HEADER CELL ADHESION 18-AUG-17 5OSQ
TITLE ZP-N DOMAIN OF MAMMALIAN SPERM RECEPTOR ZP3 (CRYSTAL FORM II,
TITLE 2 PROCESSED IN P21221)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MALTOSE-BINDING PERIPLASMIC PROTEIN,ZONA PELLUCIDA SPERM-
COMPND 3 BINDING PROTEIN 3;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: UNP RESIDUES 27-393,ZP3 ZP-N DOMAIN, UNP RESIDUES 42-143;
COMPND 6 SYNONYM: MBP,MMBP,MALTODEXTRIN-BINDING PROTEIN,SPERM RECEPTOR,ZONA
COMPND 7 PELLUCIDA GLYCOPROTEIN 3,ZP-3,ZONA PELLUCIDA PROTEIN C;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 OTHER_DETAILS: THIS PROTEIN IS A CHIMERA. RESIDUES 2-368 ARE FROM E.
COMPND 11 COLI MALTOSE BINDING PROTEIN (MBP), CORRESPOND TO RESIDUES 27-393 OF
COMPND 12 SWISS-PROT DATABASE ENTRY P0AEX9 AND CONTAIN MUTATIONS I3T, E360A,
COMPND 13 K363A, D364A, R368N (CORRESPONDING TO I28T, E385A, K388A, D389A AND
COMPND 14 R393N IN P0AEX9). RESIDUES 372-473 ARE FROM MOUSE ZP3 PROTEIN AND
COMPND 15 CORRESPOND TO RESIDUES 42-143 OF SWISS-PROT DATABASE ENTRY P10761.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12, MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 83333, 10090;
SOURCE 5 CELLULAR_LOCATION: EXTRACELLULAR MATRIX;
SOURCE 6 GENE: MALE, B4034, JW3994, ZP3, ZP-3, ZPC;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: ORIGAMI B;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PLJMBP4C, PLJDIS1
KEYWDS FERTILIZATION, OOCYTE, EGG COAT, ZONA PELLUCIDA, VITELLINE ENVELOPE,
KEYWDS 2 ZP DOMAIN, EGG-SPERM INTERACTION, SPECIES-SPECIFIC GAMETE
KEYWDS 3 RECOGNITION, SPECIATION, BIODIVERSITY, INFERTILITY, EXTRACELLULAR
KEYWDS 4 MATRIX, IMMUNOGLOBULIN-LIKE FOLD, GLYCOPROTEIN, RECEPTOR, SECRETED,
KEYWDS 5 TRANSMEMBRANE, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR L.JOVINE,M.MONNE
REVDAT 3 17-JAN-24 5OSQ 1 HETSYN
REVDAT 2 29-JUL-20 5OSQ 1 COMPND REMARK HET HETNAM
REVDAT 2 2 1 FORMUL LINK SITE ATOM
REVDAT 1 06-SEP-17 5OSQ 0
JRNL AUTH M.MONNE,L.HAN,T.SCHWEND,S.BURENDAHL,L.JOVINE
JRNL TITL CRYSTAL STRUCTURE OF THE ZP-N DOMAIN OF ZP3 REVEALS THE CORE
JRNL TITL 2 FOLD OF ANIMAL EGG COATS
JRNL REF NATURE V. 456 653 2008
JRNL REFN ISSN 0028-0836
JRNL PMID 19052627
JRNL DOI 10.1038/NATURE07599
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.D.BLEIL,P.M.WASSARMAN
REMARK 1 TITL MAMMALIAN SPERM-EGG INTERACTION: IDENTIFICATION OF A
REMARK 1 TITL 2 GLYCOPROTEIN IN MOUSE EGG ZONAE PELLUCIDAE POSSESSING
REMARK 1 TITL 3 RECEPTOR ACTIVITY FOR SPERM
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 20 873 1980
REMARK 1 REFN ISSN 0092-8674
REMARK 1 PMID 7418009
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.BORK,C.SANDER
REMARK 1 TITL A LARGE DOMAIN COMMON TO SPERM RECEPTORS (ZP2 AND ZP3) AND
REMARK 1 TITL 2 TGF-BETA TYPE III RECEPTOR
REMARK 1 REF FEBS LETT. V. 300 237 1992
REMARK 1 REFN ISSN 0014-5793
REMARK 1 PMID 1313375
REMARK 1 REFERENCE 3
REMARK 1 AUTH L.JOVINE,H.QI,Z.WILLIAMS,E.LITSCHER,P.M.WASSARMAN
REMARK 1 TITL THE ZP DOMAIN IS A CONSERVED MODULE FOR POLYMERIZATION OF
REMARK 1 TITL 2 EXTRACELLULAR PROTEINS
REMARK 1 REF NAT.CELL BIOL. V. 4 457 2002
