HEADER HYDROLASE 18-FEB-11 2YA7
TITLE CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANA (TIGR4)
TITLE 2 IN COMPLEX WITH ZANAMIVIR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEURAMINIDASE A;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 280-754;
COMPND 5 SYNONYM: NANA;
COMPND 6 EC: 3.2.1.18;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: THE SEQUENCE NUMBERING ABOVE CORRESPONDS TO THE
COMPND 9 CLOSEST UNIPROT SEQUENCE MATCH UNP B2DJD9. THE SEQUENCE NUMBERING
COMPND 10 FOR THE ENTRY SHOULD BE 303-777
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 170187;
SOURCE 4 STRAIN: TIGR4;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS HYDROLASE, SIALIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.GUT,G.XU,G.L.TAYLOR,M.A.WALSH
REVDAT 2 08-JUN-11 2YA7 1 JRNL
REVDAT 1 27-APR-11 2YA7 0
JRNL AUTH H.GUT,G.XU,G.L.TAYLOR,M.A.WALSH
JRNL TITL STRUCTURAL BASIS FOR STREPTOCOCCUS PNEUMONIAE NANA
JRNL TITL 2 INHIBITION BY INFLUENZA ANTIVIRALS ZANAMIVIR AND
JRNL TITL 3 OSELTAMIVIR CARBOXYLATE.
JRNL REF J.MOL.BIOL. V. 409 496 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21514303
JRNL DOI 10.1016/J.JMB.2011.04.016
REMARK 2
REMARK 2 RESOLUTION. 1.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.00
REMARK 3 NUMBER OF REFLECTIONS : 145055
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) : 0.20881
REMARK 3 R VALUE (WORKING SET) : 0.20759
REMARK 3 FREE R VALUE : 0.25692
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.5
REMARK 3 FREE R VALUE TEST SET COUNT : 3718
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) : 1.892
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.941
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9712
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.266
REMARK 3 BIN FREE R VALUE SET COUNT : 233
REMARK 3 BIN FREE R VALUE : 0.315
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14992
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 1297
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.4
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.432
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00
REMARK 3 B22 (A**2) : 0.00
REMARK 3 B33 (A**2) : 0.00
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.180
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.165
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.120
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.027
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15425 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20870 ; 1.249 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1907 ; 6.472 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 747 ;34.789 ;24.458
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2693 ;13.880 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 99 ;13.568 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2198 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11887 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7413 ; 0.191 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 10426 ; 0.302 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1578 ; 0.138 ; 0.200
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): 37 ; 0.189 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.272 ; 0.200
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): 9642 ; 0.688 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15127 ; 1.171 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6653 ; 1.508 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5743 ; 2.319 ; 4.500
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2YA7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-FEB-11.
REMARK 100 THE PDBE ID CODE IS EBI-47420.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-07
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 : 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) : 0.976
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL CUT
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (MX-225)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200 DATA SCALING SOFTWARE : HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 148783
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.90
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 200 DATA REDUNDANCY : 2.1
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.9
REMARK 200 R MERGE FOR SHELL (I) : 0.28
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.50
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: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.5
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 200 MM KFORMATE,
REMARK 280 20 MM TRIS PH 7.5 .
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 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 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 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 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 ALA A 285
REMARK 465 HIS A 286
REMARK 465 HIS A 287
REMARK 465 HIS A 288
REMARK 465 HIS A 289
REMARK 465 HIS A 290
REMARK 465 HIS A 291
REMARK 465 SER A 292
