HEADER LIGASE 09-APR-10 2XBF
TITLE NEDD4 HECT STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE NEDD4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HECT DOMAIN, RESIDUES 519-900;
COMPND 5 SYNONYM: NEDD-4, NEURAL PRECURSOR CELL EXPRESSED DEVELOPMENTALLY
COMPND 6 DOWN-REGULATED PROTEIN 4, CELL PROLIFERATION-INDUCING GENE 53
COMPND 7 PROTEIN;
COMPND 8 EC: 6.3.2.-;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1
KEYWDS LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.MASPERO,V.CECATIELLO,A.MUSACCHIO,S.POLO,S.PASQUALATO
REVDAT 3 20-DEC-23 2XBF 1 REMARK
REVDAT 2 13-APR-11 2XBF 1 JRNL
REVDAT 1 23-MAR-11 2XBF 0
JRNL AUTH E.MASPERO,S.MARI,E.VALENTINI,A.MUSACCHIO,A.FISH,
JRNL AUTH 2 S.PASQUALATO,S.POLO
JRNL TITL STRUCTURE OF THE HECT:UBIQUITIN COMPLEX AND ITS ROLE IN
JRNL TITL 2 UBIQUITIN CHAIN ELONGATION
JRNL REF EMBO REP. V. 12 342 2011
JRNL REFN ISSN 1469-221X
JRNL PMID 21399620
JRNL DOI 10.1038/EMBOR.2011.21
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.58
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 14282
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 705
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 48.5855 - 4.2799 1.00 2838 130 0.1741 0.2241
REMARK 3 2 4.2799 - 3.3974 1.00 2739 160 0.1641 0.2278
REMARK 3 3 3.3974 - 2.9680 1.00 2730 134 0.2060 0.2550
REMARK 3 4 2.9680 - 2.6966 1.00 2729 131 0.2303 0.3166
REMARK 3 5 2.6966 - 2.5034 0.94 2541 150 0.2410 0.3112
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 : 0.32
REMARK 3 B_SOL : 29.78
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 1.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.57
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.96010
REMARK 3 B22 (A**2) : -2.29810
REMARK 3 B33 (A**2) : 0.33790
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.25690
REMARK 3 B23 (A**2) : 0.00000
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 3278
REMARK 3 ANGLE : 0.603 4415
REMARK 3 CHIRALITY : 0.047 443
REMARK 3 PLANARITY : 0.002 570
REMARK 3 DIHEDRAL : 16.381 1206
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 2XBF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-APR-10.
REMARK 100 THE DEPOSITION ID IS D_1290043603.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-SEP-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14288
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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 2ONI
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NA-MES, PH 6.0, 4% PEG 400, 35
REMARK 280 MM CACL2, 5 MM TCEP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
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 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 87.70250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 19.42150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 87.70250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 19.42150
