HEADER TRANSCRIPTION/ANTITUMOR PROTEIN 09-OCT-08 3EU7
TITLE CRYSTAL STRUCTURE OF A PALB2 / BRCA2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PARTNER AND LOCALIZER OF BRCA2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL WD40 DOMAIN, RESIDUES 835-1186;
COMPND 5 SYNONYM: PALB2, FANCONI ANEMIA GROUP N PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 19MERIC PEPTIDE FROM BREAST CANCER TYPE 2 SUSCEPTIBILITY
COMPND 9 PROTEIN;
COMPND 10 CHAIN: X;
COMPND 11 FRAGMENT: INTERACTION WITH PALB2, RESIDUES 21-39;
COMPND 12 SYNONYM: BRCA2, FANCONI ANEMIA GROUP D1 PROTEIN;
COMPND 13 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: PALB2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTWO-B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: CHEMICALLY SYNTHESIZED; THIS SEQUENCE OCCURS
SOURCE 14 NATURALLY IN HUMANS
KEYWDS WD40 DOMAIN, BETA PROPELLER, PROTEIN-PEPTIDE COMPLEX, FANCONI ANEMIA,
KEYWDS 2 NUCLEUS, PHOSPHOPROTEIN, WD REPEAT, DISEASE MUTATION, DNA DAMAGE,
KEYWDS 3 DNA REPAIR, TRANSCRIPTION-ANTITUMOR PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.W.OLIVER,L.H.PEARL
REVDAT 6 01-NOV-23 3EU7 1 REMARK SEQADV LINK
REVDAT 5 12-NOV-14 3EU7 1 HET HETATM HETNAM
REVDAT 4 05-FEB-14 3EU7 1 REMARK
REVDAT 3 13-JUL-11 3EU7 1 VERSN
REVDAT 2 15-SEP-09 3EU7 1 JRNL
REVDAT 1 28-JUL-09 3EU7 0
JRNL AUTH A.W.OLIVER,S.SWIFT,C.J.LORD,A.ASHWORTH,L.H.PEARL
JRNL TITL STRUCTURAL BASIS FOR RECRUITMENT OF BRCA2 BY PALB2
JRNL REF EMBO REP. V. 10 990 2009
JRNL REFN ISSN 1469-221X
JRNL PMID 19609323
JRNL DOI 10.1038/EMBOR.2009.126
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.50
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.910
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.8
REMARK 3 NUMBER OF REFLECTIONS : 19019
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 : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1691
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 37.5005 - 5.0320 0.89 2643 146 0.1811 0.2115
REMARK 3 2 5.0320 - 3.9955 0.90 2660 139 0.1475 0.1719
REMARK 3 3 3.9955 - 3.4908 0.90 2672 149 0.1694 0.2436
REMARK 3 4 3.4908 - 3.1718 0.89 2633 153 0.1925 0.2454
REMARK 3 5 3.1718 - 2.9446 0.89 2611 148 0.2028 0.2984
REMARK 3 6 2.9446 - 2.7711 0.88 2617 116 0.2193 0.3029
REMARK 3 7 2.7711 - 2.6323 0.88 2639 147 0.2188 0.3230
REMARK 3 8 2.6323 - 2.5178 0.87 2565 139 0.2209 0.2770
REMARK 3 9 2.5178 - 2.4208 0.86 2543 134 0.2262 0.2938
REMARK 3 10 2.4208 - 2.3373 0.86 2571 132 0.2475 0.2992
REMARK 3 11 2.3373 - 2.2642 0.86 2517 148 0.2605 0.3354
REMARK 3 12 2.2642 - 2.1995 0.85 2577 140 0.3052 0.3683
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 : 0.37
REMARK 3 B_SOL : 60.52
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.61
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.19280
REMARK 3 B22 (A**2) : 2.08420
REMARK 3 B33 (A**2) : 3.10860
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.96540