REMARK 465 SER A 293
REMARK 465 GLY A 294
REMARK 465 LEU A 295
REMARK 465 GLU A 296
REMARK 465 VAL A 297
REMARK 465 LEU A 298
REMARK 465 PHE A 299
REMARK 465 GLN A 300
REMARK 465 GLY A 301
REMARK 465 PRO A 302
REMARK 465 PRO A 303
REMARK 465 GLU A 304
REMARK 465 GLY A 305
REMARK 465 ALA A 306
REMARK 465 LYS A 776
REMARK 465 ASN A 777
REMARK 465 ALA B 285
REMARK 465 HIS B 286
REMARK 465 HIS B 287
REMARK 465 HIS B 288
REMARK 465 HIS B 289
REMARK 465 HIS B 290
REMARK 465 HIS B 291
REMARK 465 SER B 292
REMARK 465 SER B 293
REMARK 465 GLY B 294
REMARK 465 LEU B 295
REMARK 465 GLU B 296
REMARK 465 VAL B 297
REMARK 465 LEU B 298
REMARK 465 PHE B 299
REMARK 465 GLN B 300
REMARK 465 GLY B 301
REMARK 465 PRO B 302
REMARK 465 PRO B 303
REMARK 465 GLU B 304
REMARK 465 GLY B 305
REMARK 465 ALA B 306
REMARK 465 SER B 775
REMARK 465 LYS B 776
REMARK 465 ASN B 777
REMARK 465 ALA C 285
REMARK 465 HIS C 286
REMARK 465 HIS C 287
REMARK 465 HIS C 288
REMARK 465 HIS C 289
REMARK 465 HIS C 290
REMARK 465 HIS C 291
REMARK 465 SER C 292
REMARK 465 SER C 293
REMARK 465 GLY C 294
REMARK 465 LEU C 295
REMARK 465 GLU C 296
REMARK 465 VAL C 297
REMARK 465 LEU C 298
REMARK 465 PHE C 299
REMARK 465 GLN C 300
REMARK 465 GLY C 301
REMARK 465 PRO C 302
REMARK 465 PRO C 303
REMARK 465 GLU C 304
REMARK 465 GLY C 305
REMARK 465 ALA C 306
REMARK 465 ASN C 777
REMARK 465 ALA D 285
REMARK 465 HIS D 286
REMARK 465 HIS D 287
REMARK 465 HIS D 288
REMARK 465 HIS D 289
REMARK 465 HIS D 290
REMARK 465 HIS D 291
REMARK 465 SER D 292
REMARK 465 SER D 293
REMARK 465 GLY D 294
REMARK 465 LEU D 295
REMARK 465 GLU D 296
REMARK 465 VAL D 297
REMARK 465 LEU D 298
REMARK 465 PHE D 299
REMARK 465 GLN D 300
REMARK 465 GLY D 301
REMARK 465 PRO D 302
REMARK 465 PRO D 303
REMARK 465 GLU D 304
REMARK 465 GLY D 305
REMARK 465 ALA D 306
REMARK 465 ASN D 777
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 O HOH C 2036 O HOH C 2041 2.03
REMARK 500 O HOH A 2047 O HOH A 2051 2.03
REMARK 500 NH1 ARG C 672 O HOH C 2291 2.07
REMARK 500 OD1 ASN C 383 O HOH C 2036 2.14
REMARK 500 OG SER D 765 O HOH D 2303 2.16
REMARK 500 ND2 ASN A 383 O HOH A 2047 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 ILE A 333 69.70 70.97
REMARK 500 HIS A 354 -179.65 -172.00
REMARK 500 ASP A 357 35.00 -88.43
REMARK 500 TRP A 358 -169.96 -167.51
REMARK 500 ASP A 402 117.71 71.95
REMARK 500 LYS A 412 -0.59 73.98
REMARK 500 ARG A 461 -160.29 -112.03
REMARK 500 ALA A 486 15.28 55.69
REMARK 500 LYS A 549 -81.11 -92.24
REMARK 500 SER A 581 -3.63 -141.04
REMARK 500 HIS A 582 -125.53 45.62
REMARK 500 THR A 631 -115.10 -120.03
REMARK 500 TYR A 680 70.06 72.79
REMARK 500 LYS A 705 -158.15 -104.98
REMARK 500 ASN A 708 64.34 65.54
REMARK 500 GLN A 731 111.44 -161.49
REMARK 500 ALA A 736 -113.92 -135.61
REMARK 500 LYS A 757 75.45 16.74
REMARK 500 ILE B 333 67.77 67.33
REMARK 500 SER B 355 50.92 -106.13
REMARK 500 ASP B 357 39.04 -90.57
REMARK 500 TRP B 358 -170.86 -170.46
REMARK 500 ASP B 402 113.23 66.89
REMARK 500 ARG B 461 -150.79 -110.62
REMARK 500 ASP B 481 78.68 -119.58
REMARK 500 LYS B 549 -87.46 -89.44
REMARK 500 HIS B 582 -123.46 46.66
REMARK 500 ASP B 614 65.71 35.59
REMARK 500 THR B 631 -120.08 -123.69
REMARK 500 TYR B 680 65.55 89.03
REMARK 500 LYS B 705 -168.39 -109.05
REMARK 500 ASN B 708 84.15 49.35
REMARK 500 GLN B 731 109.88 -165.74
REMARK 500 ALA B 736 -115.35 -131.63
REMARK 500 ASN B 745 -117.40 -111.22
REMARK 500 ILE C 333 69.28 72.33
REMARK 500 ASP C 357 39.26 -92.75
REMARK 500 TRP C 358 -170.09 -171.53
REMARK 500 ASP C 402 115.47 73.02
REMARK 500 ARG C 461 -164.86 -109.38
REMARK 500 LYS C 549 -83.91 -88.75
REMARK 500 HIS C 582 -124.78 42.96
REMARK 500 THR C 631 -114.37 -118.80
REMARK 500 TYR C 680 71.12 72.47
REMARK 500 LYS C 705 -153.28 -105.36
REMARK 500 ASN C 708 67.81 64.66
REMARK 500 ALA C 736 -116.52 -136.71
REMARK 500 SER C 775 37.77 -94.38
REMARK 500 ILE D 333 68.29 68.66
REMARK 500 SER D 355 49.89 -102.29
REMARK 500
REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS.
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 ZMR A1776
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1777
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMR B1776
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1777
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMR C1776
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C1777
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMR D1776
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D1777
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2YA4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANA (TIGR4)
REMARK 900 RELATED ID: 2YA8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANA (TIGR4)
REMARK 900 IN COMPLEX WITH OSELTAMIVIR CARBOXYLATE
REMARK 900 RELATED ID: 2YA6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANA (TIGR4)
REMARK 900 IN COMPLEX WITH DANA
REMARK 900 RELATED ID: 2YA5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANA (TIGR4)
REMARK 900 IN COMPLEX WITH SIALIC ACID
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 HYPOTHETICAL PROTEIN SPNET_02001817 STREPTOCOCCUS
