HEADER CELL ADHESION 26-APR-16 5JKB
TITLE CRYSTAL STRUCTURE OF HUMAN JUNO (CRYSTAL FORM 2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPERM-EGG FUSION PROTEIN JUNO;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: FOLATE RECEPTOR 4,FOLATE RECEPTOR DELTA,FR-DELTA,IZUMO1
COMPND 5 RECEPTOR PROTEIN JUNO;
COMPND 6 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: IZUMO1R, FOLR4, JUNO;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7215
KEYWDS FERTILIZATION, IZUMO1, JUNO, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR U.OHTO,H.ISHIDA,T.SHIMIZU
REVDAT 4 08-NOV-23 5JKB 1 REMARK
REVDAT 3 19-FEB-20 5JKB 1 JRNL REMARK
REVDAT 2 29-JUN-16 5JKB 1 JRNL
REVDAT 1 22-JUN-16 5JKB 0
JRNL AUTH U.OHTO,H.ISHIDA,E.KRAYUKHINA,S.UCHIYAMA,N.INOUE,T.SHIMIZU
JRNL TITL STRUCTURE OF IZUMO1-JUNO REVEALS SPERM-OOCYTE RECOGNITION
JRNL TITL 2 DURING MAMMALIAN FERTILIZATION
JRNL REF NATURE V. 534 566 2016
JRNL REFN ESSN 1476-4687
JRNL PMID 27309808
JRNL DOI 10.1038/NATURE18596
REMARK 2
REMARK 2 RESOLUTION. 3.23 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 13842
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) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 730
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.23
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1026
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.3230
REMARK 3 BIN FREE R VALUE SET COUNT : 44
REMARK 3 BIN FREE R VALUE : 0.3860
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6410
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.72000
REMARK 3 B22 (A**2) : 0.76000
REMARK 3 B33 (A**2) : 0.59000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.49000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.540
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.464
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 64.762
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.909
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6664 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5874 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9080 ; 1.443 ; 1.923
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13606 ; 1.223 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 784 ; 5.937 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 330 ;35.056 ;23.879
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1042 ;15.662 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;19.188 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 880 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7552 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1640 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3160 ; 2.351 ; 5.003
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3159 ; 2.343 ; 5.002
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3936 ; 4.007 ; 7.498
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3937 ; 4.006 ; 7.499
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3504 ; 2.598 ; 5.279
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3502 ; 2.594 ; 5.277
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5144 ; 4.442 ; 7.798
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 27715 ; 8.940 ;47.393
