HEADER HYDROLASE 21-OCT-08 2W20
TITLE STRUCTURE OF THE CATALYTIC DOMAIN OF THE NATIVE NANA
TITLE 2 SIALIDASE FROM STREPTOCOCCUS PNEUMONIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIALIDASE A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 321-791;
COMPND 5 SYNONYM: NEURAMINIDASE A, NANA SIALIDASE;
COMPND 6 EC: 3.2.1.18;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 171101;
SOURCE 4 STRAIN: R6;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS SECRETED, CELL WALL, HYDROLASE, SIALIDASE, GLYCOSIDASE,
KEYWDS 2 NEURAMINIDASE, PEPTIDOGLYCAN-ANCHOR
EXPDTA X-RAY DIFFRACTION
AUTHOR G.XU,P.W.ANDREW,G.L.TAYLOR
REVDAT 2 10-NOV-09 2W20 1 REMARK
REVDAT 1 23-DEC-08 2W20 0
JRNL AUTH G.XU,X.LI,P.W.ANDREW,G.L.TAYLOR
JRNL TITL STRUCTURE OF THE CATALYTIC DOMAIN OF STREPTOCOCCUS
JRNL TITL 2 PNEUMONIAE SIALIDASE NANA.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 64 772 2008
JRNL REFN ISSN 1744-3091
JRNL PMID 18765901
JRNL DOI 10.1107/S1744309108024044
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.23
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 159301
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8003
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 40.2411 - 4.6338 0.88 4899 235 0.1801 0.1815
REMARK 3 2 4.6338 - 3.6788 0.94 4991 261 0.1602 0.1778
REMARK 3 3 3.6788 - 3.2140 0.96 5049 270 0.1735 0.1950
REMARK 3 4 3.2140 - 2.9202 0.96 5019 279 0.1878 0.2126
REMARK 3 5 2.9202 - 2.7109 0.97 5067 294 0.1971 0.2355
REMARK 3 6 2.7109 - 2.5511 0.98 5060 256 0.2015 0.2253
REMARK 3 7 2.5511 - 2.4234 0.98 5093 270 0.1966 0.2055
REMARK 3 8 2.4234 - 2.3179 0.98 5059 276 0.1986 0.2409
REMARK 3 9 2.3179 - 2.2287 0.98 5055 277 0.1976 0.2144
REMARK 3 10 2.2287 - 2.1518 0.99 5035 273 0.1915 0.2150
REMARK 3 11 2.1518 - 2.0845 0.99 5112 299 0.1935 0.2095
REMARK 3 12 2.0845 - 2.0249 0.99 5086 262 0.1910 0.2290
REMARK 3 13 2.0249 - 1.9716 0.99 5073 270 0.1990 0.2439
REMARK 3 14 1.9716 - 1.9235 0.99 5160 256 0.1974 0.2232
REMARK 3 15 1.9235 - 1.8798 1.00 5074 281 0.1920 0.2134
REMARK 3 16 1.8798 - 1.8398 1.00 5195 244 0.2007 0.2489
REMARK 3 17 1.8398 - 1.8030 1.00 5064 274 0.2065 0.2343
REMARK 3 18 1.8030 - 1.7690 1.00 5143 256 0.2022 0.2475
REMARK 3 19 1.7690 - 1.7374 1.00 5078 272 0.2160 0.2649
REMARK 3 20 1.7374 - 1.7079 0.99 5120 276 0.2140 0.2659
REMARK 3 21 1.7079 - 1.6804 0.99 5016 281 0.2105 0.2496
REMARK 3 22 1.6804 - 1.6545 0.99 5112 263 0.2071 0.2284
REMARK 3 23 1.6545 - 1.6302 0.99 4977 264 0.2200 0.2953
REMARK 3 24 1.6302 - 1.6072 0.98 5067 281 0.2225 0.2551
REMARK 3 25 1.6072 - 1.5855 0.99 5038 260 0.2305 0.2766
REMARK 3 26 1.5855 - 1.5649 0.98 5060 262 0.2430 0.2652
REMARK 3 27 1.5649 - 1.5453 0.98 5004 251 0.2422 0.2605
REMARK 3 28 1.5453 - 1.5267 0.99 5002 252 0.2471 0.2609
REMARK 3 29 1.5267 - 1.5090 0.97 5003 249 0.2475 0.2620
REMARK 3 30 1.5090 - 1.4920 0.90 4587 259 0.2624 0.2845
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 45.55
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.85
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.81280
REMARK 3 B22 (A**2) : -1.01710
REMARK 3 B33 (A**2) : -1.79570
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.000 7630
REMARK 3 ANGLE : 1.220 10302
REMARK 3 CHIRALITY : 0.110 1083
REMARK 3 PLANARITY : 0.000 1343
REMARK 3 DIHEDRAL : 17.270 2825
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2W20 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-OCT-08.