REMARK 1 REFN ISSN 1465-7392
REMARK 1 PMID 12021773
REMARK 1 DOI 10.1038/NCB802
REMARK 1 REFERENCE 4
REMARK 1 AUTH L.JOVINE,H.QI,Z.WILLIAMS,E.S.LITSCHER,P.M.WASSARMAN
REMARK 1 TITL A DUPLICATED MOTIF CONTROLS ASSEMBLY OF ZONA PELLUCIDA
REMARK 1 TITL 2 DOMAIN PROTEINS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 101 5922 2004
REMARK 1 REFN ISSN 0027-8424
REMARK 1 PMID 15079052
REMARK 1 DOI 10.1073/PNAS.0401600101
REMARK 1 REFERENCE 5
REMARK 1 AUTH L.JOVINE,C.C.DARIE,E.S.LITSCHER,P.M.WASSARMAN
REMARK 1 TITL ZONA PELLUCIDA DOMAIN PROTEINS
REMARK 1 REF ANNU.REV.BIOCHEM. V. 74 83 2005
REMARK 1 REFN ISSN 0066-4154
REMARK 1 PMID 15952882
REMARK 1 DOI 10.1146/ANNUREV.BIOCHEM.74.082803.133039
REMARK 1 REFERENCE 6
REMARK 1 AUTH L.JOVINE,W.G.JANSSEN,E.S.LITSCHER,P.M.WASSARMAN
REMARK 1 TITL THE PLAC1-HOMOLOGY REGION OF THE ZP DOMAIN IS SUFFICIENT FOR
REMARK 1 TITL 2 PROTEIN POLYMERISATION
REMARK 1 REF BMC BIOCHEM. V. 7 11 2006
REMARK 1 REFN ESSN 1471-2091
REMARK 1 PMID 16600035
REMARK 1 DOI 10.1186/1471-2091-7-11
REMARK 1 REFERENCE 7
REMARK 1 AUTH L.HAN,M.MONNE,H.OKUMURA,T.SCHWEND,A.L.CHERRY,D.FLOT,
REMARK 1 AUTH 2 T.MATSUDA,L.JOVINE
REMARK 1 TITL INSIGHTS INTO EGG COAT ASSEMBLY AND EGG-SPERM INTERACTION
REMARK 1 TITL 2 FROM THE X-RAY STRUCTURE OF FULL-LENGTH ZP3.
REMARK 1 REF CELL V. 143 404 2010
REMARK 1 REFN ISSN 1097-4172
REMARK 1 PMID 20970175
REMARK 1 DOI 10.1016/J.CELL.2010.09.041
REMARK 1 REFERENCE 8
REMARK 1 AUTH M.MONNE,L.JOVINE
REMARK 1 TITL A STRUCTURAL VIEW OF EGG COAT ARCHITECTURE AND FUNCTION IN
REMARK 1 TITL 2 FERTILIZATION
REMARK 1 REF BIOL. REPROD. V. 85 661 2011
REMARK 1 REFN ISSN 1529-7268
REMARK 1 PMID 21715714
REMARK 1 DOI 10.1095/BIOLREPROD.111.092098
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12-2829
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.90
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 75143
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.470
REMARK 3 FREE R VALUE TEST SET COUNT : 1857
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 32.9024 - 4.4134 0.99 7625 195 0.1607 0.1881
REMARK 3 2 4.4134 - 3.5043 1.00 7418 186 0.1628 0.2018
REMARK 3 3 3.5043 - 3.0617 1.00 7353 187 0.2162 0.2492
REMARK 3 4 3.0617 - 2.7819 1.00 7335 191 0.2385 0.2791
REMARK 3 5 2.7819 - 2.5826 1.00 7303 184 0.2538 0.2574
REMARK 3 6 2.5826 - 2.4304 1.00 7265 186 0.2665 0.2970
REMARK 3 7 2.4304 - 2.3087 1.00 7266 180 0.2890 0.3111
REMARK 3 8 2.3087 - 2.2083 1.00 7261 187 0.3318 0.3787
REMARK 3 9 2.2083 - 2.1233 1.00 7250 181 0.3499 0.3627
REMARK 3 10 2.1233 - 2.0500 1.00 7210 180 0.3653 0.3808
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.840
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.00
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 : 0.011 7580
REMARK 3 ANGLE : 0.783 10266
REMARK 3 CHIRALITY : 0.046 1152
REMARK 3 PLANARITY : 0.006 1327
REMARK 3 DIHEDRAL : 12.553 2795
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESI 3:371 OR RESI 900)
REMARK 3 ORIGIN FOR THE GROUP (A): 114.3080 89.0011 48.8151
REMARK 3 T TENSOR
REMARK 3 T11: 0.5950 T22: 0.5401