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 : 0.014 2539
REMARK 3 ANGLE : 1.630 3457
REMARK 3 CHIRALITY : 0.097 411
REMARK 3 PLANARITY : 0.009 427
REMARK 3 DIHEDRAL : 19.007 879
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 3EU7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000049772.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9430
REMARK 200 MONOCHROMATOR : DIAMOND (111)
REMARK 200 OPTICS : HORIZONTALLY BENDED GE(220)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19026
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 37.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.60200
REMARK 200 R SYM FOR SHELL (I) : 0.60200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2W18
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA-CACODYLATE PH 6.5, 0.2M
REMARK 280 MAGNESIUM ACETATE, 10% (W/V) PEG 8000, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
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 41.40750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.01300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 41.40750
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.01300
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, X
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 831
REMARK 465 PRO A 832
REMARK 465 HIS A 833
REMARK 465 MET A 834
REMARK 465 SER A 835
REMARK 465 VAL A 836
REMARK 465 GLU A 837
REMARK 465 GLN A 838
REMARK 465 THR A 839
REMARK 465 GLU A 840
REMARK 465 THR A 841
REMARK 465 ALA A 842
REMARK 465 GLU A 843
REMARK 465 LEU A 844
REMARK 465 PRO A 845
REMARK 465 ALA A 846
REMARK 465 SER A 847
REMARK 465 ASP A 848
REMARK 465 SER A 849
REMARK 465 ILE A 850
REMARK 465 ASN A 851
REMARK 465 PRO A 852
REMARK 465 GLY A 853
REMARK 465 ARG A 879
REMARK 465 ALA A 880
REMARK 465 SER A 950
REMARK 465 SER A 951
REMARK 465 ASP A 952
REMARK 465 ASP A 953
REMARK 465 GLU A 954
REMARK 465 GLU A 996
REMARK 465 ASP A 997
REMARK 465 PRO A 1077
REMARK 465 CYS A 1078
REMARK 465 ALA A 1079
REMARK 465 LYS A 1080
REMARK 465 GLU A 1081
REMARK 465 SER A 1082
REMARK 465 GLU A 1083
REMARK 465 SER A 1084
REMARK 465 LEU A 1085
REMARK 465 ARG A 1086
REMARK 465 SER A 1087
REMARK 465 LYS X 21
REMARK 465 ALA X 22
REMARK 465 ASP X 23
REMARK 465 GLU X 38
REMARK 465 ALA X 39
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 ASN A 854 CG OD1 ND2
REMARK 470 GLU A 878 CG CD OE1 OE2
REMARK 470 GLU A 884 CG CD OE1 OE2
REMARK 470 GLU A 916 CG CD OE1 OE2
REMARK 470 LYS A 957 CG CD CE NZ
REMARK 470 ASN A 965 CG OD1 ND2
REMARK 470 LYS A 974 CE NZ
REMARK 470 LYS A1041 CD CE NZ
REMARK 470 SER A1054 OG
REMARK 470 TYR A1055 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN A1056 CG CD OE1 NE2
REMARK 470 SER A1058 OG
REMARK 470 HIS A1076 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A1117 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1146 CG CD OE1 NE2
REMARK 470 ASP A1156 CG OD1 OD2
REMARK 470 LYS A1176 CE NZ