REMARK 999 PNEUMONIAE TIGR4. APPARENT CONFLICTS ARE DUE TO CURRENT
REMARK 999 UNIPROT MAPPING. SEQUENCE REFERENCE: UNIREF100_UPI00005582E2.
DBREF 2YA7 A 303 777 UNP B2DJD9 B2DJD9_STRPN 280 754
DBREF 2YA7 B 303 777 UNP B2DJD9 B2DJD9_STRPN 280 754
DBREF 2YA7 C 303 777 UNP B2DJD9 B2DJD9_STRPN 280 754
DBREF 2YA7 D 303 777 UNP B2DJD9 B2DJD9_STRPN 280 754
SEQADV 2YA7 ALA A 285 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS A 286 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS A 287 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS A 288 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS A 289 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS A 290 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS A 291 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 SER A 292 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 SER A 293 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 GLY A 294 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 LEU A 295 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 GLU A 296 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 VAL A 297 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 LEU A 298 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 PHE A 299 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 GLN A 300 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 GLY A 301 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 PRO A 302 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 LYS A 440 UNP B2DJD9 GLU 417 SEE REMARK 999
SEQADV 2YA7 ASP A 584 UNP B2DJD9 ASN 561 SEE REMARK 999
SEQADV 2YA7 ALA B 285 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS B 286 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS B 287 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS B 288 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS B 289 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS B 290 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS B 291 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 SER B 292 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 SER B 293 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 GLY B 294 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 LEU B 295 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 GLU B 296 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 VAL B 297 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 LEU B 298 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 PHE B 299 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 GLN B 300 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 GLY B 301 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 PRO B 302 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 LYS B 440 UNP B2DJD9 GLU 417 SEE REMARK 999
SEQADV 2YA7 ASP B 584 UNP B2DJD9 ASN 561 SEE REMARK 999
SEQADV 2YA7 ALA C 285 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS C 286 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS C 287 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS C 288 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS C 289 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS C 290 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS C 291 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 SER C 292 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 SER C 293 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 GLY C 294 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 LEU C 295 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 GLU C 296 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 VAL C 297 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 LEU C 298 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 PHE C 299 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 GLN C 300 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 GLY C 301 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 PRO C 302 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 LYS C 440 UNP B2DJD9 GLU 417 SEE REMARK 999
SEQADV 2YA7 ASP C 584 UNP B2DJD9 ASN 561 SEE REMARK 999
SEQADV 2YA7 ALA D 285 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS D 286 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS D 287 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS D 288 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS D 289 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS D 290 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 HIS D 291 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 SER D 292 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 SER D 293 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 GLY D 294 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 LEU D 295 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 GLU D 296 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 VAL D 297 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 LEU D 298 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 PHE D 299 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 GLN D 300 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 GLY D 301 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 PRO D 302 UNP B2DJD9 EXPRESSION TAG