REMARK 3 T33: 0.4903 T12: -0.2424
REMARK 3 T13: 0.0954 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 3.1651 L22: 1.4389
REMARK 3 L33: 0.8479 L12: 0.6391
REMARK 3 L13: 0.9558 L23: 0.2551
REMARK 3 S TENSOR
REMARK 3 S11: -0.3368 S12: 0.5470 S13: 0.6031
REMARK 3 S21: -0.2928 S22: 0.4286 S23: -0.1648
REMARK 3 S31: -0.3835 S32: 0.4813 S33: 0.0189
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESI 372:474
REMARK 3 ORIGIN FOR THE GROUP (A): 104.4415 62.9531 55.1983
REMARK 3 T TENSOR
REMARK 3 T11: 0.4673 T22: 0.4618
REMARK 3 T33: 0.4260 T12: -0.0032
REMARK 3 T13: -0.0300 T23: -0.0832
REMARK 3 L TENSOR
REMARK 3 L11: 0.9447 L22: 0.4358
REMARK 3 L33: 0.3846 L12: 0.2452
REMARK 3 L13: -0.1816 L23: 0.0550
REMARK 3 S TENSOR
REMARK 3 S11: 0.0663 S12: 0.0577 S13: -0.1395
REMARK 3 S21: 0.1197 S22: 0.0523 S23: -0.0461
REMARK 3 S31: 0.0084 S32: 0.0359 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN B AND (RESI 2:371 OR RESI 900)
REMARK 3 ORIGIN FOR THE GROUP (A): 115.3311 43.2975 22.3083
REMARK 3 T TENSOR
REMARK 3 T11: 0.3207 T22: 0.4338
REMARK 3 T33: 0.3355 T12: 0.0448
REMARK 3 T13: -0.0045 T23: -0.0991
REMARK 3 L TENSOR
REMARK 3 L11: 2.0187 L22: 2.4634
REMARK 3 L33: 1.3493 L12: -0.1042
REMARK 3 L13: -0.0883 L23: 1.1043
REMARK 3 S TENSOR
REMARK 3 S11: -0.0841 S12: -0.1629 S13: 0.2160
REMARK 3 S21: -0.0794 S22: -0.1947 S23: 0.3039
REMARK 3 S31: -0.0599 S32: -0.3228 S33: -0.0762
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND RESI 372:473
REMARK 3 ORIGIN FOR THE GROUP (A): 124.8521 16.6897 16.2748
REMARK 3 T TENSOR
REMARK 3 T11: 0.5076 T22: 0.3936
REMARK 3 T33: 0.3931 T12: -0.0328
REMARK 3 T13: -0.0181 T23: 0.0350
REMARK 3 L TENSOR
REMARK 3 L11: 0.8995 L22: 0.5063
REMARK 3 L33: 0.4011 L12: -0.2313
REMARK 3 L13: -0.3427 L23: 0.0766
REMARK 3 S TENSOR
REMARK 3 S11: 0.1052 S12: 0.0376 S13: -0.1603
REMARK 3 S21: -0.0767 S22: -0.1222 S23: -0.0098
REMARK 3 S31: 0.2210 S32: 0.0075 S33: 0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 3 THROUGH 41 OR RESID
REMARK 3 43 THROUGH 344 OR RESID 346 THROUGH 473))
REMARK 3 SELECTION : (CHAIN B AND (RESID 3 THROUGH 41 OR RESID
REMARK 3 43 THROUGH 344 OR RESID 346 THROUGH 473))
REMARK 3 ATOM PAIRS NUMBER : 5614
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5OSQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1200006291.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95350
REMARK 200 MONOCHROMATOR : SI(111) MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS JUN 1, 2017 BUILT=20170720
REMARK 200 DATA SCALING SOFTWARE : XDS JUN 1, 2017 BUILT=20170720
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75254
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.430
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.51
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.38630
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.670
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.6.0
REMARK 200 STARTING MODEL: PDB ENTRY 3D4C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SAMPLE: 15MG/ML PROTEIN IN 0.05M
REMARK 280 SODIUM CHLORIDE, 0.01M TRIS-HCL, PH7.2, 0.001M MALTOSE.