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 27715 ; 8.940 ;47.393
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 18 229 B 18 229 23228 0.06 0.05
REMARK 3 2 A 20 228 C 20 228 23048 0.04 0.05
REMARK 3 3 A 20 228 D 20 228 23026 0.04 0.05
REMARK 3 4 B 20 228 C 20 228 23080 0.05 0.05
REMARK 3 5 B 20 228 D 20 228 23060 0.05 0.05
REMARK 3 6 C 20 229 D 20 229 23324 0.01 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 18 A 229
REMARK 3 ORIGIN FOR THE GROUP (A): 34.1167 -0.4528 1.8659
REMARK 3 T TENSOR
REMARK 3 T11: 0.1233 T22: 0.2116
REMARK 3 T33: 0.0776 T12: 0.0203
REMARK 3 T13: -0.0293 T23: -0.0620
REMARK 3 L TENSOR
REMARK 3 L11: 2.5422 L22: 0.5493
REMARK 3 L33: 2.3692 L12: 0.3951
REMARK 3 L13: 0.6199 L23: 0.8568
REMARK 3 S TENSOR
REMARK 3 S11: 0.0955 S12: 0.1493 S13: 0.0493
REMARK 3 S21: 0.0785 S22: -0.1265 S23: 0.0798
REMARK 3 S31: -0.0460 S32: 0.0437 S33: 0.0311
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 18 B 229
REMARK 3 ORIGIN FOR THE GROUP (A): 10.2780 -32.5205 -10.0961
REMARK 3 T TENSOR
REMARK 3 T11: 0.1457 T22: 0.3011
REMARK 3 T33: 0.0824 T12: -0.0084
REMARK 3 T13: 0.0073 T23: -0.0618
REMARK 3 L TENSOR
REMARK 3 L11: 2.2906 L22: 0.6138
REMARK 3 L33: 2.0823 L12: -0.0508
REMARK 3 L13: -0.9375 L23: -0.7702
REMARK 3 S TENSOR
REMARK 3 S11: -0.0471 S12: 0.2021 S13: 0.0037
REMARK 3 S21: -0.0079 S22: 0.0882 S23: -0.1218
REMARK 3 S31: 0.0368 S32: -0.1360 S33: -0.0411
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 20 C 229
REMARK 3 ORIGIN FOR THE GROUP (A): 39.9338 -41.7631 -18.0474
REMARK 3 T TENSOR
REMARK 3 T11: 0.1202 T22: 0.1846
REMARK 3 T33: 0.2136 T12: 0.0258
REMARK 3 T13: 0.0849 T23: -0.1288
REMARK 3 L TENSOR
REMARK 3 L11: 2.0471 L22: 2.4723
REMARK 3 L33: 1.5010 L12: -0.7263
REMARK 3 L13: -1.1279 L23: -0.7023
REMARK 3 S TENSOR
REMARK 3 S11: -0.1646 S12: -0.1742 S13: -0.2077
REMARK 3 S21: -0.0763 S22: 0.0062 S23: -0.1012
REMARK 3 S31: -0.0199 S32: 0.0364 S33: 0.1584
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 20 D 229
REMARK 3 ORIGIN FOR THE GROUP (A): 65.1092 -35.8969 -32.2426
REMARK 3 T TENSOR
REMARK 3 T11: 0.0913 T22: 0.1531
REMARK 3 T33: 0.2153 T12: -0.0012
REMARK 3 T13: 0.0136 T23: -0.1216
REMARK 3 L TENSOR
REMARK 3 L11: 3.4095 L22: 2.2427
REMARK 3 L33: 0.9134 L12: 0.1407
REMARK 3 L13: -0.7291 L23: 1.2322
REMARK 3 S TENSOR
REMARK 3 S11: 0.1780 S12: -0.1879 S13: 0.1195
REMARK 3 S21: -0.0611 S22: -0.0493 S23: -0.0157
REMARK 3 S31: -0.0598 S32: 0.0556 S33: -0.1286
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5JKB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220776.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NE3A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14574
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.230
REMARK 200 RESOLUTION RANGE LOW (A) : 44.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 5JKA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3% (W/V) PEG4000, 5% 2-PROPANOL, 0.1 M
REMARK 280 HEPES-NAOH PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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+1/2
REMARK 290 4555 -X+1/2,Y+1/2,-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 41.90842