SEQADV 2YA7 LYS D 440 UNP B2DJD9 GLU 417 SEE REMARK 999
SEQADV 2YA7 ASP D 584 UNP B2DJD9 ASN 561 SEE REMARK 999
SEQRES 1 A 493 ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU VAL
SEQRES 2 A 493 LEU PHE GLN GLY PRO PRO GLU GLY ALA ALA LEU THR GLU
SEQRES 3 A 493 LYS THR ASP ILE PHE GLU SER GLY ARG ASN GLY ASN PRO
SEQRES 4 A 493 ASN LYS ASP GLY ILE LYS SER TYR ARG ILE PRO ALA LEU
SEQRES 5 A 493 LEU LYS THR ASP LYS GLY THR LEU ILE ALA GLY ALA ASP
SEQRES 6 A 493 GLU ARG ARG LEU HIS SER SER ASP TRP GLY ASP ILE GLY
SEQRES 7 A 493 MET VAL ILE ARG ARG SER GLU ASP ASN GLY LYS THR TRP
SEQRES 8 A 493 GLY ASP ARG VAL THR ILE THR ASN LEU ARG ASP ASN PRO
SEQRES 9 A 493 LYS ALA SER ASP PRO SER ILE GLY SER PRO VAL ASN ILE
SEQRES 10 A 493 ASP MET VAL LEU VAL GLN ASP PRO GLU THR LYS ARG ILE
SEQRES 11 A 493 PHE SER ILE TYR ASP MET PHE PRO GLU GLY LYS GLY ILE
SEQRES 12 A 493 PHE GLY MET SER SER GLN LYS GLU GLU ALA TYR LYS LYS
SEQRES 13 A 493 ILE ASP GLY LYS THR TYR GLN ILE LEU TYR ARG GLU GLY
SEQRES 14 A 493 GLU LYS GLY ALA TYR THR ILE ARG GLU ASN GLY THR VAL
SEQRES 15 A 493 TYR THR PRO ASP GLY LYS ALA THR ASP TYR ARG VAL VAL
SEQRES 16 A 493 VAL ASP PRO VAL LYS PRO ALA TYR SER ASP LYS GLY ASP
SEQRES 17 A 493 LEU TYR LYS GLY ASP GLN LEU LEU GLY ASN ILE TYR PHE
SEQRES 18 A 493 THR THR ASN LYS THR SER PRO PHE ARG ILE ALA LYS ASP
SEQRES 19 A 493 SER TYR LEU TRP MET SER TYR SER ASP ASP ASP GLY LYS
SEQRES 20 A 493 THR TRP SER ALA PRO GLN ASP ILE THR PRO MET VAL LYS
SEQRES 21 A 493 ALA ASP TRP MET LYS PHE LEU GLY VAL GLY PRO GLY THR
SEQRES 22 A 493 GLY ILE VAL LEU ARG ASN GLY PRO HIS LYS GLY ARG ILE
SEQRES 23 A 493 LEU ILE PRO VAL TYR THR THR ASN ASN VAL SER HIS LEU
SEQRES 24 A 493 ASP GLY SER GLN SER SER ARG VAL ILE TYR SER ASP ASP
SEQRES 25 A 493 HIS GLY LYS THR TRP HIS ALA GLY GLU ALA VAL ASN ASP
SEQRES 26 A 493 ASN ARG GLN VAL ASP GLY GLN LYS ILE HIS SER SER THR
SEQRES 27 A 493 MET ASN ASN ARG ARG ALA GLN ASN THR GLU SER THR VAL
SEQRES 28 A 493 VAL GLN LEU ASN ASN GLY ASP VAL LYS LEU PHE MET ARG
SEQRES 29 A 493 GLY LEU THR GLY ASP LEU GLN VAL ALA THR SER LYS ASP
SEQRES 30 A 493 GLY GLY VAL THR TRP GLU LYS ASP ILE LYS ARG TYR PRO
SEQRES 31 A 493 GLN VAL LYS ASP VAL TYR VAL GLN MET SER ALA ILE HIS
SEQRES 32 A 493 THR MET HIS GLU GLY LYS GLU TYR ILE ILE LEU SER ASN
SEQRES 33 A 493 ALA GLY GLY PRO LYS ARG GLU ASN GLY MET VAL HIS LEU
SEQRES 34 A 493 ALA ARG VAL GLU GLU ASN GLY GLU LEU THR TRP LEU LYS
SEQRES 35 A 493 HIS ASN PRO ILE GLN LYS GLY GLU PHE ALA TYR ASN SER
SEQRES 36 A 493 LEU GLN GLU LEU GLY ASN GLY GLU TYR GLY ILE LEU TYR
SEQRES 37 A 493 GLU HIS THR GLU LYS GLY GLN ASN ALA TYR THR LEU SER
SEQRES 38 A 493 PHE ARG LYS PHE ASN TRP GLU PHE LEU SER LYS ASN
SEQRES 1 B 493 ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU VAL
SEQRES 2 B 493 LEU PHE GLN GLY PRO PRO GLU GLY ALA ALA LEU THR GLU
SEQRES 3 B 493 LYS THR ASP ILE PHE GLU SER GLY ARG ASN GLY ASN PRO
SEQRES 4 B 493 ASN LYS ASP GLY ILE LYS SER TYR ARG ILE PRO ALA LEU
SEQRES 5 B 493 LEU LYS THR ASP LYS GLY THR LEU ILE ALA GLY ALA ASP
SEQRES 6 B 493 GLU ARG ARG LEU HIS SER SER ASP TRP GLY ASP ILE GLY
SEQRES 7 B 493 MET VAL ILE ARG ARG SER GLU ASP ASN GLY LYS THR TRP
SEQRES 8 B 493 GLY ASP ARG VAL THR ILE THR ASN LEU ARG ASP ASN PRO
SEQRES 9 B 493 LYS ALA SER ASP PRO SER ILE GLY SER PRO VAL ASN ILE
SEQRES 10 B 493 ASP MET VAL LEU VAL GLN ASP PRO GLU THR LYS ARG ILE
SEQRES 11 B 493 PHE SER ILE TYR ASP MET PHE PRO GLU GLY LYS GLY ILE
SEQRES 12 B 493 PHE GLY MET SER SER GLN LYS GLU GLU ALA TYR LYS LYS
SEQRES 13 B 493 ILE ASP GLY LYS THR TYR GLN ILE LEU TYR ARG GLU GLY
SEQRES 14 B 493 GLU LYS GLY ALA TYR THR ILE ARG GLU ASN GLY THR VAL
SEQRES 15 B 493 TYR THR PRO ASP GLY LYS ALA THR ASP TYR ARG VAL VAL
SEQRES 16 B 493 VAL ASP PRO VAL LYS PRO ALA TYR SER ASP LYS GLY ASP
SEQRES 17 B 493 LEU TYR LYS GLY ASP GLN LEU LEU GLY ASN ILE TYR PHE
SEQRES 18 B 493 THR THR ASN LYS THR SER PRO PHE ARG ILE ALA LYS ASP
SEQRES 19 B 493 SER TYR LEU TRP MET SER TYR SER ASP ASP ASP GLY LYS
SEQRES 20 B 493 THR TRP SER ALA PRO GLN ASP ILE THR PRO MET VAL LYS
SEQRES 21 B 493 ALA ASP TRP MET LYS PHE LEU GLY VAL GLY PRO GLY THR
SEQRES 22 B 493 GLY ILE VAL LEU ARG ASN GLY PRO HIS LYS GLY ARG ILE
SEQRES 23 B 493 LEU ILE PRO VAL TYR THR THR ASN ASN VAL SER HIS LEU
SEQRES 24 B 493 ASP GLY SER GLN SER SER ARG VAL ILE TYR SER ASP ASP
SEQRES 25 B 493 HIS GLY LYS THR TRP HIS ALA GLY GLU ALA VAL ASN ASP
SEQRES 26 B 493 ASN ARG GLN VAL ASP GLY GLN LYS ILE HIS SER SER THR
SEQRES 27 B 493 MET ASN ASN ARG ARG ALA GLN ASN THR GLU SER THR VAL
SEQRES 28 B 493 VAL GLN LEU ASN ASN GLY ASP VAL LYS LEU PHE MET ARG
SEQRES 29 B 493 GLY LEU THR GLY ASP LEU GLN VAL ALA THR SER LYS ASP
SEQRES 30 B 493 GLY GLY VAL THR TRP GLU LYS ASP ILE LYS ARG TYR PRO
SEQRES 31 B 493 GLN VAL LYS ASP VAL TYR VAL GLN MET SER ALA ILE HIS
SEQRES 32 B 493 THR MET HIS GLU GLY LYS GLU TYR ILE ILE LEU SER ASN
SEQRES 33 B 493 ALA GLY GLY PRO LYS ARG GLU ASN GLY MET VAL HIS LEU