REMARK 280 RESERVOIR: 10% PEG6000, 0.2M CALCIUM CHLORIDE, 0.1M TRIS-HCL,
REMARK 280 PH7.0. SAMPLE TO RESERVOIR RATIO IN DROP: 1:1, PH7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21
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,-Z+1/2
REMARK 290 4555 -X+1/2,-Y,Z+1/2
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 45.67000
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.47500
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.67000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 70.47500
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 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 APPLY THE FOLLOWING TO CHAINS: A, C
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 1
REMARK 465 LYS A 2
REMARK 465 GLU A 475
REMARK 465 HIS A 476
REMARK 465 HIS A 477
REMARK 465 HIS A 478
REMARK 465 HIS A 479
REMARK 465 HIS A 480
REMARK 465 HIS A 481
REMARK 465 MET B 1
REMARK 465 LEU B 474
REMARK 465 GLU B 475
REMARK 465 HIS B 476
REMARK 465 HIS B 477
REMARK 465 HIS B 478
REMARK 465 HIS B 479
REMARK 465 HIS B 480
REMARK 465 HIS B 481
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 HH22 ARG B 355 O HOH B 612 1.58
REMARK 500 H ASN B 101 O HOH B 613 1.59
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 56 -154.21 -110.42
REMARK 500 LEU A 123 80.90 -156.35
REMARK 500 ALA A 169 -82.72 -78.71
REMARK 500 LEU A 458 -131.56 59.57
REMARK 500 ASP B 56 -152.40 -109.99
REMARK 500 LEU B 123 81.36 -156.86
REMARK 500 ALA B 169 -80.91 -77.12
REMARK 500 LYS B 203 30.43 70.19
REMARK 500 GLU B 378 -71.42 -53.45
REMARK 500 LEU B 458 -129.65 60.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 182 O
REMARK 620 2 ASP A 185 OD1 85.6
REMARK 620 3 ASP A 185 OD2 127.4 45.0
REMARK 620 4 GLN A 366 OE1 74.8 93.8 89.2
REMARK 620 5 HOH A 670 O 81.0 157.9 151.7 99.4
REMARK 620 6 HOH A 681 O 110.0 70.6 74.7 162.8 97.6
REMARK 620 7 HOH B 632 O 154.3 120.1 77.6 102.6 74.2 80.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 210 OD2
REMARK 620 2 SER A 212 OG 91.6
REMARK 620 3 ASP A 437 OD1 90.4 160.7
REMARK 620 4 ASP A 437 OD2 87.4 154.7 44.6
REMARK 620 5 HOH A 638 O 134.1 100.3 92.0 63.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 234 OG
REMARK 620 2 LYS A 296 O 146.3
REMARK 620 3 ASP A 297 O 80.0 75.7
REMARK 620 4 HOH A 615 O 143.5 61.9 93.5
REMARK 620 5 HOH A 617 O 61.9 149.5 133.5 101.6
REMARK 620 6 HOH A 630 O 83.7 104.3 61.4 62.3 87.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 703 O
REMARK 620 2 THR B 54 O 79.5
REMARK 620 3 HOH B 662 O 147.3 76.5
REMARK 620 4 HOH B 751 O 110.4 97.5 94.6
REMARK 620 5 HOH B 766 O 79.1 97.0 82.2 163.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 182 O
REMARK 620 2 ASP B 185 OD1 84.3
REMARK 620 3 GLN B 366 OE1 66.0 82.3
REMARK 620 4 HOH B 630 O 67.2 145.6 102.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 234 OG
REMARK 620 2 LYS B 296 O 125.2
REMARK 620 3 ASP B 297 O 75.2 72.7
REMARK 620 4 HOH B 606 O 59.9 71.6 79.9
REMARK 620 5 HOH B 683 O 88.2 119.7 70.3 141.2
REMARK 620 6 HOH B 735 O 162.0 72.1 109.6 137.3 77.7
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3D4C RELATED DB: PDB
REMARK 900 CRYSTAL FORM I OF THE SAME PROTEIN RELATED ENTRIES
REMARK 900 RELATED ID: 3D4G RELATED DB: PDB
REMARK 900 CRYSTAL FORM II OF THE SAME PROTEIN, PROCESSED IN P1