REMARK 470 ASP A1177 CG OD1 OD2
REMARK 470 TYR A1185 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU X 24 CG CD1 CD2
REMARK 470 SER X 37 OG
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 907 O HOH A 1273 2.19
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 PRO A 864 85.66 -66.16
REMARK 500 TRP A 877 -147.63 -104.42
REMARK 500 ASP A 902 -159.62 -150.19
REMARK 500 GLU A 916 -88.57 98.20
REMARK 500 LEU A 939 -55.72 -154.97
REMARK 500 THR A 983 -31.46 -134.68
REMARK 500 LEU A 984 -111.58 -138.90
REMARK 500 LYS A1047 140.56 -171.00
REMARK 500 ASP A1052 124.64 -32.34
REMARK 500 ASP A1053 5.87 -51.51
REMARK 500 SER A1054 142.97 146.46
REMARK 500 GLN A1056 104.64 108.22
REMARK 500 ALA A1057 130.51 144.83
REMARK 500 SER A1058 -71.50 112.79
REMARK 500 THR A1100 -8.90 84.52
REMARK 500 PRO A1112 -73.00 -18.51
REMARK 500 GLN A1114 109.35 -168.87
REMARK 500 ASP A1125 -114.53 44.88
REMARK 500 ALA A1149 145.40 174.84
REMARK 500 SER A1155 -147.71 80.29
REMARK 500 ASP A1177 -46.43 -176.87
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 GOL A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2
DBREF 3EU7 A 835 1186 UNP Q86YC2 PALB2_HUMAN 835 1186
DBREF 3EU7 X 21 39 UNP P51587 BRCA2_HUMAN 21 39
SEQADV 3EU7 GLY A 831 UNP Q86YC2 EXPRESSION TAG
SEQADV 3EU7 PRO A 832 UNP Q86YC2 EXPRESSION TAG
SEQADV 3EU7 HIS A 833 UNP Q86YC2 EXPRESSION TAG
SEQADV 3EU7 MET A 834 UNP Q86YC2 EXPRESSION TAG
SEQRES 1 A 356 GLY PRO HIS MET SER VAL GLU GLN THR GLU THR ALA GLU
SEQRES 2 A 356 LEU PRO ALA SER ASP SER ILE ASN PRO GLY ASN LEU GLN
SEQRES 3 A 356 LEU VAL SER GLU LEU LYS ASN PRO SER GLY SER CYS SER
SEQRES 4 A 356 VAL ASP VAL SER ALA MET PHE TRP GLU ARG ALA GLY CYS
SEQRES 5 A 356 LYS GLU PRO CYS ILE ILE THR ALA CYS GLU ASP VAL VAL
SEQRES 6 A 356 SER LEU TRP LYS ALA LEU ASP ALA TRP GLN TRP GLU LYS
SEQRES 7 A 356 LEU TYR THR TRP HIS PHE ALA GLU VAL PRO VAL LEU GLN
SEQRES 8 A 356 ILE VAL PRO VAL PRO ASP VAL TYR ASN LEU VAL CYS VAL
SEQRES 9 A 356 ALA LEU GLY ASN LEU GLU ILE ARG GLU ILE ARG ALA LEU
SEQRES 10 A 356 PHE CYS SER SER ASP ASP GLU SER GLU LYS GLN VAL LEU
SEQRES 11 A 356 LEU LYS SER GLY ASN ILE LYS ALA VAL LEU GLY LEU THR
SEQRES 12 A 356 LYS ARG ARG LEU VAL SER SER SER GLY THR LEU SER ASP
SEQRES 13 A 356 GLN GLN VAL GLU VAL MET THR PHE ALA GLU ASP GLY GLY
SEQRES 14 A 356 GLY LYS GLU ASN GLN PHE LEU MET PRO PRO GLU GLU THR
SEQRES 15 A 356 ILE LEU THR PHE ALA GLU VAL GLN GLY MET GLN GLU ALA
SEQRES 16 A 356 LEU LEU GLY THR THR ILE MET ASN ASN ILE VAL ILE TRP
SEQRES 17 A 356 ASN LEU LYS THR GLY GLN LEU LEU LYS LYS MET HIS ILE
SEQRES 18 A 356 ASP ASP SER TYR GLN ALA SER VAL CYS HIS LYS ALA TYR
SEQRES 19 A 356 SER GLU MET GLY LEU LEU PHE ILE VAL LEU SER HIS PRO
SEQRES 20 A 356 CYS ALA LYS GLU SER GLU SER LEU ARG SER PRO VAL PHE
SEQRES 21 A 356 GLN LEU ILE VAL ILE ASN PRO LYS THR THR LEU SER VAL
SEQRES 22 A 356 GLY VAL MET LEU TYR CYS LEU PRO PRO GLY GLN ALA GLY