REMARK 100 THE PDBE ID CODE IS EBI-37899.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 159417
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.49
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 3.9
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.00
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: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG4K, 0.1 M MES PH6.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 23.60000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 109.10000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.30000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 109.10000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.60000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.30000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 GENERATING THE BIOMOLECULE
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 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 LYS A 791
REMARK 465 ALA B 321
REMARK 465 LYS B 791
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 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 348 71.12 71.52
REMARK 500 HIS A 369 176.07 178.88
REMARK 500 ASP A 372 46.42 -80.00
REMARK 500 ASP A 417 103.99 71.41
REMARK 500 ARG A 476 -149.64 -112.49
REMARK 500 LYS A 564 -87.70 -89.99
REMARK 500 HIS A 597 -124.38 41.63
REMARK 500 THR A 646 -119.10 -123.09
REMARK 500 TYR A 695 68.28 73.46
REMARK 500 LYS A 720 -158.49 -103.73
REMARK 500 GLU A 733 50.36 -92.13
REMARK 500 ALA A 751 -116.16 -132.84
REMARK 500 ASN B 339 -169.34 -79.78
REMARK 500 ILE B 348 68.92 70.25
REMARK 500 HIS B 369 176.81 179.12
REMARK 500 ASP B 372 45.13 -76.15
REMARK 500 ASP B 417 103.00 71.14
REMARK 500 ARG B 476 -152.13 -117.04
REMARK 500 ASP B 533 -156.11 -128.66
REMARK 500 LYS B 564 -86.15 -89.66
REMARK 500 HIS B 597 -126.33 44.67
REMARK 500 THR B 646 -117.83 -120.39
REMARK 500 TYR B 695 70.33 71.33
REMARK 500 LYS B 720 -152.53 -107.00
REMARK 500 GLU B 733 -120.25 30.10
REMARK 500 ALA B 751 -120.88 -133.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A1791
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B1791
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1792
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1792
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1793
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1793
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1794
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1795
DBREF 2W20 A 321 791 UNP P62576 NANA_STRR6 321 791
DBREF 2W20 B 321 791 UNP P62576 NANA_STRR6 321 791
SEQRES 1 A 471 ALA ALA LEU THR GLU LYS THR ASP ILE PHE GLU SER GLY