REMARK 900 RELATED ID: 3EF7 RELATED DB: PDB
REMARK 900 CRYSTAL FORM III OF THE SAME PROTEIN
REMARK 900 RELATED ID: 3NK3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FULL-LENGTH CHICKEN ZP3
REMARK 900 RELATED ID: 3NK4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FULL-LENGTH CHICKEN ZP3
DBREF 5OSQ A 2 368 UNP P0AEX9 MALE_ECOLI 27 393
DBREF 5OSQ A 372 473 UNP P10761 ZP3_MOUSE 42 143
DBREF 5OSQ B 2 368 UNP P0AEX9 MALE_ECOLI 27 393
DBREF 5OSQ B 372 473 UNP P10761 ZP3_MOUSE 42 143
SEQADV 5OSQ MET A 1 UNP P0AEX9 INITIATING METHIONINE
SEQADV 5OSQ THR A 3 UNP P0AEX9 ILE 28 ENGINEERED MUTATION
SEQADV 5OSQ ALA A 360 UNP P0AEX9 GLU 385 ENGINEERED MUTATION
SEQADV 5OSQ ALA A 363 UNP P0AEX9 LYS 388 ENGINEERED MUTATION
SEQADV 5OSQ ALA A 364 UNP P0AEX9 ASP 389 ENGINEERED MUTATION
SEQADV 5OSQ ASN A 368 UNP P0AEX9 ARG 393 ENGINEERED MUTATION
SEQADV 5OSQ ALA A 369 UNP P0AEX9 LINKER
SEQADV 5OSQ ALA A 370 UNP P0AEX9 LINKER
SEQADV 5OSQ ALA A 371 UNP P0AEX9 LINKER
SEQADV 5OSQ LEU A 474 UNP P10761 EXPRESSION TAG
SEQADV 5OSQ GLU A 475 UNP P10761 EXPRESSION TAG
SEQADV 5OSQ HIS A 476 UNP P10761 EXPRESSION TAG
SEQADV 5OSQ HIS A 477 UNP P10761 EXPRESSION TAG
SEQADV 5OSQ HIS A 478 UNP P10761 EXPRESSION TAG
SEQADV 5OSQ HIS A 479 UNP P10761 EXPRESSION TAG
SEQADV 5OSQ HIS A 480 UNP P10761 EXPRESSION TAG
SEQADV 5OSQ HIS A 481 UNP P10761 EXPRESSION TAG
SEQADV 5OSQ MET B 1 UNP P0AEX9 INITIATING METHIONINE
SEQADV 5OSQ THR B 3 UNP P0AEX9 ILE 28 ENGINEERED MUTATION
SEQADV 5OSQ ALA B 360 UNP P0AEX9 GLU 385 ENGINEERED MUTATION
SEQADV 5OSQ ALA B 363 UNP P0AEX9 LYS 388 ENGINEERED MUTATION
SEQADV 5OSQ ALA B 364 UNP P0AEX9 ASP 389 ENGINEERED MUTATION
SEQADV 5OSQ ASN B 368 UNP P0AEX9 ARG 393 ENGINEERED MUTATION
SEQADV 5OSQ ALA B 369 UNP P0AEX9 LINKER
SEQADV 5OSQ ALA B 370 UNP P0AEX9 LINKER
SEQADV 5OSQ ALA B 371 UNP P0AEX9 LINKER
SEQADV 5OSQ LEU B 474 UNP P10761 EXPRESSION TAG
SEQADV 5OSQ GLU B 475 UNP P10761 EXPRESSION TAG
SEQADV 5OSQ HIS B 476 UNP P10761 EXPRESSION TAG
SEQADV 5OSQ HIS B 477 UNP P10761 EXPRESSION TAG
SEQADV 5OSQ HIS B 478 UNP P10761 EXPRESSION TAG
SEQADV 5OSQ HIS B 479 UNP P10761 EXPRESSION TAG
SEQADV 5OSQ HIS B 480 UNP P10761 EXPRESSION TAG
SEQADV 5OSQ HIS B 481 UNP P10761 EXPRESSION TAG
SEQRES 1 A 481 MET LYS THR GLU GLU GLY LYS LEU VAL ILE TRP ILE ASN
SEQRES 2 A 481 GLY ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY LYS
SEQRES 3 A 481 LYS PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL GLU
SEQRES 4 A 481 HIS PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL ALA
SEQRES 5 A 481 ALA THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA HIS
SEQRES 6 A 481 ASP ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU ALA
SEQRES 7 A 481 GLU ILE THR PRO ASP LYS ALA PHE GLN ASP LYS LEU TYR
SEQRES 8 A 481 PRO PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS LEU
SEQRES 9 A 481 ILE ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU ILE
SEQRES 10 A 481 TYR ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR TRP
SEQRES 11 A 481 GLU GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA LYS
SEQRES 12 A 481 GLY LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO TYR
SEQRES 13 A 481 PHE THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR ALA