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.28950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 53.67668
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 41.90842
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 44.28950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 53.67668
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 TOTAL BURIED SURFACE AREA: 130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ARG A 16
REMARK 465 SER A 17
REMARK 465 VAL A 110
REMARK 465 GLY A 111
REMARK 465 SER A 112
REMARK 465 LEU A 113
REMARK 465 GLY A 114
REMARK 465 TRP A 115
REMARK 465 GLU A 116
REMARK 465 VAL A 117
REMARK 465 ALA A 118
REMARK 465 PRO A 119
REMARK 465 SER A 120
REMARK 465 GLY A 121
REMARK 465 GLN A 122
REMARK 465 PHE A 230
REMARK 465 LEU A 231
REMARK 465 GLU A 232
REMARK 465 VAL A 233
REMARK 465 LEU A 234
REMARK 465 PHE A 235
REMARK 465 GLN A 236
REMARK 465 ARG B 16
REMARK 465 SER B 17
REMARK 465 VAL B 110
REMARK 465 GLY B 111
REMARK 465 SER B 112
REMARK 465 LEU B 113
REMARK 465 GLY B 114
REMARK 465 TRP B 115
REMARK 465 GLU B 116
REMARK 465 VAL B 117
REMARK 465 ALA B 118
REMARK 465 PRO B 119
REMARK 465 SER B 120
REMARK 465 GLY B 121
REMARK 465 GLN B 122
REMARK 465 PHE B 230
REMARK 465 LEU B 231
REMARK 465 GLU B 232
REMARK 465 VAL B 233
REMARK 465 LEU B 234
REMARK 465 PHE B 235
REMARK 465 GLN B 236
REMARK 465 ARG C 16
REMARK 465 SER C 17
REMARK 465 PRO C 18
REMARK 465 TRP C 19
REMARK 465 VAL C 110
REMARK 465 GLY C 111
REMARK 465 SER C 112
REMARK 465 LEU C 113
REMARK 465 GLY C 114
REMARK 465 TRP C 115
REMARK 465 GLU C 116
REMARK 465 VAL C 117
REMARK 465 ALA C 118
REMARK 465 PRO C 119
REMARK 465 SER C 120
REMARK 465 GLY C 121
REMARK 465 GLN C 122
REMARK 465 PHE C 230
REMARK 465 LEU C 231
REMARK 465 GLU C 232
REMARK 465 VAL C 233
REMARK 465 LEU C 234
REMARK 465 PHE C 235
REMARK 465 GLN C 236
REMARK 465 ARG D 16
REMARK 465 SER D 17
REMARK 465 PRO D 18
REMARK 465 TRP D 19
REMARK 465 VAL D 110
REMARK 465 GLY D 111
REMARK 465 SER D 112
REMARK 465 LEU D 113
REMARK 465 GLY D 114
REMARK 465 TRP D 115
REMARK 465 GLU D 116
REMARK 465 VAL D 117
REMARK 465 ALA D 118
REMARK 465 PRO D 119
REMARK 465 SER D 120
REMARK 465 GLY D 121
REMARK 465 GLN D 122
REMARK 465 PHE D 230
REMARK 465 LEU D 231
REMARK 465 GLU D 232
REMARK 465 VAL D 233
REMARK 465 LEU D 234
REMARK 465 PHE D 235
REMARK 465 GLN D 236
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 OD1 ASN A 29 OG SER C 160 1.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU B 22 OE1 GLN D 171 4554 1.69
REMARK 500 OE2 GLU B 22 CD GLN D 171 4554 1.78
REMARK 500 O MET A 145 OH TYR D 44 3455 1.89
REMARK 500 OE2 GLU B 22 CG GLN D 171 4554 1.95
REMARK 500 CG ASP D 41 OD2 ASP D 158 4654 2.04
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 B 87 NE - CZ - NH2 ANGL. DEV. = -3.0 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 GLU A 45 -112.98 38.96
REMARK 500 ASN A 53 97.61 -168.88
REMARK 500 GLU B 45 -113.64 38.29
REMARK 500 ASN B 53 97.01 -168.83
REMARK 500 GLU C 45 -113.85 38.59
REMARK 500 ASN C 53 97.53 -168.81
REMARK 500 GLU D 45 -113.10 38.97
REMARK 500 ASN D 53 97.15 -168.14
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JKE RELATED DB: PDB