SEQRES 34 B 493 ALA ARG VAL GLU GLU ASN GLY GLU LEU THR TRP LEU LYS
SEQRES 35 B 493 HIS ASN PRO ILE GLN LYS GLY GLU PHE ALA TYR ASN SER
SEQRES 36 B 493 LEU GLN GLU LEU GLY ASN GLY GLU TYR GLY ILE LEU TYR
SEQRES 37 B 493 GLU HIS THR GLU LYS GLY GLN ASN ALA TYR THR LEU SER
SEQRES 38 B 493 PHE ARG LYS PHE ASN TRP GLU PHE LEU SER LYS ASN
SEQRES 1 C 493 ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU VAL
SEQRES 2 C 493 LEU PHE GLN GLY PRO PRO GLU GLY ALA ALA LEU THR GLU
SEQRES 3 C 493 LYS THR ASP ILE PHE GLU SER GLY ARG ASN GLY ASN PRO
SEQRES 4 C 493 ASN LYS ASP GLY ILE LYS SER TYR ARG ILE PRO ALA LEU
SEQRES 5 C 493 LEU LYS THR ASP LYS GLY THR LEU ILE ALA GLY ALA ASP
SEQRES 6 C 493 GLU ARG ARG LEU HIS SER SER ASP TRP GLY ASP ILE GLY
SEQRES 7 C 493 MET VAL ILE ARG ARG SER GLU ASP ASN GLY LYS THR TRP
SEQRES 8 C 493 GLY ASP ARG VAL THR ILE THR ASN LEU ARG ASP ASN PRO
SEQRES 9 C 493 LYS ALA SER ASP PRO SER ILE GLY SER PRO VAL ASN ILE
SEQRES 10 C 493 ASP MET VAL LEU VAL GLN ASP PRO GLU THR LYS ARG ILE
SEQRES 11 C 493 PHE SER ILE TYR ASP MET PHE PRO GLU GLY LYS GLY ILE
SEQRES 12 C 493 PHE GLY MET SER SER GLN LYS GLU GLU ALA TYR LYS LYS
SEQRES 13 C 493 ILE ASP GLY LYS THR TYR GLN ILE LEU TYR ARG GLU GLY
SEQRES 14 C 493 GLU LYS GLY ALA TYR THR ILE ARG GLU ASN GLY THR VAL
SEQRES 15 C 493 TYR THR PRO ASP GLY LYS ALA THR ASP TYR ARG VAL VAL
SEQRES 16 C 493 VAL ASP PRO VAL LYS PRO ALA TYR SER ASP LYS GLY ASP
SEQRES 17 C 493 LEU TYR LYS GLY ASP GLN LEU LEU GLY ASN ILE TYR PHE
SEQRES 18 C 493 THR THR ASN LYS THR SER PRO PHE ARG ILE ALA LYS ASP
SEQRES 19 C 493 SER TYR LEU TRP MET SER TYR SER ASP ASP ASP GLY LYS
SEQRES 20 C 493 THR TRP SER ALA PRO GLN ASP ILE THR PRO MET VAL LYS
SEQRES 21 C 493 ALA ASP TRP MET LYS PHE LEU GLY VAL GLY PRO GLY THR
SEQRES 22 C 493 GLY ILE VAL LEU ARG ASN GLY PRO HIS LYS GLY ARG ILE
SEQRES 23 C 493 LEU ILE PRO VAL TYR THR THR ASN ASN VAL SER HIS LEU
SEQRES 24 C 493 ASP GLY SER GLN SER SER ARG VAL ILE TYR SER ASP ASP
SEQRES 25 C 493 HIS GLY LYS THR TRP HIS ALA GLY GLU ALA VAL ASN ASP
SEQRES 26 C 493 ASN ARG GLN VAL ASP GLY GLN LYS ILE HIS SER SER THR
SEQRES 27 C 493 MET ASN ASN ARG ARG ALA GLN ASN THR GLU SER THR VAL
SEQRES 28 C 493 VAL GLN LEU ASN ASN GLY ASP VAL LYS LEU PHE MET ARG
SEQRES 29 C 493 GLY LEU THR GLY ASP LEU GLN VAL ALA THR SER LYS ASP
SEQRES 30 C 493 GLY GLY VAL THR TRP GLU LYS ASP ILE LYS ARG TYR PRO
SEQRES 31 C 493 GLN VAL LYS ASP VAL TYR VAL GLN MET SER ALA ILE HIS
SEQRES 32 C 493 THR MET HIS GLU GLY LYS GLU TYR ILE ILE LEU SER ASN
SEQRES 33 C 493 ALA GLY GLY PRO LYS ARG GLU ASN GLY MET VAL HIS LEU
SEQRES 34 C 493 ALA ARG VAL GLU GLU ASN GLY GLU LEU THR TRP LEU LYS
SEQRES 35 C 493 HIS ASN PRO ILE GLN LYS GLY GLU PHE ALA TYR ASN SER
SEQRES 36 C 493 LEU GLN GLU LEU GLY ASN GLY GLU TYR GLY ILE LEU TYR
SEQRES 37 C 493 GLU HIS THR GLU LYS GLY GLN ASN ALA TYR THR LEU SER
SEQRES 38 C 493 PHE ARG LYS PHE ASN TRP GLU PHE LEU SER LYS ASN
SEQRES 1 D 493 ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU VAL
SEQRES 2 D 493 LEU PHE GLN GLY PRO PRO GLU GLY ALA ALA LEU THR GLU
SEQRES 3 D 493 LYS THR ASP ILE PHE GLU SER GLY ARG ASN GLY ASN PRO
SEQRES 4 D 493 ASN LYS ASP GLY ILE LYS SER TYR ARG ILE PRO ALA LEU
SEQRES 5 D 493 LEU LYS THR ASP LYS GLY THR LEU ILE ALA GLY ALA ASP
SEQRES 6 D 493 GLU ARG ARG LEU HIS SER SER ASP TRP GLY ASP ILE GLY
SEQRES 7 D 493 MET VAL ILE ARG ARG SER GLU ASP ASN GLY LYS THR TRP
SEQRES 8 D 493 GLY ASP ARG VAL THR ILE THR ASN LEU ARG ASP ASN PRO
SEQRES 9 D 493 LYS ALA SER ASP PRO SER ILE GLY SER PRO VAL ASN ILE
SEQRES 10 D 493 ASP MET VAL LEU VAL GLN ASP PRO GLU THR LYS ARG ILE
SEQRES 11 D 493 PHE SER ILE TYR ASP MET PHE PRO GLU GLY LYS GLY ILE
SEQRES 12 D 493 PHE GLY MET SER SER GLN LYS GLU GLU ALA TYR LYS LYS
SEQRES 13 D 493 ILE ASP GLY LYS THR TYR GLN ILE LEU TYR ARG GLU GLY
SEQRES 14 D 493 GLU LYS GLY ALA TYR THR ILE ARG GLU ASN GLY THR VAL
SEQRES 15 D 493 TYR THR PRO ASP GLY LYS ALA THR ASP TYR ARG VAL VAL
SEQRES 16 D 493 VAL ASP PRO VAL LYS PRO ALA TYR SER ASP LYS GLY ASP
SEQRES 17 D 493 LEU TYR LYS GLY ASP GLN LEU LEU GLY ASN ILE TYR PHE
SEQRES 18 D 493 THR THR ASN LYS THR SER PRO PHE ARG ILE ALA LYS ASP
SEQRES 19 D 493 SER TYR LEU TRP MET SER TYR SER ASP ASP ASP GLY LYS
SEQRES 20 D 493 THR TRP SER ALA PRO GLN ASP ILE THR PRO MET VAL LYS
SEQRES 21 D 493 ALA ASP TRP MET LYS PHE LEU GLY VAL GLY PRO GLY THR
SEQRES 22 D 493 GLY ILE VAL LEU ARG ASN GLY PRO HIS LYS GLY ARG ILE
SEQRES 23 D 493 LEU ILE PRO VAL TYR THR THR ASN ASN VAL SER HIS LEU
SEQRES 24 D 493 ASP GLY SER GLN SER SER ARG VAL ILE TYR SER ASP ASP
SEQRES 25 D 493 HIS GLY LYS THR TRP HIS ALA GLY GLU ALA VAL ASN ASP
SEQRES 26 D 493 ASN ARG GLN VAL ASP GLY GLN LYS ILE HIS SER SER THR
SEQRES 27 D 493 MET ASN ASN ARG ARG ALA GLN ASN THR GLU SER THR VAL
SEQRES 28 D 493 VAL GLN LEU ASN ASN GLY ASP VAL LYS LEU PHE MET ARG
SEQRES 29 D 493 GLY LEU THR GLY ASP LEU GLN VAL ALA THR SER LYS ASP
SEQRES 30 D 493 GLY GLY VAL THR TRP GLU LYS ASP ILE LYS ARG TYR PRO
SEQRES 31 D 493 GLN VAL LYS ASP VAL TYR VAL GLN MET SER ALA ILE HIS
SEQRES 32 D 493 THR MET HIS GLU GLY LYS GLU TYR ILE ILE LEU SER ASN