SEQRES 14 A 481 PHE LYS TYR GLU ASN GLY LYS TYR ASP ILE LYS ASP VAL
SEQRES 15 A 481 GLY VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU THR PHE
SEQRES 16 A 481 LEU VAL ASP LEU ILE LYS ASN LYS HIS MET ASN ALA ASP
SEQRES 17 A 481 THR ASP TYR SER ILE ALA GLU ALA ALA PHE ASN LYS GLY
SEQRES 18 A 481 GLU THR ALA MET THR ILE ASN GLY PRO TRP ALA TRP SER
SEQRES 19 A 481 ASN ILE ASP THR SER LYS VAL ASN TYR GLY VAL THR VAL
SEQRES 20 A 481 LEU PRO THR PHE LYS GLY GLN PRO SER LYS PRO PHE VAL
SEQRES 21 A 481 GLY VAL LEU SER ALA GLY ILE ASN ALA ALA SER PRO ASN
SEQRES 22 A 481 LYS GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR LEU LEU
SEQRES 23 A 481 THR ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP LYS PRO
SEQRES 24 A 481 LEU GLY ALA VAL ALA LEU LYS SER TYR GLU GLU GLU LEU
SEQRES 25 A 481 ALA LYS ASP PRO ARG ILE ALA ALA THR MET GLU ASN ALA
SEQRES 26 A 481 GLN LYS GLY GLU ILE MET PRO ASN ILE PRO GLN MET SER
SEQRES 27 A 481 ALA PHE TRP TYR ALA VAL ARG THR ALA VAL ILE ASN ALA
SEQRES 28 A 481 ALA SER GLY ARG GLN THR VAL ASP ALA ALA LEU ALA ALA
SEQRES 29 A 481 ALA GLN THR ASN ALA ALA ALA VAL LYS VAL GLU CYS LEU
SEQRES 30 A 481 GLU ALA GLU LEU VAL VAL THR VAL SER ARG ASP LEU PHE
SEQRES 31 A 481 GLY THR GLY LYS LEU VAL GLN PRO GLY ASP LEU THR LEU
SEQRES 32 A 481 GLY SER GLU GLY CYS GLN PRO ARG VAL SER VAL ASP THR
SEQRES 33 A 481 ASP VAL VAL ARG PHE ASN ALA GLN LEU HIS GLU CYS SER
SEQRES 34 A 481 SER ARG VAL GLN MET THR LYS ASP ALA LEU VAL TYR SER
SEQRES 35 A 481 THR PHE LEU LEU HIS ASP PRO ARG PRO VAL SER GLY LEU
SEQRES 36 A 481 SER ILE LEU ARG THR ASN ARG VAL GLU VAL PRO ILE GLU
SEQRES 37 A 481 CYS ARG TYR PRO ARG LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 481 MET LYS THR GLU GLU GLY LYS LEU VAL ILE TRP ILE ASN
SEQRES 2 B 481 GLY ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY LYS
SEQRES 3 B 481 LYS PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL GLU
SEQRES 4 B 481 HIS PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL ALA
SEQRES 5 B 481 ALA THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA HIS
SEQRES 6 B 481 ASP ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU ALA
SEQRES 7 B 481 GLU ILE THR PRO ASP LYS ALA PHE GLN ASP LYS LEU TYR
SEQRES 8 B 481 PRO PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS LEU
SEQRES 9 B 481 ILE ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU ILE
SEQRES 10 B 481 TYR ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR TRP
SEQRES 11 B 481 GLU GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA LYS
SEQRES 12 B 481 GLY LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO TYR
SEQRES 13 B 481 PHE THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR ALA
SEQRES 14 B 481 PHE LYS TYR GLU ASN GLY LYS TYR ASP ILE LYS ASP VAL
SEQRES 15 B 481 GLY VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU THR PHE
SEQRES 16 B 481 LEU VAL ASP LEU ILE LYS ASN LYS HIS MET ASN ALA ASP
SEQRES 17 B 481 THR ASP TYR SER ILE ALA GLU ALA ALA PHE ASN LYS GLY
SEQRES 18 B 481 GLU THR ALA MET THR ILE ASN GLY PRO TRP ALA TRP SER
SEQRES 19 B 481 ASN ILE ASP THR SER LYS VAL ASN TYR GLY VAL THR VAL
SEQRES 20 B 481 LEU PRO THR PHE LYS GLY GLN PRO SER LYS PRO PHE VAL
SEQRES 21 B 481 GLY VAL LEU SER ALA GLY ILE ASN ALA ALA SER PRO ASN
