOR
KEYWDS 2 DOMAIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.D.F.LICCHESI,M.AKUTSU,D.KOMANDER
REVDAT 2 25-JAN-12 3ZRH 1 JRNL
REVDAT 1 14-DEC-11 3ZRH 0
JRNL AUTH J.D.F.LICCHESI,J.MIESZCZANEK,T.E.T.MEVISSEN,T.J.RUTHERFORD,
JRNL AUTH 2 M.AKUTSU,S.VIRDEE,F.E.OUALID,J.W.CHIN,H.OVAA,M.BIENZ,
JRNL AUTH 3 D.KOMANDER
JRNL TITL AN ANKYRIN-REPEAT UBIQUITIN-BINDING DOMAIN DETERMINES
JRNL TITL 2 TRABID'S SPECIFICITY FOR ATYPICAL UBIQUITIN CHAINS.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 19 62 2011
JRNL REFN ISSN 1545-9993
JRNL PMID 22157957
JRNL DOI 10.1038/NSMB.2169
REMARK 2
REMARK 2 RESOLUTION. 2.23 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_764)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.712
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.80
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.95
REMARK 3 NUMBER OF REFLECTIONS : 54669
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.2035
REMARK 3 R VALUE (WORKING SET) : 0.2001
REMARK 3 FREE R VALUE : 0.2478
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.8
REMARK 3 FREE R VALUE TEST SET COUNT : 3741
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 44.7211 - 4.8026 1.00 5093 375 0.1922 0.2193
REMARK 3 2 4.8026 - 3.8126 1.00 5083 372 0.1638 0.1979
REMARK 3 3 3.8126 - 3.3309 1.00 5101 377 0.1959 0.2315
REMARK 3 4 3.3309 - 3.0264 1.00 5064 369 0.1965 0.2592
REMARK 3 5 3.0264 - 2.8095 1.00 5104 379 0.1805 0.2330
REMARK 3 6 2.8095 - 2.6439 1.00 5140 382 0.2063 0.2810
REMARK 3 7 2.6439 - 2.5115 1.00 5067 370 0.2296 0.3213
REMARK 3 8 2.5115 - 2.4022 1.00 5111 365 0.2502 0.3150
REMARK 3 9 2.4022 - 2.3097 1.00 5103 384 0.2558 0.3416
REMARK 3 10 2.3097 - 2.2300 1.00 5062 368 0.3143 0.3734
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.327
REMARK 3 B_SOL : 44.619
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.85
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.59
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.45
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 : 0.013 3520
REMARK 3 ANGLE : 1.413 4787
REMARK 3 CHIRALITY : 0.099 535
REMARK 3 PLANARITY : 0.006 610
REMARK 3 DIHEDRAL : 18.102 1261
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND ((RESSEQ 244:340))
REMARK 3 ORIGIN FOR THE GROUP (A): 55.5874 70.0735 15.1967
REMARK 3 T TENSOR
REMARK 3 T11: 0.2593 T22: 0.1745
REMARK 3 T33: 0.1095 T12: 0.0169
REMARK 3 T13: 0.0545 T23: 0.0426
REMARK 3 L TENSOR
REMARK 3 L11: 2.7998 L22: 1.8027
REMARK 3 L33: 1.9007 L12: 0.8436
REMARK 3 L13: 0.9130 L23: -0.5974
REMARK 3 S TENSOR
REMARK 3 S11: -0.3837 S12: -0.1741 S13: -0.0987
REMARK 3 S21: -0.4411 S22: 0.1712 S23: 0.0235
REMARK 3 S31: 0.1316 S32: -0.2210 S33: 0.1582
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND ((RESSEQ 341:692))
REMARK 3 ORIGIN FOR THE GROUP (A): 21.2816 50.0897 18.3257
REMARK 3 T TENSOR
REMARK 3 T11: 0.1339 T22: 0.1022
REMARK 3 T33: 0.0677 T12: -0.0017
REMARK 3 T13: -0.0361 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 1.0336 L22: 1.3377
REMARK 3 L33: 1.4472 L12: -0.3020
REMARK 3 L13: 0.1319 L23: -0.0598
REMARK 3 S TENSOR
REMARK 3 S11: 0.1171 S12: 0.1237 S13: -0.0732
REMARK 3 S21: -0.2195 S22: -0.1031 S23: 0.0825
REMARK 3 S31: 0.1613 S32: -0.0612 S33: 0.0177
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 3ZRH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-DEC-11.