SEQRES 33 D 493 ALA GLY GLY PRO LYS ARG GLU ASN GLY MET VAL HIS LEU
SEQRES 34 D 493 ALA ARG VAL GLU GLU ASN GLY GLU LEU THR TRP LEU LYS
SEQRES 35 D 493 HIS ASN PRO ILE GLN LYS GLY GLU PHE ALA TYR ASN SER
SEQRES 36 D 493 LEU GLN GLU LEU GLY ASN GLY GLU TYR GLY ILE LEU TYR
SEQRES 37 D 493 GLU HIS THR GLU LYS GLY GLN ASN ALA TYR THR LEU SER
SEQRES 38 D 493 PHE ARG LYS PHE ASN TRP GLU PHE LEU SER LYS ASN
HET ZMR A1776 23
HET CL A1777 1
HET ZMR B1776 23
HET CL B1777 1
HET ZMR C1776 23
HET CL C1777 1
HET ZMR D1776 23
HET CL D1777 1
HETNAM ZMR ZANAMIVIR
HETNAM CL CHLORIDE ION
HETSYN ZMR MODIFIED SIALIC ACID
FORMUL 5 ZMR 4(C12 H20 N4 O7)
FORMUL 6 CL 4(CL 1-)
FORMUL 7 HOH *1297(H2 O)
HELIX 1 1 ASP A 392 GLY A 396 5 5
HELIX 2 2 LYS A 425 MET A 430 5 6
HELIX 3 3 LYS A 484 SER A 488 5 5
HELIX 4 4 ILE A 539 LYS A 544 1 6
HELIX 5 5 SER A 581 SER A 586 1 6
HELIX 6 6 ASN A 625 GLN A 629 5 5
HELIX 7 7 TRP A 771 SER A 775 1 5
HELIX 8 8 ASP B 392 GLY B 396 5 5
HELIX 9 9 LYS B 425 MET B 430 5 6
HELIX 10 10 LYS B 484 SER B 488 5 5
HELIX 11 11 ILE B 539 LYS B 544 1 6
HELIX 12 12 SER B 581 SER B 586 1 6
HELIX 13 13 ASP C 392 GLY C 396 5 5
HELIX 14 14 LYS C 425 MET C 430 5 6
HELIX 15 15 LYS C 484 SER C 488 5 5
HELIX 16 16 ILE C 539 LYS C 544 1 6
HELIX 17 17 SER C 581 SER C 586 1 6
HELIX 18 18 ASN C 625 GLN C 629 5 5
HELIX 19 19 TRP C 771 SER C 775 1 5
HELIX 20 20 ASP D 392 GLY D 396 5 5
HELIX 21 21 LYS D 425 MET D 430 5 6
HELIX 22 22 LYS D 484 SER D 488 5 5
HELIX 23 23 ILE D 539 LYS D 544 1 6
HELIX 24 24 SER D 581 SER D 586 1 6
HELIX 25 25 ASN D 625 GLN D 629 5 5
HELIX 26 26 TRP D 771 LYS D 776 1 6
SHEET 1 AA 4 THR A 312 PHE A 315 0
SHEET 2 AA 4 THR A 763 ASN A 770 -1 O LEU A 764 N ILE A 314
SHEET 3 AA 4 GLU A 747 HIS A 754 -1 O TYR A 748 N PHE A 769
SHEET 4 AA 4 ASN A 738 GLY A 744 -1 O SER A 739 N LEU A 751
SHEET 1 AB 4 SER A 330 LYS A 338 0
SHEET 2 AB 4 LEU A 344 ARG A 351 -1 O ILE A 345 N LEU A 337
SHEET 3 AB 4 ILE A 361 SER A 368 -1 O GLY A 362 N GLU A 350
SHEET 4 AB 4 VAL A 379 THR A 382 -1 O VAL A 379 N ILE A 365
SHEET 1 AC 5 GLN A 537 ASP A 538 0
SHEET 2 AC 5 TYR A 520 SER A 526 -1 O MET A 523 N GLN A 537
SHEET 3 AC 5 ILE A 414 PHE A 421 -1 O ILE A 414 N SER A 526
SHEET 4 AC 5 VAL A 399 GLN A 407 -1 O VAL A 399 N PHE A 421
SHEET 5 AC 5 GLY A 556 THR A 557 1 O GLY A 556 N LEU A 405
SHEET 1 AD 2 TYR A 438 ILE A 441 0
SHEET 2 AD 2 LYS A 444 ARG A 451 -1 O LYS A 444 N ILE A 441
SHEET 1 AE 7 GLN A 498 ASN A 502 0
SHEET 2 AE 7 ASP A 492 LYS A 495 -1 O LEU A 493 N LEU A 500
SHEET 3 AE 7 ALA A 473 VAL A 478 -1 O ARG A 477 N TYR A 494
SHEET 4 AE 7 THR A 465 TYR A 467 -1 O VAL A 466 N THR A 474
SHEET 5 AE 7 TYR A 458 ILE A 460 -1 O THR A 459 N TYR A 467
SHEET 6 AE 7 LYS A 444 ARG A 451 -1 O GLN A 447 N ILE A 460
SHEET 7 AE 7 PHE A 513 ARG A 514 1 O ARG A 514 N TYR A 450
SHEET 1 AF 7 GLN A 498 ASN A 502 0
SHEET 2 AF 7 ASP A 492 LYS A 495 -1 O LEU A 493 N LEU A 500
SHEET 3 AF 7 ALA A 473 VAL A 478 -1 O ARG A 477 N TYR A 494
SHEET 4 AF 7 THR A 465 TYR A 467 -1 O VAL A 466 N THR A 474
SHEET 5 AF 7 TYR A 458 ILE A 460 -1 O THR A 459 N TYR A 467
SHEET 6 AF 7 LYS A 444 ARG A 451 -1 O GLN A 447 N ILE A 460
SHEET 7 AF 7 TYR A 438 ILE A 441 -1 O LYS A 439 N TYR A 446
SHEET 1 AG 2 PHE A 513 ARG A 514 0
SHEET 2 AG 2 LYS A 444 ARG A 451 1 O TYR A 450 N ARG A 514
SHEET 1 AH 2 LEU A 551 VAL A 553 0
SHEET 2 AH 2 ILE A 570 THR A 576 -1 O TYR A 575 N GLY A 552
SHEET 1 AI 2 ILE A 559 VAL A 560 0
SHEET 2 AI 2 ILE A 570 THR A 576 1 O LEU A 571 N ILE A 559
SHEET 1 AJ 4 HIS A 602 ALA A 603 0
SHEET 2 AJ 4 SER A 588 SER A 594 -1 O TYR A 593 N HIS A 602
SHEET 3 AJ 4 ILE A 570 THR A 576 -1 O ILE A 570 N SER A 594
SHEET 4 AJ 4 ILE A 559 VAL A 560 1 O ILE A 559 N LEU A 571
SHEET 1 AK 4 HIS A 602 ALA A 603 0
SHEET 2 AK 4 SER A 588 SER A 594 -1 O TYR A 593 N HIS A 602
SHEET 3 AK 4 ILE A 570 THR A 576 -1 O ILE A 570 N SER A 594
SHEET 4 AK 4 LEU A 551 VAL A 553 -1 O GLY A 552 N TYR A 575
SHEET 1 AL 2 ARG A 611 VAL A 613 0
SHEET 2 AL 2 GLN A 616 ILE A 618 -1 O GLN A 616 N VAL A 613
SHEET 1 AM 4 SER A 633 GLN A 637 0
SHEET 2 AM 4 VAL A 643 MET A 647 -1 O LYS A 644 N VAL A 636
SHEET 3 AM 4 ASP A 653 SER A 659 -1 O GLN A 655 N MET A 647
SHEET 4 AM 4 LYS A 671 LYS A 677 -1 O LYS A 671 N VAL A 656
SHEET 1 AN 4 SER A 684 HIS A 690 0
SHEET 2 AN 4 LYS A 693 ALA A 701 -1 O LYS A 693 N HIS A 690
SHEET 3 AN 4 GLU A 707 VAL A 716 -1 O MET A 710 N ASN A 700
SHEET 4 AN 4 LEU A 722 GLU A 734 -1 O THR A 723 N ARG A 715
SHEET 1 BA 4 THR B 312 PHE B 315 0
SHEET 2 BA 4 THR B 763 ASN B 770 -1 O LEU B 764 N ILE B 314
SHEET 3 BA 4 GLU B 747 HIS B 754 -1 O TYR B 748 N PHE B 769
SHEET 4 BA 4 ASN B 738 GLU B 742 -1 O SER B 739 N LEU B 751
SHEET 1 BB 4 SER B 330 LYS B 338 0
SHEET 2 BB 4 LEU B 344 ARG B 351 -1 O ILE B 345 N LEU B 337
SHEET 3 BB 4 ILE B 361 SER B 368 -1 O GLY B 362 N GLU B 350
SHEET 4 BB 4 VAL B 379 THR B 382 -1 O VAL B 379 N ILE B 365
SHEET 1 BC 5 GLN B 537 ASP B 538 0
SHEET 2 BC 5 TYR B 520 SER B 526 -1 O MET B 523 N GLN B 537
SHEET 3 BC 5 ILE B 414 PHE B 421 -1 O ILE B 414 N SER B 526
SHEET 4 BC 5 VAL B 399 GLN B 407 -1 O VAL B 399 N PHE B 421