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 GLY A 515
REMARK 465 PRO A 516
REMARK 465 LEU A 517
REMARK 465 GLY A 518
REMARK 465 GLN A 894
REMARK 465 GLY A 895
REMARK 465 PHE A 896
REMARK 465 ASP A 897
REMARK 465 GLY A 898
REMARK 465 VAL A 899
REMARK 465 ASP A 900
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 ARG A 832 CG CD NE CZ NH1 NH2
REMARK 470 THR A 893 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 ASP A 538 48.27 -83.10
REMARK 500 ASN A 623 35.45 -99.21
REMARK 500 VAL A 677 -69.49 -103.76
REMARK 500 VAL A 742 -51.53 -121.95
REMARK 500 ASP A 784 97.92 -65.15
REMARK 500 PRO A 858 -7.71 -49.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2001 DISTANCE = 6.03 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1894
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1895
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1896
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1897
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1898
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XBB RELATED DB: PDB
REMARK 900 NEDD4 HECT:UB COMPLEX
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ISOFORM 4 P46934-4
DBREF 2XBF A 519 900 UNP P46934 NEDD4_HUMAN 519 900
SEQADV 2XBF GLY A 515 UNP P46934 EXPRESSION TAG
SEQADV 2XBF PRO A 516 UNP P46934 EXPRESSION TAG
SEQADV 2XBF LEU A 517 UNP P46934 EXPRESSION TAG
SEQADV 2XBF GLY A 518 UNP P46934 EXPRESSION TAG
SEQRES 1 A 386 GLY PRO LEU GLY SER ARG ASP TYR LYS ARG LYS TYR GLU
SEQRES 2 A 386 PHE PHE ARG ARG LYS LEU LYS LYS GLN ASN ASP ILE PRO
SEQRES 3 A 386 ASN LYS PHE GLU MET LYS LEU ARG ARG ALA THR VAL LEU
SEQRES 4 A 386 GLU ASP SER TYR ARG ARG ILE MET GLY VAL LYS ARG ALA
SEQRES 5 A 386 ASP PHE LEU LYS ALA ARG LEU TRP ILE GLU PHE ASP GLY
SEQRES 6 A 386 GLU LYS GLY LEU ASP TYR GLY GLY VAL ALA ARG GLU TRP
SEQRES 7 A 386 PHE PHE LEU ILE SER LYS GLU MET PHE ASN PRO TYR TYR
SEQRES 8 A 386 GLY LEU PHE GLU TYR SER ALA THR ASP ASN TYR THR LEU
SEQRES 9 A 386 GLN ILE ASN PRO ASN SER GLY LEU CYS ASN GLU ASP HIS
SEQRES 10 A 386 LEU SER TYR PHE LYS PHE ILE GLY ARG VAL ALA GLY MET
SEQRES 11 A 386 ALA VAL TYR HIS GLY LYS LEU LEU ASP GLY PHE PHE ILE
SEQRES 12 A 386 ARG PRO PHE TYR LYS MET MET LEU HIS LYS PRO ILE THR
SEQRES 13 A 386 LEU HIS ASP MET GLU SER VAL ASP SER GLU TYR TYR ASN
SEQRES 14 A 386 SER LEU ARG TRP ILE LEU GLU ASN ASP PRO THR GLU LEU
SEQRES 15 A 386 ASP LEU ARG PHE ILE ILE ASP GLU GLU LEU PHE GLY GLN
SEQRES 16 A 386 THR HIS GLN HIS GLU LEU LYS ASN GLY GLY SER GLU ILE
SEQRES 17 A 386 VAL VAL THR ASN LYS ASN LYS LYS GLU TYR ILE TYR LEU
SEQRES 18 A 386 VAL ILE GLN TRP ARG PHE VAL ASN ARG ILE GLN LYS GLN
SEQRES 19 A 386 MET ALA ALA PHE LYS GLU GLY PHE PHE GLU LEU ILE PRO
SEQRES 20 A 386 GLN ASP LEU ILE LYS ILE PHE ASP GLU ASN GLU LEU GLU