SEQRES 22 B 481 LYS GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR LEU LEU
SEQRES 23 B 481 THR ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP LYS PRO
SEQRES 24 B 481 LEU GLY ALA VAL ALA LEU LYS SER TYR GLU GLU GLU LEU
SEQRES 25 B 481 ALA LYS ASP PRO ARG ILE ALA ALA THR MET GLU ASN ALA
SEQRES 26 B 481 GLN LYS GLY GLU ILE MET PRO ASN ILE PRO GLN MET SER
SEQRES 27 B 481 ALA PHE TRP TYR ALA VAL ARG THR ALA VAL ILE ASN ALA
SEQRES 28 B 481 ALA SER GLY ARG GLN THR VAL ASP ALA ALA LEU ALA ALA
SEQRES 29 B 481 ALA GLN THR ASN ALA ALA ALA VAL LYS VAL GLU CYS LEU
SEQRES 30 B 481 GLU ALA GLU LEU VAL VAL THR VAL SER ARG ASP LEU PHE
SEQRES 31 B 481 GLY THR GLY LYS LEU VAL GLN PRO GLY ASP LEU THR LEU
SEQRES 32 B 481 GLY SER GLU GLY CYS GLN PRO ARG VAL SER VAL ASP THR
SEQRES 33 B 481 ASP VAL VAL ARG PHE ASN ALA GLN LEU HIS GLU CYS SER
SEQRES 34 B 481 SER ARG VAL GLN MET THR LYS ASP ALA LEU VAL TYR SER
SEQRES 35 B 481 THR PHE LEU LEU HIS ASP PRO ARG PRO VAL SER GLY LEU
SEQRES 36 B 481 SER ILE LEU ARG THR ASN ARG VAL GLU VAL PRO ILE GLU
SEQRES 37 B 481 CYS ARG TYR PRO ARG LEU GLU HIS HIS HIS HIS HIS HIS
HET GLC C 1 22
HET GLC C 2 22
HET GLC D 1 22
HET GLC D 2 22
HET CA A 502 1
HET CA A 503 1
HET CA A 504 1
HET CA B 502 1
HET CA B 503 1
HET CA B 504 1
HET PGE B 505 24
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 3 GLC 4(C6 H12 O6)
FORMUL 5 CA 6(CA 2+)
FORMUL 11 PGE C6 H14 O4
FORMUL 12 HOH *309(H2 O)
HELIX 1 1 TYR A 18 THR A 32 1 15
HELIX 2 2 LEU A 44 ALA A 52 1 9
HELIX 3 3 HIS A 65 GLN A 73 5 9
HELIX 4 4 LYS A 84 LYS A 89 1 6
HELIX 5 5 PRO A 92 VAL A 98 1 7
HELIX 6 6 TRP A 130 LYS A 143 5 14
HELIX 7 7 PRO A 155 ALA A 164 1 10
HELIX 8 8 ALA A 187 LYS A 201 1 15
HELIX 9 9 TYR A 211 LYS A 220 1 10
HELIX 10 10 PRO A 230 SER A 239 5 10
HELIX 11 11 LYS A 274 ASN A 283 1 10
HELIX 12 12 ASP A 288 ASP A 297 1 10
HELIX 13 13 LYS A 306 LEU A 312 1 7
HELIX 14 14 PRO A 316 LYS A 327 1 12
HELIX 15 15 PRO A 335 ALA A 352 5 18
HELIX 16 16 VAL A 358 ALA A 371 1 14
HELIX 17 17 PRO A 398 ASP A 400 5 3
HELIX 18 18 LEU A 425 CYS A 428 1 4
HELIX 19 19 TYR B 18 THR B 32 1 15
HELIX 20 20 LEU B 44 ALA B 52 1 9
HELIX 21 21 HIS B 65 GLN B 73 5 9
HELIX 22 22 LYS B 84 LYS B 89 1 6
HELIX 23 23 PRO B 92 VAL B 98 1 7
HELIX 24 24 TRP B 130 LYS B 143 5 14
HELIX 25 25 PRO B 155 ALA B 164 1 10
HELIX 26 26 ALA B 187 LYS B 201 1 15
HELIX 27 27 TYR B 211 LYS B 220 1 10
HELIX 28 28 PRO B 230 SER B 239 5 10
HELIX 29 29 LYS B 274 ASN B 283 1 10
HELIX 30 30 ASP B 288 ASP B 297 1 10
HELIX 31 31 LYS B 306 LEU B 312 1 7
HELIX 32 32 PRO B 316 LYS B 327 1 12
HELIX 33 33 PRO B 335 ALA B 352 5 18
HELIX 34 34 VAL B 358 ALA B 371 1 14
HELIX 35 35 PRO B 398 ASP B 400 5 3
HELIX 36 36 LEU B 425 CYS B 428 1 4
SHEET 1 A 2 LEU A 8 TRP A 11 0
SHEET 2 A 2 VAL A 36 GLU A 39 1 N THR A 37 O LEU A 8
SHEET 1 B 3 ILE A 60 ALA A 64 0
SHEET 2 B 3 GLY A 261 ILE A 267 -1 N GLY A 266 O ILE A 61
SHEET 3 B 3 TYR A 107 GLU A 112 -1 N GLU A 112 O GLY A 261
SHEET 1 C 3 MET A 225 ASN A 228 0
SHEET 2 C 3 SER A 115 ASN A 119 -1 N ILE A 117 O THR A 226
SHEET 3 C 3 TYR A 243 THR A 246 -1 N THR A 246 O LEU A 116
SHEET 1 D 4 VAL A 372 CYS A 376 0
SHEET 2 D 4 GLU A 380 SER A 386 -1 N THR A 384 O LYS A 373
SHEET 3 D 4 VAL A 418 GLN A 424 -1 N ALA A 423 O LEU A 381
SHEET 4 D 4 ARG A 411 VAL A 414 -1 N SER A 413 O ARG A 420