SHEET 5 BC 5 GLY B 556 THR B 557 1 O GLY B 556 N LEU B 405
SHEET 1 BD 2 TYR B 438 ILE B 441 0
SHEET 2 BD 2 LYS B 444 ARG B 451 -1 O LYS B 444 N ILE B 441
SHEET 1 BE 7 GLN B 498 ASN B 502 0
SHEET 2 BE 7 ASP B 492 LYS B 495 -1 O LEU B 493 N LEU B 500
SHEET 3 BE 7 ALA B 473 VAL B 478 -1 O ARG B 477 N TYR B 494
SHEET 4 BE 7 THR B 465 TYR B 467 -1 O VAL B 466 N THR B 474
SHEET 5 BE 7 TYR B 458 ILE B 460 -1 O THR B 459 N TYR B 467
SHEET 6 BE 7 LYS B 444 ARG B 451 -1 O GLN B 447 N ILE B 460
SHEET 7 BE 7 PHE B 513 ARG B 514 1 O ARG B 514 N TYR B 450
SHEET 1 BF 7 GLN B 498 ASN B 502 0
SHEET 2 BF 7 ASP B 492 LYS B 495 -1 O LEU B 493 N LEU B 500
SHEET 3 BF 7 ALA B 473 VAL B 478 -1 O ARG B 477 N TYR B 494
SHEET 4 BF 7 THR B 465 TYR B 467 -1 O VAL B 466 N THR B 474
SHEET 5 BF 7 TYR B 458 ILE B 460 -1 O THR B 459 N TYR B 467
SHEET 6 BF 7 LYS B 444 ARG B 451 -1 O GLN B 447 N ILE B 460
SHEET 7 BF 7 TYR B 438 ILE B 441 -1 O LYS B 439 N TYR B 446
SHEET 1 BG 2 PHE B 513 ARG B 514 0
SHEET 2 BG 2 LYS B 444 ARG B 451 1 O TYR B 450 N ARG B 514
SHEET 1 BH 2 LEU B 551 VAL B 553 0
SHEET 2 BH 2 ILE B 570 THR B 576 -1 O TYR B 575 N GLY B 552
SHEET 1 BI 2 ILE B 559 VAL B 560 0
SHEET 2 BI 2 ILE B 570 THR B 576 1 O LEU B 571 N ILE B 559
SHEET 1 BJ 4 HIS B 602 ALA B 603 0
SHEET 2 BJ 4 SER B 588 SER B 594 -1 O TYR B 593 N HIS B 602
SHEET 3 BJ 4 ILE B 570 THR B 576 -1 O ILE B 570 N SER B 594
SHEET 4 BJ 4 ILE B 559 VAL B 560 1 O ILE B 559 N LEU B 571
SHEET 1 BK 4 HIS B 602 ALA B 603 0
SHEET 2 BK 4 SER B 588 SER B 594 -1 O TYR B 593 N HIS B 602
SHEET 3 BK 4 ILE B 570 THR B 576 -1 O ILE B 570 N SER B 594
SHEET 4 BK 4 LEU B 551 VAL B 553 -1 O GLY B 552 N TYR B 575
SHEET 1 BL 2 ARG B 611 VAL B 613 0
SHEET 2 BL 2 GLN B 616 ILE B 618 -1 O GLN B 616 N VAL B 613
SHEET 1 BM 4 SER B 633 GLN B 637 0
SHEET 2 BM 4 VAL B 643 MET B 647 -1 O LYS B 644 N VAL B 636
SHEET 3 BM 4 ASP B 653 SER B 659 -1 O GLN B 655 N MET B 647
SHEET 4 BM 4 LYS B 671 LYS B 677 -1 O LYS B 671 N VAL B 656
SHEET 1 BN 4 SER B 684 HIS B 690 0
SHEET 2 BN 4 LYS B 693 ALA B 701 -1 O LYS B 693 N HIS B 690
SHEET 3 BN 4 GLU B 707 VAL B 716 -1 O MET B 710 N ASN B 700
SHEET 4 BN 4 LEU B 722 GLU B 734 -1 O THR B 723 N ARG B 715
SHEET 1 CA 4 THR C 312 PHE C 315 0
SHEET 2 CA 4 THR C 763 ASN C 770 -1 O LEU C 764 N ILE C 314
SHEET 3 CA 4 GLU C 747 HIS C 754 -1 O TYR C 748 N PHE C 769
SHEET 4 CA 4 ASN C 738 GLY C 744 -1 O SER C 739 N LEU C 751
SHEET 1 CB 4 SER C 330 LYS C 338 0
SHEET 2 CB 4 LEU C 344 ARG C 351 -1 O ILE C 345 N LEU C 337
SHEET 3 CB 4 ILE C 361 SER C 368 -1 O GLY C 362 N GLU C 350
SHEET 4 CB 4 VAL C 379 THR C 382 -1 O VAL C 379 N ILE C 365
SHEET 1 CC 5 GLN C 537 ASP C 538 0
SHEET 2 CC 5 TYR C 520 SER C 526 -1 O MET C 523 N GLN C 537
SHEET 3 CC 5 ILE C 414 PHE C 421 -1 O ILE C 414 N SER C 526
SHEET 4 CC 5 VAL C 399 GLN C 407 -1 O VAL C 399 N PHE C 421
SHEET 5 CC 5 GLY C 556 THR C 557 1 O GLY C 556 N LEU C 405
SHEET 1 CD 2 TYR C 438 ILE C 441 0
SHEET 2 CD 2 LYS C 444 ARG C 451 -1 O LYS C 444 N ILE C 441
SHEET 1 CE 7 GLN C 498 ASN C 502 0
SHEET 2 CE 7 ASP C 492 LYS C 495 -1 O LEU C 493 N LEU C 500
SHEET 3 CE 7 ALA C 473 VAL C 478 -1 O ARG C 477 N TYR C 494
SHEET 4 CE 7 THR C 465 TYR C 467 -1 O VAL C 466 N THR C 474
SHEET 5 CE 7 ALA C 457 ILE C 460 -1 O THR C 459 N TYR C 467
SHEET 6 CE 7 LYS C 444 ARG C 451 -1 O GLN C 447 N ILE C 460
SHEET 7 CE 7 PHE C 513 ILE C 515 1 O ARG C 514 N TYR C 450
SHEET 1 CF 7 GLN C 498 ASN C 502 0
SHEET 2 CF 7 ASP C 492 LYS C 495 -1 O LEU C 493 N LEU C 500
SHEET 3 CF 7 ALA C 473 VAL C 478 -1 O ARG C 477 N TYR C 494
SHEET 4 CF 7 THR C 465 TYR C 467 -1 O VAL C 466 N THR C 474
SHEET 5 CF 7 ALA C 457 ILE C 460 -1 O THR C 459 N TYR C 467
SHEET 6 CF 7 LYS C 444 ARG C 451 -1 O GLN C 447 N ILE C 460
SHEET 7 CF 7 TYR C 438 ILE C 441 -1 O LYS C 439 N TYR C 446
SHEET 1 CG 2 PHE C 513 ILE C 515 0
SHEET 2 CG 2 LYS C 444 ARG C 451 1 O TYR C 450 N ARG C 514
SHEET 1 CH 2 LEU C 551 VAL C 553 0
SHEET 2 CH 2 ILE C 570 THR C 576 -1 O TYR C 575 N GLY C 552
SHEET 1 CI 2 ILE C 559 VAL C 560 0
SHEET 2 CI 2 ILE C 570 THR C 576 1 O LEU C 571 N ILE C 559
SHEET 1 CJ 4 HIS C 602 ALA C 603 0
SHEET 2 CJ 4 SER C 588 SER C 594 -1 O TYR C 593 N HIS C 602
SHEET 3 CJ 4 ILE C 570 THR C 576 -1 O ILE C 570 N SER C 594
SHEET 4 CJ 4 ILE C 559 VAL C 560 1 O ILE C 559 N LEU C 571
SHEET 1 CK 4 HIS C 602 ALA C 603 0
SHEET 2 CK 4 SER C 588 SER C 594 -1 O TYR C 593 N HIS C 602
SHEET 3 CK 4 ILE C 570 THR C 576 -1 O ILE C 570 N SER C 594
SHEET 4 CK 4 LEU C 551 VAL C 553 -1 O GLY C 552 N TYR C 575
SHEET 1 CL 2 ARG C 611 VAL C 613 0
SHEET 2 CL 2 GLN C 616 ILE C 618 -1 O GLN C 616 N VAL C 613
SHEET 1 CM 4 SER C 633 GLN C 637 0
SHEET 2 CM 4 VAL C 643 MET C 647 -1 O LYS C 644 N VAL C 636
SHEET 3 CM 4 ASP C 653 SER C 659 -1 O GLN C 655 N MET C 647
SHEET 4 CM 4 LYS C 671 LYS C 677 -1 O LYS C 671 N VAL C 656
SHEET 1 CN 4 SER C 684 HIS C 690 0
SHEET 2 CN 4 LYS C 693 ALA C 701 -1 O LYS C 693 N HIS C 690
SHEET 3 CN 4 GLU C 707 VAL C 716 -1 O MET C 710 N ASN C 700
SHEET 4 CN 4 LEU C 722 GLU C 734 -1 O THR C 723 N ARG C 715
SHEET 1 DA 4 THR D 312 PHE D 315 0
SHEET 2 DA 4 THR D 763 ASN D 770 -1 O LEU D 764 N ILE D 314