REMARK 900 RELATED ID: 5JKD RELATED DB: PDB
REMARK 900 RELATED ID: 5JKC RELATED DB: PDB
REMARK 900 RELATED ID: 5JKA RELATED DB: PDB
REMARK 900 RELATED ID: 5JK9 RELATED DB: PDB
DBREF 5JKB A 20 228 UNP A6ND01 JUNO_HUMAN 20 228
DBREF 5JKB B 20 228 UNP A6ND01 JUNO_HUMAN 20 228
DBREF 5JKB C 20 228 UNP A6ND01 JUNO_HUMAN 20 228
DBREF 5JKB D 20 228 UNP A6ND01 JUNO_HUMAN 20 228
SEQADV 5JKB ARG A 16 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB SER A 17 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB PRO A 18 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB TRP A 19 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB GLU A 229 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB PHE A 230 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB LEU A 231 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB GLU A 232 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB VAL A 233 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB LEU A 234 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB PHE A 235 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB GLN A 236 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB ARG B 16 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB SER B 17 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB PRO B 18 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB TRP B 19 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB GLU B 229 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB PHE B 230 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB LEU B 231 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB GLU B 232 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB VAL B 233 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB LEU B 234 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB PHE B 235 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB GLN B 236 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB ARG C 16 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB SER C 17 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB PRO C 18 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB TRP C 19 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB GLU C 229 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB PHE C 230 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB LEU C 231 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB GLU C 232 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB VAL C 233 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB LEU C 234 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB PHE C 235 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB GLN C 236 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB ARG D 16 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB SER D 17 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB PRO D 18 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB TRP D 19 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB GLU D 229 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB PHE D 230 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB LEU D 231 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB GLU D 232 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB VAL D 233 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB LEU D 234 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB PHE D 235 UNP A6ND01 EXPRESSION TAG