REMARK 100 THE PDBE ID CODE IS EBI-48715.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29095
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.23
REMARK 200 RESOLUTION RANGE LOW (A) : 46.32
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.1
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.1
REMARK 200 R MERGE FOR SHELL (I) : 0.49
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.70
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 150 MM NACL, 100 MM NAOAC, 5 MM
REMARK 280 MGCL2, 50 MM MES [PH 5.9]
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 30.20000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.50500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.07500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.50500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.20000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.07500
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: 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 ALA A 244
REMARK 465 SER A 547
REMARK 465 PHE A 548
REMARK 465 ARG A 549
REMARK 465 GLY A 550
REMARK 465 GLU A 551
REMARK 465 GLY A 596
REMARK 465 TYR A 597
REMARK 465 GLY A 598
REMARK 465 ASN A 599
REMARK 465 ARG A 600
REMARK 465 GLY A 601
REMARK 465 ALA A 602
REMARK 465 GLY A 603
REMARK 465 ALA A 604
REMARK 465 ASN A 605
REMARK 465 LEU A 606
REMARK 465 ASN A 607
REMARK 465 THR A 608
REMARK 465 ASP A 609
REMARK 465 ASP A 610
REMARK 465 CYS A 693
REMARK 465 THR A 694
REMARK 465 SER A 695
REMARK 465 LEU A 696
REMARK 465 SER A 697
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 250 CG CD CE NZ
REMARK 470 LYS A 251 CG CD CE NZ
REMARK 470 LEU A 252 CG CD1 CD2
REMARK 470 LYS A 253 CG CD CE NZ
REMARK 470 GLU A 282 CG CD OE1 OE2
REMARK 470 LYS A 285 CG CD CE NZ
REMARK 470 LEU A 494 CG CD1 CD2
REMARK 470 GLU A 501 CG CD OE1 OE2
REMARK 470 GLN A 502 CG CD OE1 NE2
REMARK 470 ASP A 506 CG OD1 OD2
REMARK 470 LYS A 543 CG CD CE NZ
REMARK 470 TYR A 544 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR A 545 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 546 CG CD CE NZ
REMARK 470 THR A 552 OG1 CG2
REMARK 470 LEU A 553 CG CD1 CD2
REMARK 470 ASP A 595 CB CG OD1 OD2
REMARK 470 GLN A 635 CG CD OE1 NE2
REMARK 470 GLU A 640 CG CD OE1 OE2
REMARK 470 GLU A 641 CG CD OE1 OE2
REMARK 470 LYS A 645 CG CD CE NZ
REMARK 470 ARG A 670 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 671 CG CD NE CZ NH1 NH2
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 OE1 GLU A 350 O HOH A 2030 2.11
REMARK 500 O TYR A 488 OG SER A 491 2.14
REMARK 500 OG SER A 491 O HOH A 2134 2.05