SEQRES 2 A 471 ARG ASN GLY LYS PRO ASN LYS ASP GLY ILE LYS SER TYR
SEQRES 3 A 471 ARG ILE PRO ALA LEU LEU LYS THR ASP LYS GLY THR LEU
SEQRES 4 A 471 ILE ALA GLY ALA ASP GLU ARG ARG LEU HIS SER SER ASP
SEQRES 5 A 471 TRP GLY ASP ILE GLY MET VAL ILE ARG ARG SER GLU ASP
SEQRES 6 A 471 ASN GLY LYS THR TRP GLY ASP ARG VAL THR ILE THR ASN
SEQRES 7 A 471 LEU ARG ASP ASN PRO LYS ALA SER ASP PRO SER ILE GLY
SEQRES 8 A 471 SER PRO VAL ASN ILE ASP MET VAL LEU VAL GLN ASP PRO
SEQRES 9 A 471 GLU THR LYS ARG ILE PHE SER ILE TYR ASP MET PHE PRO
SEQRES 10 A 471 GLU GLY LYS GLY ILE PHE GLY MET SER SER GLN LYS GLU
SEQRES 11 A 471 GLU ALA TYR LYS LYS ILE ASP GLY LYS THR TYR GLN ILE
SEQRES 12 A 471 LEU TYR ARG GLU GLY GLU LYS GLY ALA TYR THR ILE ARG
SEQRES 13 A 471 GLU ASN GLY THR VAL TYR THR PRO ASP GLY LYS ALA THR
SEQRES 14 A 471 ASP TYR ARG VAL VAL VAL ASP PRO VAL LYS PRO ALA TYR
SEQRES 15 A 471 SER ASP LYS GLY ASP LEU TYR LYS GLY ASN GLN LEU LEU
SEQRES 16 A 471 GLY ASN ILE TYR PHE THR THR ASN LYS THR SER PRO PHE
SEQRES 17 A 471 ARG ILE ALA LYS ASP SER TYR LEU TRP MET SER TYR SER
SEQRES 18 A 471 ASP ASP ASP GLY LYS THR TRP SER ALA PRO GLN ASP ILE
SEQRES 19 A 471 THR PRO MET VAL LYS ALA ASP TRP MET LYS PHE LEU GLY
SEQRES 20 A 471 VAL GLY PRO GLY THR GLY ILE VAL LEU ARG ASN GLY PRO
SEQRES 21 A 471 HIS LYS GLY ARG ILE LEU ILE PRO VAL TYR THR THR ASN
SEQRES 22 A 471 ASN VAL SER HIS LEU ASN GLY SER GLN SER SER ARG ILE
SEQRES 23 A 471 ILE TYR SER ASP ASP HIS GLY LYS THR TRP HIS ALA GLY
SEQRES 24 A 471 GLU ALA VAL ASN ASP ASN ARG GLN VAL ASP GLY GLN LYS
SEQRES 25 A 471 ILE HIS SER SER THR MET ASN ASN ARG ARG ALA GLN ASN
SEQRES 26 A 471 THR GLU SER THR VAL VAL GLN LEU ASN ASN GLY ASP VAL
SEQRES 27 A 471 LYS LEU PHE MET ARG GLY LEU THR GLY ASP LEU GLN VAL
SEQRES 28 A 471 ALA THR SER LYS ASP GLY GLY VAL THR TRP GLU LYS ASP
SEQRES 29 A 471 ILE LYS ARG TYR PRO GLN VAL LYS ASP VAL TYR VAL GLN
SEQRES 30 A 471 MET SER ALA ILE HIS THR MET HIS GLU GLY LYS GLU TYR
SEQRES 31 A 471 ILE ILE LEU SER ASN ALA GLY GLY PRO LYS ARG GLU ASN
SEQRES 32 A 471 GLY MET VAL HIS LEU ALA ARG VAL GLU GLU ASN GLY GLU
SEQRES 33 A 471 LEU THR TRP LEU LYS HIS ASN PRO ILE GLN LYS GLY GLU
SEQRES 34 A 471 PHE ALA TYR ASN SER LEU GLN GLU LEU GLY ASN GLY GLU
SEQRES 35 A 471 TYR GLY ILE LEU TYR GLU HIS THR GLU LYS GLY GLN ASN
SEQRES 36 A 471 ALA TYR THR LEU SER PHE ARG LYS PHE ASN TRP ASP PHE
SEQRES 37 A 471 LEU SER LYS
SEQRES 1 B 471 ALA ALA LEU THR GLU LYS THR ASP ILE PHE GLU SER GLY
SEQRES 2 B 471 ARG ASN GLY LYS PRO ASN LYS ASP GLY ILE LYS SER TYR
SEQRES 3 B 471 ARG ILE PRO ALA LEU LEU LYS THR ASP LYS GLY THR LEU