SEQRES 21 A 386 LEU LEU MET CYS GLY LEU GLY ASP VAL ASP VAL ASN ASP
SEQRES 22 A 386 TRP ARG GLU HIS THR LYS TYR LYS ASN GLY TYR SER ALA
SEQRES 23 A 386 ASN HIS GLN VAL ILE GLN TRP PHE TRP LYS ALA VAL LEU
SEQRES 24 A 386 MET MET ASP SER GLU LYS ARG ILE ARG LEU LEU GLN PHE
SEQRES 25 A 386 VAL THR GLY THR SER ARG VAL PRO MET ASN GLY PHE ALA
SEQRES 26 A 386 GLU LEU TYR GLY SER ASN GLY PRO GLN SER PHE THR VAL
SEQRES 27 A 386 GLU GLN TRP GLY THR PRO GLU LYS LEU PRO ARG ALA HIS
SEQRES 28 A 386 THR CYS PHE ASN ARG LEU ASP LEU PRO PRO TYR GLU SER
SEQRES 29 A 386 PHE GLU GLU LEU TRP ASP LYS LEU GLN MET ALA ILE GLU
SEQRES 30 A 386 ASN THR GLN GLY PHE ASP GLY VAL ASP
HET EDO A1894 4
HET EDO A1895 4
HET EDO A1896 4
HET EDO A1897 4
HET CA A1898 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CA CALCIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO 4(C2 H6 O2)
FORMUL 6 CA CA 2+
FORMUL 7 HOH *197(H2 O)
HELIX 1 1 ASP A 521 LEU A 533 1 13
HELIX 2 2 ARG A 548 ALA A 550 5 3
HELIX 3 3 THR A 551 MET A 561 1 11
HELIX 4 4 ARG A 565 ALA A 571 5 7
HELIX 5 5 ASP A 584 PHE A 601 1 18
HELIX 6 6 ASN A 602 GLY A 606 5 5
HELIX 7 7 ASN A 623 ASN A 628 1 6
HELIX 8 8 ASP A 630 HIS A 648 1 19
HELIX 9 9 ILE A 657 LEU A 665 1 9
HELIX 10 10 THR A 670 SER A 676 1 7
HELIX 11 11 ASP A 678 ASN A 691 1 14
HELIX 12 12 PRO A 693 ASP A 697 5 5
HELIX 13 13 GLY A 718 ILE A 722 5 5
HELIX 14 14 ASN A 728 VAL A 742 1 15
HELIX 15 15 ILE A 745 PHE A 757 1 13
HELIX 16 16 PRO A 761 LYS A 766 1 6
HELIX 17 17 ASP A 769 GLY A 779 1 11
HELIX 18 18 ASP A 784 HIS A 791 1 8
HELIX 19 19 HIS A 802 MET A 815 1 14
HELIX 20 20 ASP A 816 GLY A 829 1 14
HELIX 21 21 GLY A 837 LEU A 841 5 5
HELIX 22 22 THR A 866 PHE A 868 5 3
HELIX 23 23 SER A 878 ASN A 892 1 15
SHEET 1 AA 2 LYS A 542 LEU A 547 0
SHEET 2 AA 2 ARG A 572 PHE A 577 1 O ARG A 572 N PHE A 543
SHEET 1 AB 2 PHE A 608 TYR A 610 0
SHEET 2 AB 2 LEU A 618 ILE A 620 -1 O GLN A 619 N GLU A 609
SHEET 1 AC 2 ILE A 701 LEU A 706 0
SHEET 2 AC 2 GLN A 709 GLU A 714 -1 O GLN A 709 N LEU A 706
SHEET 1 AD 4 THR A 792 LYS A 795 0
SHEET 2 AD 4 PHE A 850 GLN A 854 1 O PHE A 850 N LYS A 793
SHEET 3 AD 4 ARG A 870 LEU A 873 1 O LEU A 871 N GLU A 853
SHEET 4 AD 4 ARG A 863 HIS A 865 -1 O ARG A 863 N ASP A 872
LINK CA CA A1898 O HOH A2148 1555 1555 3.07
SITE 1 AC1 5 TRP A 687 LEU A 696 GLU A 731 EDO A1895
SITE 2 AC1 5 HOH A2197
SITE 1 AC2 2 SER A 684 EDO A1894
SITE 1 AC3 3 ARG A 558 ARG A 559 GLN A 712
SITE 1 AC4 4 TYR A 557 MET A 561 HIS A 711 GLN A 712
SITE 1 AC5 3 TYR A 794 ALA A 800 HOH A2148
CRYST1 175.405 38.843 60.640 90.00 93.13 90.00 C 1 2 1 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 0.005701 0.000000 0.000312 0.00000
SCALE2 0.000000 0.025745 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016515 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