SEQRES 23 A 356 ARG PHE LEU GLU GLY ASP VAL LYS ASP HIS CSD ALA ALA
SEQRES 24 A 356 ALA ILE LEU THR SER GLY THR ILE ALA ILE TRP ASP LEU
SEQRES 25 A 356 LEU LEU GLY GLN CYS THR ALA LEU LEU PRO PRO VAL SER
SEQRES 26 A 356 ASP GLN HIS TRP SER PHE VAL LYS TRP SER GLY THR ASP
SEQRES 27 A 356 SER HIS LEU LEU ALA GLY GLN LYS ASP GLY ASN ILE PHE
SEQRES 28 A 356 VAL TYR HIS TYR SER
SEQRES 1 X 19 LYS ALA ASP LEU GLY PRO ILE SER LEU ASN TRP PHE GLU
SEQRES 2 X 19 GLU LEU SER SER GLU ALA
MODRES 3EU7 CSD A 1127 CYS 3-SULFINOALANINE
HET CSD A1127 8
HET GOL A 1 6
HET GOL A 2 6
HETNAM CSD 3-SULFINOALANINE
HETNAM GOL GLYCEROL
HETSYN CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 CSD C3 H7 N O4 S
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 HOH *98(H2 O)
HELIX 1 1 ASN X 30 SER X 36 1 7
SHEET 1 A 4 LEU A 855 LEU A 861 0
SHEET 2 A 4 ILE A1180 TYR A1185 -1 O ILE A1180 N LEU A 861
SHEET 3 A 4 HIS A1170 GLY A1174 -1 N ALA A1173 O PHE A1181
SHEET 4 A 4 PHE A1161 TRP A1164 -1 N PHE A1161 O GLY A1174
SHEET 1 B 4 SER A 869 PHE A 876 0
SHEET 2 B 4 PRO A 885 CYS A 891 -1 O ILE A 888 N SER A 873
SHEET 3 B 4 VAL A 894 ALA A 900 -1 O VAL A 894 N CYS A 891
SHEET 4 B 4 TRP A 906 HIS A 913 -1 O LEU A 909 N LEU A 897
SHEET 1 C 7 VAL A 919 VAL A 923 0
SHEET 2 C 7 VAL A 932 LEU A 936 -1 O ALA A 935 N LEU A 920
SHEET 3 C 7 ILE A 941 PHE A 948 -1 O ARG A 942 N LEU A 936
SHEET 4 C 7 LYS A 957 LEU A 972 -1 O LEU A 961 N ILE A 944
SHEET 5 C 7 ARG A 976 SER A 981 -1 O ARG A 976 N LEU A 972
SHEET 6 C 7 GLN A 988 PHE A 994 -1 O GLU A 990 N SER A 979
SHEET 7 C 7 GLY A1000 LEU A1006 -1 O GLN A1004 N VAL A 991
SHEET 1 D 8 LEU A1045 HIS A1050 0
SHEET 2 D 8 ASN A1034 ASN A1039 -1 N ILE A1035 O MET A1049
SHEET 3 D 8 ALA A1025 THR A1030 -1 N GLY A1028 O VAL A1036
SHEET 4 D 8 ILE A1013 GLN A1020 -1 N LEU A1014 O THR A1029
SHEET 5 D 8 CYS A1060 GLU A1066 1 O SER A1065 N GLN A1020
SHEET 6 D 8 LEU A1069 SER A1075 -1 O PHE A1071 N TYR A1064
SHEET 7 D 8 PHE A1090 ILE A1095 -1 O ILE A1093 N ILE A1072
SHEET 8 D 8 SER A1102 TYR A1108 -1 O VAL A1103 N VAL A1094
SHEET 1 E 4 PHE A1118 LYS A1124 0
SHEET 2 E 4 CSD A1127 LEU A1132 -1 O CSD A1127 N LYS A1124
SHEET 3 E 4 ILE A1137 ASP A1141 -1 O TRP A1140 N ALA A1128
SHEET 4 E 4 CYS A1147 LEU A1151 -1 O LEU A1151 N ILE A1137
LINK C HIS A1126 N CSD A1127 1555 1555 1.33
LINK C CSD A1127 N ALA A1128 1555 1555 1.32
CISPEP 1 SER A 1054 TYR A 1055 0 -2.12
CISPEP 2 TYR A 1055 GLN A 1056 0 12.36
CISPEP 3 ALA A 1057 SER A 1058 0 -8.13
CISPEP 4 ASP A 1177 GLY A 1178 0 0.91
SITE 1 AC1 7 ALA A 874 PRO A 885 CYS A 886 SER A1165
SITE 2 AC1 7 THR A1167 ASP A1168 HIS A1170
SITE 1 AC2 5 ARG A 942 GLU A 943 SER A 963 ASN A1003
SITE 2 AC2 5 HOH A1217
CRYST1 82.815 62.026 77.975 90.00 108.23 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 0.012075 0.000000 0.003978 0.00000
SCALE2 0.000000 0.016122 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013503 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