SEQRES 4 B 471 ILE ALA GLY ALA ASP GLU ARG ARG LEU HIS SER SER ASP
SEQRES 5 B 471 TRP GLY ASP ILE GLY MET VAL ILE ARG ARG SER GLU ASP
SEQRES 6 B 471 ASN GLY LYS THR TRP GLY ASP ARG VAL THR ILE THR ASN
SEQRES 7 B 471 LEU ARG ASP ASN PRO LYS ALA SER ASP PRO SER ILE GLY
SEQRES 8 B 471 SER PRO VAL ASN ILE ASP MET VAL LEU VAL GLN ASP PRO
SEQRES 9 B 471 GLU THR LYS ARG ILE PHE SER ILE TYR ASP MET PHE PRO
SEQRES 10 B 471 GLU GLY LYS GLY ILE PHE GLY MET SER SER GLN LYS GLU
SEQRES 11 B 471 GLU ALA TYR LYS LYS ILE ASP GLY LYS THR TYR GLN ILE
SEQRES 12 B 471 LEU TYR ARG GLU GLY GLU LYS GLY ALA TYR THR ILE ARG
SEQRES 13 B 471 GLU ASN GLY THR VAL TYR THR PRO ASP GLY LYS ALA THR
SEQRES 14 B 471 ASP TYR ARG VAL VAL VAL ASP PRO VAL LYS PRO ALA TYR
SEQRES 15 B 471 SER ASP LYS GLY ASP LEU TYR LYS GLY ASN GLN LEU LEU
SEQRES 16 B 471 GLY ASN ILE TYR PHE THR THR ASN LYS THR SER PRO PHE
SEQRES 17 B 471 ARG ILE ALA LYS ASP SER TYR LEU TRP MET SER TYR SER
SEQRES 18 B 471 ASP ASP ASP GLY LYS THR TRP SER ALA PRO GLN ASP ILE
SEQRES 19 B 471 THR PRO MET VAL LYS ALA ASP TRP MET LYS PHE LEU GLY
SEQRES 20 B 471 VAL GLY PRO GLY THR GLY ILE VAL LEU ARG ASN GLY PRO
SEQRES 21 B 471 HIS LYS GLY ARG ILE LEU ILE PRO VAL TYR THR THR ASN
SEQRES 22 B 471 ASN VAL SER HIS LEU ASN GLY SER GLN SER SER ARG ILE
SEQRES 23 B 471 ILE TYR SER ASP ASP HIS GLY LYS THR TRP HIS ALA GLY
SEQRES 24 B 471 GLU ALA VAL ASN ASP ASN ARG GLN VAL ASP GLY GLN LYS
SEQRES 25 B 471 ILE HIS SER SER THR MET ASN ASN ARG ARG ALA GLN ASN
SEQRES 26 B 471 THR GLU SER THR VAL VAL GLN LEU ASN ASN GLY ASP VAL
SEQRES 27 B 471 LYS LEU PHE MET ARG GLY LEU THR GLY ASP LEU GLN VAL
SEQRES 28 B 471 ALA THR SER LYS ASP GLY GLY VAL THR TRP GLU LYS ASP
SEQRES 29 B 471 ILE LYS ARG TYR PRO GLN VAL LYS ASP VAL TYR VAL GLN
SEQRES 30 B 471 MET SER ALA ILE HIS THR MET HIS GLU GLY LYS GLU TYR
SEQRES 31 B 471 ILE ILE LEU SER ASN ALA GLY GLY PRO LYS ARG GLU ASN
SEQRES 32 B 471 GLY MET VAL HIS LEU ALA ARG VAL GLU GLU ASN GLY GLU
SEQRES 33 B 471 LEU THR TRP LEU LYS HIS ASN PRO ILE GLN LYS GLY GLU
SEQRES 34 B 471 PHE ALA TYR ASN SER LEU GLN GLU LEU GLY ASN GLY GLU
SEQRES 35 B 471 TYR GLY ILE LEU TYR GLU HIS THR GLU LYS GLY GLN ASN
SEQRES 36 B 471 ALA TYR THR LEU SER PHE ARG LYS PHE ASN TRP ASP PHE
SEQRES 37 B 471 LEU SER LYS
HET MES A1791 12
HET MES B1791 12
HET CL B1792 1
HET CL A1792 1
HET CL A1793 1
HET GOL B1793 6
HET GOL A1794 6
HET GOL A1795 6
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
FORMUL 3 GOL 3(C3 H8 O3)
FORMUL 4 CL 3(CL 1-)
FORMUL 5 MES 2(C6 H13 N O4 S)
FORMUL 6 HOH *1025(H2 O1)
HELIX 1 1 ASP A 407 GLY A 411 5 5
HELIX 2 2 LYS A 440 MET A 445 5 6
HELIX 3 3 LYS A 499 SER A 503 5 5