SEQADV 5JKB GLN D 236 UNP A6ND01 EXPRESSION TAG
SEQRES 1 A 221 ARG SER PRO TRP GLY ASP GLU LEU LEU ASN ILE CYS MET
SEQRES 2 A 221 ASN ALA LYS HIS HIS LYS ARG VAL PRO SER PRO GLU ASP
SEQRES 3 A 221 LYS LEU TYR GLU GLU CYS ILE PRO TRP LYS ASP ASN ALA
SEQRES 4 A 221 CYS CYS THR LEU THR THR SER TRP GLU ALA HIS LEU ASP
SEQRES 5 A 221 VAL SER PRO LEU TYR ASN PHE SER LEU PHE HIS CYS GLY
SEQRES 6 A 221 LEU LEU MET PRO GLY CYS ARG LYS HIS PHE ILE GLN ALA
SEQRES 7 A 221 ILE CYS PHE TYR GLU CYS SER PRO ASN LEU GLY PRO TRP
SEQRES 8 A 221 ILE GLN PRO VAL GLY SER LEU GLY TRP GLU VAL ALA PRO
SEQRES 9 A 221 SER GLY GLN GLY GLU ARG VAL VAL ASN VAL PRO LEU CYS
SEQRES 10 A 221 GLN GLU ASP CYS GLU GLU TRP TRP GLU ASP CYS ARG MET
SEQRES 11 A 221 SER TYR THR CYS LYS SER ASN TRP ARG GLY GLY TRP ASP
SEQRES 12 A 221 TRP SER GLN GLY LYS ASN ARG CYS PRO LYS GLY ALA GLN
SEQRES 13 A 221 CYS LEU PRO PHE SER HIS TYR PHE PRO THR PRO ALA ASP
SEQRES 14 A 221 LEU CYS GLU LYS THR TRP SER ASN SER PHE LYS ALA SER
SEQRES 15 A 221 PRO GLU ARG ARG ASN SER GLY ARG CYS LEU GLN LYS TRP
SEQRES 16 A 221 PHE GLU PRO ALA GLN GLY ASN PRO ASN VAL ALA VAL ALA
SEQRES 17 A 221 ARG LEU PHE ALA SER GLU PHE LEU GLU VAL LEU PHE GLN
SEQRES 1 B 221 ARG SER PRO TRP GLY ASP GLU LEU LEU ASN ILE CYS MET
SEQRES 2 B 221 ASN ALA LYS HIS HIS LYS ARG VAL PRO SER PRO GLU ASP
SEQRES 3 B 221 LYS LEU TYR GLU GLU CYS ILE PRO TRP LYS ASP ASN ALA
SEQRES 4 B 221 CYS CYS THR LEU THR THR SER TRP GLU ALA HIS LEU ASP
SEQRES 5 B 221 VAL SER PRO LEU TYR ASN PHE SER LEU PHE HIS CYS GLY
SEQRES 6 B 221 LEU LEU MET PRO GLY CYS ARG LYS HIS PHE ILE GLN ALA
SEQRES 7 B 221 ILE CYS PHE TYR GLU CYS SER PRO ASN LEU GLY PRO TRP
SEQRES 8 B 221 ILE GLN PRO VAL GLY SER LEU GLY TRP GLU VAL ALA PRO
SEQRES 9 B 221 SER GLY GLN GLY GLU ARG VAL VAL ASN VAL PRO LEU CYS
SEQRES 10 B 221 GLN GLU ASP CYS GLU GLU TRP TRP GLU ASP CYS ARG MET
SEQRES 11 B 221 SER TYR THR CYS LYS SER ASN TRP ARG GLY GLY TRP ASP
SEQRES 12 B 221 TRP SER GLN GLY LYS ASN ARG CYS PRO LYS GLY ALA GLN
SEQRES 13 B 221 CYS LEU PRO PHE SER HIS TYR PHE PRO THR PRO ALA ASP
SEQRES 14 B 221 LEU CYS GLU LYS THR TRP SER ASN SER PHE LYS ALA SER
SEQRES 15 B 221 PRO GLU ARG ARG ASN SER GLY ARG CYS LEU GLN LYS TRP
SEQRES 16 B 221 PHE GLU PRO ALA GLN GLY ASN PRO ASN VAL ALA VAL ALA
SEQRES 17 B 221 ARG LEU PHE ALA SER GLU PHE LEU GLU VAL LEU PHE GLN
SEQRES 1 C 221 ARG SER PRO TRP GLY ASP GLU LEU LEU ASN ILE CYS MET
SEQRES 2 C 221 ASN ALA LYS HIS HIS LYS ARG VAL PRO SER PRO GLU ASP
SEQRES 3 C 221 LYS LEU TYR GLU GLU CYS ILE PRO TRP LYS ASP ASN ALA
SEQRES 4 C 221 CYS CYS THR LEU THR THR SER TRP GLU ALA HIS LEU ASP
SEQRES 5 C 221 VAL SER PRO LEU TYR ASN PHE SER LEU PHE HIS CYS GLY
SEQRES 6 C 221 LEU LEU MET PRO GLY CYS ARG LYS HIS PHE ILE GLN ALA
SEQRES 7 C 221 ILE CYS PHE TYR GLU CYS SER PRO ASN LEU GLY PRO TRP
SEQRES 8 C 221 ILE GLN PRO VAL GLY SER LEU GLY TRP GLU VAL ALA PRO
SEQRES 9 C 221 SER GLY GLN GLY GLU ARG VAL VAL ASN VAL PRO LEU CYS