SHEET 3 DA 4 GLU D 747 HIS D 754 -1 O TYR D 748 N PHE D 769
SHEET 4 DA 4 ASN D 738 GLY D 744 -1 O SER D 739 N LEU D 751
SHEET 1 DB 4 SER D 330 LYS D 338 0
SHEET 2 DB 4 LEU D 344 ARG D 351 -1 O ILE D 345 N LEU D 337
SHEET 3 DB 4 ILE D 361 SER D 368 -1 O GLY D 362 N GLU D 350
SHEET 4 DB 4 VAL D 379 THR D 382 -1 O VAL D 379 N ILE D 365
SHEET 1 DC 5 GLN D 537 ASP D 538 0
SHEET 2 DC 5 TYR D 520 SER D 526 -1 O MET D 523 N GLN D 537
SHEET 3 DC 5 ILE D 414 PHE D 421 -1 O ILE D 414 N SER D 526
SHEET 4 DC 5 VAL D 399 GLN D 407 -1 O VAL D 399 N PHE D 421
SHEET 5 DC 5 GLY D 556 THR D 557 1 O GLY D 556 N LEU D 405
SHEET 1 DD 2 TYR D 438 ILE D 441 0
SHEET 2 DD 2 LYS D 444 ARG D 451 -1 O LYS D 444 N ILE D 441
SHEET 1 DE 7 GLN D 498 ASN D 502 0
SHEET 2 DE 7 ASP D 492 LYS D 495 -1 O LEU D 493 N LEU D 500
SHEET 3 DE 7 ALA D 473 VAL D 478 -1 O ARG D 477 N TYR D 494
SHEET 4 DE 7 THR D 465 TYR D 467 -1 O VAL D 466 N THR D 474
SHEET 5 DE 7 TYR D 458 ILE D 460 -1 O THR D 459 N TYR D 467
SHEET 6 DE 7 LYS D 444 ARG D 451 -1 O GLN D 447 N ILE D 460
SHEET 7 DE 7 PHE D 513 ARG D 514 1 O ARG D 514 N TYR D 450
SHEET 1 DF 7 GLN D 498 ASN D 502 0
SHEET 2 DF 7 ASP D 492 LYS D 495 -1 O LEU D 493 N LEU D 500
SHEET 3 DF 7 ALA D 473 VAL D 478 -1 O ARG D 477 N TYR D 494
SHEET 4 DF 7 THR D 465 TYR D 467 -1 O VAL D 466 N THR D 474
SHEET 5 DF 7 TYR D 458 ILE D 460 -1 O THR D 459 N TYR D 467
SHEET 6 DF 7 LYS D 444 ARG D 451 -1 O GLN D 447 N ILE D 460
SHEET 7 DF 7 TYR D 438 ILE D 441 -1 O LYS D 439 N TYR D 446
SHEET 1 DG 2 PHE D 513 ARG D 514 0
SHEET 2 DG 2 LYS D 444 ARG D 451 1 O TYR D 450 N ARG D 514
SHEET 1 DH 2 LEU D 551 VAL D 553 0
SHEET 2 DH 2 ILE D 570 THR D 576 -1 O TYR D 575 N GLY D 552
SHEET 1 DI 2 ILE D 559 VAL D 560 0
SHEET 2 DI 2 ILE D 570 THR D 576 1 O LEU D 571 N ILE D 559
SHEET 1 DJ 4 HIS D 602 ALA D 603 0
SHEET 2 DJ 4 SER D 588 SER D 594 -1 O TYR D 593 N HIS D 602
SHEET 3 DJ 4 ILE D 570 THR D 576 -1 O ILE D 570 N SER D 594
SHEET 4 DJ 4 ILE D 559 VAL D 560 1 O ILE D 559 N LEU D 571
SHEET 1 DK 4 HIS D 602 ALA D 603 0
SHEET 2 DK 4 SER D 588 SER D 594 -1 O TYR D 593 N HIS D 602
SHEET 3 DK 4 ILE D 570 THR D 576 -1 O ILE D 570 N SER D 594
SHEET 4 DK 4 LEU D 551 VAL D 553 -1 O GLY D 552 N TYR D 575
SHEET 1 DL 2 ARG D 611 GLN D 612 0
SHEET 2 DL 2 LYS D 617 ILE D 618 -1 N ILE D 618 O ARG D 611
SHEET 1 DM 4 SER D 633 GLN D 637 0
SHEET 2 DM 4 VAL D 643 MET D 647 -1 O LYS D 644 N VAL D 636
SHEET 3 DM 4 ASP D 653 SER D 659 -1 O GLN D 655 N MET D 647
SHEET 4 DM 4 LYS D 671 LYS D 677 -1 O LYS D 671 N VAL D 656
SHEET 1 DN 4 SER D 684 HIS D 690 0
SHEET 2 DN 4 LYS D 693 ALA D 701 -1 O LYS D 693 N HIS D 690
SHEET 3 DN 4 GLU D 707 VAL D 716 -1 O MET D 710 N ASN D 700
SHEET 4 DN 4 LEU D 722 GLU D 734 -1 O THR D 723 N ARG D 715
CISPEP 1 GLY A 703 PRO A 704 0 0.93
CISPEP 2 ALA A 761 TYR A 762 0 -2.18
CISPEP 3 GLY B 703 PRO B 704 0 3.81
CISPEP 4 ALA B 761 TYR B 762 0 1.76
CISPEP 5 GLY C 703 PRO C 704 0 4.00
CISPEP 6 ALA C 761 TYR C 762 0 0.40
CISPEP 7 GLY D 703 PRO D 704 0 5.90
CISPEP 8 ALA D 761 TYR D 762 0 3.70
SITE 1 AC1 21 ARG A 332 ILE A 333 ASP A 349 ARG A 351
SITE 2 AC1 21 ASP A 357 ILE A 401 ASP A 402 ASP A 419
SITE 3 AC1 21 ILE A 427 PHE A 428 TYR A 575 GLN A 587
SITE 4 AC1 21 ARG A 648 TYR A 680 ARG A 706 TYR A 737
SITE 5 AC1 21 HOH A2017 HOH A2024 HOH A2267 HOH A2348
SITE 6 AC1 21 HOH A2349
SITE 1 AC2 5 GLY A 501 ASN A 502 LYS A 509 THR A 510
SITE 2 AC2 5 SER A 511
SITE 1 AC3 19 ARG B 332 ILE B 333 ASP B 349 ARG B 351
SITE 2 AC3 19 ASP B 357 ILE B 401 ASP B 402 ASP B 419
SITE 3 AC3 19 ILE B 427 PHE B 428 TYR B 575 GLN B 587
SITE 4 AC3 19 ARG B 648 ARG B 706 TYR B 737 HOH B2009
SITE 5 AC3 19 HOH B2019 HOH B2231 HOH B2297
SITE 1 AC4 5 GLY B 501 ASN B 502 LYS B 509 THR B 510
SITE 2 AC4 5 SER B 511
SITE 1 AC5 19 ARG C 332 ILE C 333 ASP C 349 ARG C 351
SITE 2 AC5 19 ASP C 357 ILE C 401 ASP C 402 ASP C 419
SITE 3 AC5 19 ILE C 427 PHE C 428 TYR C 575 GLN C 587
SITE 4 AC5 19 ARG C 648 ARG C 706 TYR C 737 HOH C2341
SITE 5 AC5 19 HOH C2342 HOH C2343 HOH C2344
SITE 1 AC6 5 GLY C 501 ASN C 502 LYS C 509 THR C 510
SITE 2 AC6 5 SER C 511
SITE 1 AC7 18 ARG D 332 ILE D 333 ASP D 349 ARG D 351
SITE 2 AC7 18 ASP D 357 ILE D 401 ASP D 402 ILE D 427
SITE 3 AC7 18 PHE D 428 TYR D 575 GLN D 587 ARG D 648
SITE 4 AC7 18 ARG D 706 TYR D 737 HOH D2018 HOH D2275
SITE 5 AC7 18 HOH D2306 HOH D2307
SITE 1 AC8 4 ASN D 502 LYS D 509 THR D 510 SER D 511
CRYST1 49.856 87.161 126.410 104.06 91.04 106.68 P 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 0.020058 0.006010 0.001989 0.00000
SCALE2 0.000000 0.011977 0.003213 0.00000
SCALE3 0.000000 0.000000 0.008192 0.00000
MTRIX1 1 0.285500 -0.461700 -0.839000 9.97900 1
MTRIX2 1 -0.464900 -0.833000 0.299900 -95.80000 1
MTRIX3 1 -0.838000 0.304900 -0.452500 68.28000 1
MTRIX1 2 1.000000 -0.001879 -0.009256 25.28000 1
MTRIX2 2 -0.001870 -1.000000 0.000997 -115.20000 1
MTRIX3 2 -0.009258 -0.000980 -1.000000 120.90000 1
MTRIX1 3 0.288900 0.463700 0.837600 -31.10000 1
MTRIX2 3 -0.468900 0.831300 -0.298500 24.63000 1
MTRIX3 3 -0.834700 -0.306500 0.457600 -42.81000 1
(ATOM LINES ARE NOT SHOWN.)
END