SHEET 1 E 3 LEU A 401 LEU A 403 0
SHEET 2 E 3 ALA A 438 HIS A 447 -1 N LEU A 446 O THR A 402
SHEET 3 E 3 VAL A 463 PRO A 472 -1 N TYR A 471 O LEU A 439
SHEET 1 F 2 ARG A 431 THR A 435 0
SHEET 2 F 2 LEU A 439 SER A 442 -1 N SER A 442 O ARG A 431
SHEET 1 G 2 LYS B 7 TRP B 11 0
SHEET 2 G 2 LYS B 35 GLU B 39 1 N LYS B 35 O LEU B 8
SHEET 1 H 3 ILE B 60 ALA B 64 0
SHEET 2 H 3 GLY B 261 ILE B 267 -1 N GLY B 266 O ILE B 61
SHEET 3 H 3 TYR B 107 GLU B 112 -1 N GLU B 112 O GLY B 261
SHEET 1 I 3 MET B 225 ASN B 228 0
SHEET 2 I 3 SER B 115 ASN B 119 -1 N ILE B 117 O THR B 226
SHEET 3 I 3 TYR B 243 THR B 246 -1 N THR B 246 O LEU B 116
SHEET 1 J 2 LYS B 171 GLU B 173 0
SHEET 2 J 2 LYS B 176 ASP B 178 -1 N ASP B 178 O LYS B 171
SHEET 1 K 4 VAL B 372 CYS B 376 0
SHEET 2 K 4 GLU B 380 SER B 386 -1 N THR B 384 O LYS B 373
SHEET 3 K 4 VAL B 418 GLN B 424 -1 N ALA B 423 O LEU B 381
SHEET 4 K 4 ARG B 411 VAL B 414 -1 N SER B 413 O ARG B 420
SHEET 1 L 3 LEU B 401 LEU B 403 0
SHEET 2 L 3 ALA B 438 HIS B 447 -1 N LEU B 446 O THR B 402
SHEET 3 L 3 VAL B 463 PRO B 472 -1 N TYR B 471 O LEU B 439
SHEET 1 M 2 ARG B 431 THR B 435 0
SHEET 2 M 2 LEU B 439 SER B 442 -1 N SER B 442 O ARG B 431
SSBOND 1 CYS A 376 CYS A 469 1555 1555 2.03
SSBOND 2 CYS A 408 CYS A 428 1555 1555 2.03
SSBOND 3 CYS B 376 CYS B 469 1555 1555 2.03
SSBOND 4 CYS B 408 CYS B 428 1555 1555 2.02
LINK O4 GLC C 1 C1 GLC C 2 1555 1555 1.41
LINK O4 GLC D 1 C1 GLC D 2 1555 1555 1.40
LINK O VAL A 182 CA CA A 503 1555 1555 2.40
LINK OD1 ASP A 185 CA CA A 503 1555 1555 2.36
LINK OD2 ASP A 185 CA CA A 503 1555 1555 3.10
LINK OD2 ASP A 210 CA CA A 504 1555 1555 2.48
LINK OG SER A 212 CA CA A 504 1555 1555 2.56
LINK OG SER A 234 CA CA A 502 1555 1555 2.46
LINK O LYS A 296 CA CA A 502 1555 1555 2.56
LINK O ASP A 297 CA CA A 502 1555 1555 2.48
LINK OE1 GLN A 366 CA CA A 503 1555 1555 2.43
LINK OD1 ASP A 437 CA CA A 504 1555 1555 3.10
LINK OD2 ASP A 437 CA CA A 504 1555 1555 2.48
LINK CA CA A 502 O HOH A 615 1555 1555 2.26
LINK CA CA A 502 O HOH A 617 1555 1555 2.42
LINK CA CA A 502 O HOH A 630 1555 1555 2.69
LINK CA CA A 503 O HOH A 670 1555 1555 2.41
LINK CA CA A 503 O HOH A 681 1555 1555 2.64
LINK CA CA A 503 O HOH B 632 1555 1555 2.30
LINK CA CA A 504 O HOH A 638 1555 1555 2.53
LINK O HOH A 703 CA CA B 504 3565 1555 2.61
LINK O THR B 54 CA CA B 504 1555 1555 2.37
LINK O VAL B 182 CA CA B 503 1555 1555 2.57
LINK OD1 ASP B 185 CA CA B 503 1555 1555 2.39
LINK OG SER B 234 CA CA B 502 1555 1555 2.43
LINK O LYS B 296 CA CA B 502 1555 1555 2.71
LINK O ASP B 297 CA CA B 502 1555 1555 2.55
LINK OE1 GLN B 366 CA CA B 503 1555 1555 2.43
LINK CA CA B 502 O HOH B 606 1555 1555 2.27
LINK CA CA B 502 O HOH B 683 1555 1555 2.52
LINK CA CA B 502 O HOH B 735 1555 1555 2.45
LINK CA CA B 503 O HOH B 630 1555 1555 2.47
LINK CA CA B 504 O HOH B 662 1555 1555 2.70
LINK CA CA B 504 O HOH B 751 1555 1555 2.41
LINK CA CA B 504 O HOH B 766 1555 1555 2.27
CISPEP 1 ARG A 450 PRO A 451 0 2.16
CISPEP 2 ARG B 450 PRO B 451 0 1.72
CRYST1 91.340 92.160 140.950 90.00 90.00 90.00 P 21 2 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 0.010948 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010851 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007095 0.00000
(ATOM LINES ARE NOT SHOWN.)
END