SEQRES 10 C 221 GLN GLU ASP CYS GLU GLU TRP TRP GLU ASP CYS ARG MET
SEQRES 11 C 221 SER TYR THR CYS LYS SER ASN TRP ARG GLY GLY TRP ASP
SEQRES 12 C 221 TRP SER GLN GLY LYS ASN ARG CYS PRO LYS GLY ALA GLN
SEQRES 13 C 221 CYS LEU PRO PHE SER HIS TYR PHE PRO THR PRO ALA ASP
SEQRES 14 C 221 LEU CYS GLU LYS THR TRP SER ASN SER PHE LYS ALA SER
SEQRES 15 C 221 PRO GLU ARG ARG ASN SER GLY ARG CYS LEU GLN LYS TRP
SEQRES 16 C 221 PHE GLU PRO ALA GLN GLY ASN PRO ASN VAL ALA VAL ALA
SEQRES 17 C 221 ARG LEU PHE ALA SER GLU PHE LEU GLU VAL LEU PHE GLN
SEQRES 1 D 221 ARG SER PRO TRP GLY ASP GLU LEU LEU ASN ILE CYS MET
SEQRES 2 D 221 ASN ALA LYS HIS HIS LYS ARG VAL PRO SER PRO GLU ASP
SEQRES 3 D 221 LYS LEU TYR GLU GLU CYS ILE PRO TRP LYS ASP ASN ALA
SEQRES 4 D 221 CYS CYS THR LEU THR THR SER TRP GLU ALA HIS LEU ASP
SEQRES 5 D 221 VAL SER PRO LEU TYR ASN PHE SER LEU PHE HIS CYS GLY
SEQRES 6 D 221 LEU LEU MET PRO GLY CYS ARG LYS HIS PHE ILE GLN ALA
SEQRES 7 D 221 ILE CYS PHE TYR GLU CYS SER PRO ASN LEU GLY PRO TRP
SEQRES 8 D 221 ILE GLN PRO VAL GLY SER LEU GLY TRP GLU VAL ALA PRO
SEQRES 9 D 221 SER GLY GLN GLY GLU ARG VAL VAL ASN VAL PRO LEU CYS
SEQRES 10 D 221 GLN GLU ASP CYS GLU GLU TRP TRP GLU ASP CYS ARG MET
SEQRES 11 D 221 SER TYR THR CYS LYS SER ASN TRP ARG GLY GLY TRP ASP
SEQRES 12 D 221 TRP SER GLN GLY LYS ASN ARG CYS PRO LYS GLY ALA GLN
SEQRES 13 D 221 CYS LEU PRO PHE SER HIS TYR PHE PRO THR PRO ALA ASP
SEQRES 14 D 221 LEU CYS GLU LYS THR TRP SER ASN SER PHE LYS ALA SER
SEQRES 15 D 221 PRO GLU ARG ARG ASN SER GLY ARG CYS LEU GLN LYS TRP
SEQRES 16 D 221 PHE GLU PRO ALA GLN GLY ASN PRO ASN VAL ALA VAL ALA
SEQRES 17 D 221 ARG LEU PHE ALA SER GLU PHE LEU GLU VAL LEU PHE GLN
HET CL A 301 1
HET CL B 301 1
HET CL C 301 1
HET CL D 301 1
HETNAM CL CHLORIDE ION
FORMUL 5 CL 4(CL 1-)
HELIX 1 AA1 TRP A 19 LEU A 24 5 6
HELIX 2 AA2 TYR A 44 LYS A 51 5 8
HELIX 3 AA3 THR A 57 HIS A 65 1 9
HELIX 4 AA4 MET A 83 SER A 100 1 18
HELIX 5 AA5 LEU A 103 PRO A 105 5 3
HELIX 6 AA6 CYS A 132 ARG A 144 1 13
HELIX 7 AA7 PHE A 175 PHE A 179 1 5
HELIX 8 AA8 THR A 181 THR A 189 1 9
HELIX 9 AA9 GLU A 212 GLY A 216 5 5
HELIX 10 AB1 ASN A 219 GLU A 229 1 11
HELIX 11 AB2 TRP B 19 LEU B 24 5 6
HELIX 12 AB3 TYR B 44 LYS B 51 5 8
HELIX 13 AB4 THR B 57 LEU B 66 1 10
HELIX 14 AB5 MET B 83 SER B 100 1 18
HELIX 15 AB6 LEU B 103 PRO B 105 5 3
HELIX 16 AB7 CYS B 132 ARG B 144 1 13
HELIX 17 AB8 PHE B 175 PHE B 179 1 5
HELIX 18 AB9 THR B 181 THR B 189 1 9
HELIX 19 AC1 GLU B 212 GLY B 216 5 5
HELIX 20 AC2 ASN B 219 ALA B 227 1 9
HELIX 21 AC3 GLY C 20 LEU C 24 5 5
HELIX 22 AC4 TYR C 44 LYS C 51 5 8
HELIX 23 AC5 THR C 57 HIS C 65 1 9
HELIX 24 AC6 MET C 83 SER C 100 1 18
HELIX 25 AC7 LEU C 103 PRO C 105 5 3
HELIX 26 AC8 CYS C 132 ARG C 144 1 13
HELIX 27 AC9 PHE C 175 PHE C 179 1 5
HELIX 28 AD1 THR C 181 THR C 189 1 9
HELIX 29 AD2 GLU C 212 GLY C 216 5 5
HELIX 30 AD3 ASN C 219 GLU C 229 1 11
HELIX 31 AD4 GLY D 20 LEU D 24 5 5
HELIX 32 AD5 TYR D 44 LYS D 51 5 8
HELIX 33 AD6 THR D 57 HIS D 65 1 9
HELIX 34 AD7 MET D 83 SER D 100 1 18
HELIX 35 AD8 LEU D 103 PRO D 105 5 3
HELIX 36 AD9 CYS D 132 ARG D 144 1 13
HELIX 37 AE1 PHE D 175 PHE D 179 1 5
HELIX 38 AE2 THR D 181 THR D 189 1 9
HELIX 39 AE3 GLU D 212 GLY D 216 5 5