REMARK 500 NH1 ARG A 557 O HOH A 2141 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 688 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
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 ASP A 248 97.41 -64.50
REMARK 500 GLN A 323 45.80 -103.78
REMARK 500 ASP A 326 -64.80 -29.77
REMARK 500 CYS A 348 84.15 -150.84
REMARK 500 THR A 426 -60.37 -120.82
REMARK 500 ALA A 440 29.03 -61.31
REMARK 500 THR A 452 -84.41 -125.14
REMARK 500 TYR A 488 -72.59 -53.33
REMARK 500 SER A 489 -19.39 -49.81
REMARK 500 SER A 497 147.82 -170.97
REMARK 500 GLU A 522 -162.60 -117.89
REMARK 500 TYR A 544 92.83 179.63
REMARK 500 ARG A 583 77.32 22.19
REMARK 500 ALA A 634 -30.50 -39.06
REMARK 500 ASN A 639 174.04 -54.11
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 EDO A1693
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1694
DBREF 3ZRH A 245 697 UNP Q9UGI0 ZRAN1_HUMAN 245 697
SEQADV 3ZRH ALA A 244 UNP Q9UGI0 EXPRESSION TAG
SEQRES 1 A 454 ALA LEU GLU VAL ASP PHE LYS LYS LEU LYS GLN ILE LYS
SEQRES 2 A 454 ASN ARG MET LYS LYS THR ASP TRP LEU PHE LEU ASN ALA
SEQRES 3 A 454 CYS VAL GLY VAL VAL GLU GLY ASP LEU ALA ALA ILE GLU
SEQRES 4 A 454 ALA TYR LYS SER SER GLY GLY ASP ILE ALA ARG GLN LEU
SEQRES 5 A 454 THR ALA ASP GLU VAL ARG LEU LEU ASN ARG PRO SER ALA
SEQRES 6 A 454 PHE ASP VAL GLY TYR THR LEU VAL HIS LEU ALA ILE ARG
SEQRES 7 A 454 PHE GLN ARG GLN ASP MET LEU ALA ILE LEU LEU THR GLU
SEQRES 8 A 454 VAL SER GLN GLN ALA ALA LYS CYS ILE PRO ALA MET VAL
SEQRES 9 A 454 CYS PRO GLU LEU THR GLU GLN ILE ARG ARG GLU ILE ALA
SEQRES 10 A 454 ALA SER LEU HIS GLN ARG LYS GLY ASP PHE ALA CYS TYR
SEQRES 11 A 454 PHE LEU THR ASP LEU VAL THR PHE THR LEU PRO ALA ASP
SEQRES 12 A 454 ILE GLU ASP LEU PRO PRO THR VAL GLN GLU LYS LEU PHE
SEQRES 13 A 454 ASP GLU VAL LEU ASP ARG ASP VAL GLN LYS GLU LEU GLU
SEQRES 14 A 454 GLU GLU SER PRO ILE ILE ASN TRP SER LEU GLU LEU ALA
SEQRES 15 A 454 THR ARG LEU ASP SER ARG LEU TYR ALA LEU TRP ASN ARG
SEQRES 16 A 454 THR ALA GLY ASP CYS LEU LEU ASP SER VAL LEU GLN ALA
SEQRES 17 A 454 THR TRP GLY ILE TYR ASP LYS ASP SER VAL LEU ARG LYS
SEQRES 18 A 454 ALA LEU HIS ASP SER LEU HIS ASP CYS SER HIS TRP PHE
SEQRES 19 A 454 TYR THR ARG TRP LYS ASP TRP GLU SER TRP TYR SER GLN
SEQRES 20 A 454 SER PHE GLY LEU HIS PHE SER LEU ARG GLU GLU GLN TRP
SEQRES 21 A 454 GLN GLU ASP TRP ALA PHE ILE LEU SER LEU ALA SER GLN
SEQRES 22 A 454 PRO GLY ALA SER LEU GLU GLN THR HIS ILE PHE VAL LEU
SEQRES 23 A 454 ALA HIS ILE LEU ARG ARG PRO ILE ILE VAL TYR GLY VAL
SEQRES 24 A 454 LYS TYR TYR LYS SER PHE ARG GLY GLU THR LEU GLY TYR