HELIX 40 AE4 ASN D 219 GLU D 229 1 11
SHEET 1 AA1 2 ILE A 107 GLN A 108 0
SHEET 2 AA1 2 ARG A 125 VAL A 126 -1 O ARG A 125 N GLN A 108
SHEET 1 AA2 2 VAL A 129 LEU A 131 0
SHEET 2 AA2 2 PHE A 194 ALA A 196 1 O LYS A 195 N LEU A 131
SHEET 1 AA3 2 TYR A 147 THR A 148 0
SHEET 2 AA3 2 LEU A 173 PRO A 174 -1 O LEU A 173 N THR A 148
SHEET 1 AA4 2 ILE B 107 GLN B 108 0
SHEET 2 AA4 2 ARG B 125 VAL B 126 -1 O ARG B 125 N GLN B 108
SHEET 1 AA5 2 VAL B 129 LEU B 131 0
SHEET 2 AA5 2 PHE B 194 ALA B 196 1 O LYS B 195 N LEU B 131
SHEET 1 AA6 2 TYR B 147 THR B 148 0
SHEET 2 AA6 2 LEU B 173 PRO B 174 -1 O LEU B 173 N THR B 148
SHEET 1 AA7 2 ILE C 107 GLN C 108 0
SHEET 2 AA7 2 ARG C 125 VAL C 126 -1 O ARG C 125 N GLN C 108
SHEET 1 AA8 2 VAL C 129 LEU C 131 0
SHEET 2 AA8 2 PHE C 194 ALA C 196 1 O LYS C 195 N LEU C 131
SHEET 1 AA9 2 TYR C 147 THR C 148 0
SHEET 2 AA9 2 LEU C 173 PRO C 174 -1 O LEU C 173 N THR C 148
SHEET 1 AB1 2 ILE D 107 GLN D 108 0
SHEET 2 AB1 2 ARG D 125 VAL D 126 -1 O ARG D 125 N GLN D 108
SHEET 1 AB2 2 VAL D 129 LEU D 131 0
SHEET 2 AB2 2 PHE D 194 ALA D 196 1 O LYS D 195 N LEU D 131
SHEET 1 AB3 2 TYR D 147 THR D 148 0
SHEET 2 AB3 2 LEU D 173 PRO D 174 -1 O LEU D 173 N THR D 148
SSBOND 1 CYS A 27 CYS A 55 1555 1555 2.04
SSBOND 2 CYS A 47 CYS A 95 1555 1555 2.04
SSBOND 3 CYS A 56 CYS A 99 1555 1555 2.02
SSBOND 4 CYS A 79 CYS A 172 1555 1555 2.06
SSBOND 5 CYS A 86 CYS A 143 1555 1555 2.03
SSBOND 6 CYS A 132 CYS A 206 1555 1555 2.04
SSBOND 7 CYS A 136 CYS A 186 1555 1555 2.05
SSBOND 8 CYS A 149 CYS A 166 1555 1555 2.05
SSBOND 9 CYS B 27 CYS B 55 1555 1555 2.04
SSBOND 10 CYS B 47 CYS B 95 1555 1555 2.05
SSBOND 11 CYS B 56 CYS B 99 1555 1555 2.03
SSBOND 12 CYS B 79 CYS B 172 1555 1555 2.05
SSBOND 13 CYS B 86 CYS B 143 1555 1555 2.04
SSBOND 14 CYS B 132 CYS B 206 1555 1555 2.04
SSBOND 15 CYS B 136 CYS B 186 1555 1555 2.06
SSBOND 16 CYS B 149 CYS B 166 1555 1555 2.05
SSBOND 17 CYS C 27 CYS C 55 1555 1555 2.04
SSBOND 18 CYS C 47 CYS C 95 1555 1555 2.05
SSBOND 19 CYS C 56 CYS C 99 1555 1555 2.03
SSBOND 20 CYS C 79 CYS C 172 1555 1555 2.05
SSBOND 21 CYS C 86 CYS C 143 1555 1555 2.02
SSBOND 22 CYS C 132 CYS C 206 1555 1555 2.04
SSBOND 23 CYS C 136 CYS C 186 1555 1555 2.05
SSBOND 24 CYS C 149 CYS C 166 1555 1555 2.05
SSBOND 25 CYS D 27 CYS D 55 1555 1555 2.04
SSBOND 26 CYS D 47 CYS D 95 1555 1555 2.04
SSBOND 27 CYS D 56 CYS D 99 1555 1555 2.02
SSBOND 28 CYS D 79 CYS D 172 1555 1555 2.06
SSBOND 29 CYS D 86 CYS D 143 1555 1555 2.02
SSBOND 30 CYS D 132 CYS D 206 1555 1555 2.05
SSBOND 31 CYS D 136 CYS D 186 1555 1555 2.04
SSBOND 32 CYS D 149 CYS D 166 1555 1555 2.05
SITE 1 AC1 5 TRP A 50 SER A 100 ASN A 102 ASN A 217
SITE 2 AC1 5 ASN A 219
SITE 1 AC2 5 TRP B 50 SER B 100 ASN B 102 ASN B 217
SITE 2 AC2 5 ASN B 219
SITE 1 AC3 5 TRP C 50 SER C 100 ASN C 102 ASN C 217
SITE 2 AC3 5 ASN C 219
SITE 1 AC4 5 TRP D 50 SER D 100 ASN D 102 ASN D 217
SITE 2 AC4 5 ASN D 219
CRYST1 96.770 88.579 108.132 90.00 96.88 90.00 I 1 2 1 16
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 0.010334 0.000000 0.001247 0.00000
SCALE2 0.000000 0.011289 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009315 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