SEQRES 25 A 454 THR ARG PHE GLN GLY VAL TYR LEU PRO LEU LEU TRP GLU
SEQRES 26 A 454 GLN SER PHE CYS TRP LYS SER PRO ILE ALA LEU GLY TYR
SEQRES 27 A 454 THR ARG GLY HIS PHE SER ALA LEU VAL ALA MET GLU ASN
SEQRES 28 A 454 ASP GLY TYR GLY ASN ARG GLY ALA GLY ALA ASN LEU ASN
SEQRES 29 A 454 THR ASP ASP ASP VAL THR ILE THR PHE LEU PRO LEU VAL
SEQRES 30 A 454 ASP SER GLU ARG LYS LEU LEU HIS VAL HIS PHE LEU SER
SEQRES 31 A 454 ALA GLN GLU LEU GLY ASN GLU GLU GLN GLN GLU LYS LEU
SEQRES 32 A 454 LEU ARG GLU TRP LEU ASP CYS CYS VAL THR GLU GLY GLY
SEQRES 33 A 454 VAL LEU VAL ALA MET GLN LYS SER SER ARG ARG ARG ASN
SEQRES 34 A 454 HIS PRO LEU VAL THR GLN MET VAL GLU LYS TRP LEU ASP
SEQRES 35 A 454 ARG TYR ARG GLN ILE ARG PRO CYS THR SER LEU SER
HET EDO A1693 4
HET EDO A1694 4
HET CL A1695 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO 2(C2 H6 O2)
FORMUL 3 CL CL 1-
FORMUL 4 HOH *188(H2 O)
HELIX 1 1 ASP A 248 ARG A 258 1 11
HELIX 2 2 LYS A 260 GLY A 276 1 17
HELIX 3 3 ASP A 277 SER A 286 1 10
HELIX 4 4 THR A 296 ASN A 304 1 9
HELIX 5 5 THR A 314 PHE A 322 1 9
HELIX 6 6 ARG A 324 LYS A 341 1 18
HELIX 7 7 ILE A 343 CYS A 348 1 6
HELIX 8 8 CYS A 348 SER A 362 1 15
HELIX 9 9 PRO A 384 LEU A 390 5 7
HELIX 10 10 PRO A 391 LEU A 403 1 13
HELIX 11 11 ASP A 404 GLU A 413 1 10
HELIX 12 12 SER A 421 THR A 426 1 6
HELIX 13 13 ASP A 442 ALA A 451 1 10
HELIX 14 14 ASP A 457 ASP A 459 5 3
HELIX 15 15 SER A 460 CYS A 473 1 14
HELIX 16 16 CYS A 473 PHE A 492 1 20
HELIX 17 17 ARG A 499 ALA A 514 1 16
HELIX 18 18 GLU A 522 LEU A 533 1 12
HELIX 19 19 GLU A 568 CYS A 572 5 5
HELIX 20 20 ASN A 639 LEU A 651 1 13
HELIX 21 21 HIS A 673 GLN A 689 1 17
SHEET 1 AA 2 LEU A 363 GLN A 365 0
SHEET 2 AA 2 TYR A 373 LEU A 375 -1 O PHE A 374 N HIS A 364
SHEET 1 AB 5 LEU A 432 ALA A 434 0
SHEET 2 AB 5 HIS A 585 ALA A 591 -1 O VAL A 590 N TYR A 433
SHEET 3 AB 5 ILE A 577 THR A 582 -1 O ALA A 578 N LEU A 589
SHEET 4 AB 5 ILE A 537 GLY A 541 1 O ILE A 538 N LEU A 579
SHEET 5 AB 5 GLY A 560 TYR A 562 -1 O GLY A 560 N VAL A 539
SHEET 1 AC 3 VAL A 612 PRO A 618 0
SHEET 2 AC 3 LEU A 661 SER A 668 -1 O ALA A 663 N LEU A 617
SHEET 3 AC 3 CYS A 653 VAL A 655 -1 O CYS A 654 N VAL A 662
CISPEP 1 ARG A 691 PRO A 692 0 -3.49
SITE 1 AC1 3 LYS A 261 TRP A 264 ARG A 427
SITE 1 AC2 4 LYS A 341 LEU A 403 ARG A 405 HOH A2071
CRYST1 60.400 72.150 133.010 90.00 90.00 90.00 P 21 21 21 4
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 0.016556 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013860 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007518 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