HELIX 4 4 ILE A 554 LYS A 559 1 6
HELIX 5 5 SER A 596 SER A 601 1 6
HELIX 6 6 ASN A 640 GLN A 644 5 5
HELIX 7 7 TRP A 786 SER A 790 1 5
HELIX 8 8 ASP B 407 GLY B 411 5 5
HELIX 9 9 LYS B 440 MET B 445 5 6
HELIX 10 10 LYS B 499 SER B 503 5 5
HELIX 11 11 ILE B 554 LYS B 559 1 6
HELIX 12 12 SER B 596 SER B 601 1 6
HELIX 13 13 ASN B 640 GLN B 644 5 5
HELIX 14 14 TRP B 786 SER B 790 1 5
SHEET 1 AA 4 THR A 327 PHE A 330 0
SHEET 2 AA 4 THR A 778 ASN A 785 -1 O LEU A 779 N ILE A 329
SHEET 3 AA 4 GLU A 762 HIS A 769 -1 O TYR A 763 N PHE A 784
SHEET 4 AA 4 ASN A 753 GLY A 759 -1 O SER A 754 N LEU A 766
SHEET 1 AB 4 SER A 345 LYS A 353 0
SHEET 2 AB 4 LEU A 359 ARG A 366 -1 O ILE A 360 N LEU A 352
SHEET 3 AB 4 ILE A 376 SER A 383 -1 O GLY A 377 N GLU A 365
SHEET 4 AB 4 VAL A 394 THR A 397 -1 O VAL A 394 N ILE A 380
SHEET 1 AC 5 GLN A 552 ASP A 553 0
SHEET 2 AC 5 TYR A 535 SER A 541 -1 O MET A 538 N GLN A 552
SHEET 3 AC 5 ILE A 429 PHE A 436 -1 O ILE A 429 N SER A 541
SHEET 4 AC 5 VAL A 414 GLN A 422 -1 O VAL A 414 N PHE A 436
SHEET 5 AC 5 GLY A 571 THR A 572 1 O GLY A 571 N LEU A 420
SHEET 1 AD 7 TYR A 453 ILE A 456 0
SHEET 2 AD 7 LYS A 459 ARG A 466 -1 O LYS A 459 N ILE A 456
SHEET 3 AD 7 TYR A 473 ILE A 475 -1 O TYR A 473 N LEU A 464
SHEET 4 AD 7 THR A 480 TYR A 482 -1 O TYR A 482 N THR A 474
SHEET 5 AD 7 ALA A 488 VAL A 493 -1 N THR A 489 O VAL A 481
SHEET 6 AD 7 ASP A 507 LYS A 510 -1 O TYR A 509 N ARG A 492
SHEET 7 AD 7 GLN A 513 ASN A 517 -1 O GLN A 513 N LYS A 510
SHEET 1 AE 3 TYR A 453 ILE A 456 0
SHEET 2 AE 3 LYS A 459 ARG A 466 -1 O LYS A 459 N ILE A 456
SHEET 3 AE 3 PHE A 528 ARG A 529 -1 O ARG A 529 N TYR A 465
SHEET 1 AF 3 LEU A 566 VAL A 568 0
SHEET 2 AF 3 ILE A 585 THR A 591 -1 O TYR A 590 N GLY A 567
SHEET 3 AF 3 ILE A 574 VAL A 575 -1 O ILE A 574 N LEU A 586
SHEET 1 AG 4 LEU A 566 VAL A 568 0
SHEET 2 AG 4 ILE A 585 THR A 591 -1 O TYR A 590 N GLY A 567
SHEET 3 AG 4 SER A 603 SER A 609 -1 O SER A 603 N THR A 591
SHEET 4 AG 4 HIS A 617 ALA A 618 -1 O HIS A 617 N TYR A 608
SHEET 1 AH 2 ARG A 626 VAL A 628 0
SHEET 2 AH 2 GLN A 631 ILE A 633 -1 O GLN A 631 N VAL A 628
SHEET 1 AI 4 SER A 648 GLN A 652 0
SHEET 2 AI 4 VAL A 658 MET A 662 -1 O LYS A 659 N VAL A 651
SHEET 3 AI 4 ASP A 668 SER A 674 -1 O GLN A 670 N MET A 662
SHEET 4 AI 4 LYS A 686 LYS A 692 -1 O LYS A 686 N VAL A 671
SHEET 1 AJ 4 SER A 699 HIS A 705 0
SHEET 2 AJ 4 LYS A 708 ALA A 716 -1 O LYS A 708 N HIS A 705
SHEET 3 AJ 4 GLU A 722 VAL A 731 -1 O MET A 725 N ASN A 715
SHEET 4 AJ 4 LEU A 737 GLU A 749 -1 O THR A 738 N ARG A 730
SHEET 1 BA 4 THR B 327 PHE B 330 0
SHEET 2 BA 4 THR B 778 ASN B 785 -1 O LEU B 779 N ILE B 329
SHEET 3 BA 4 GLU B 762 HIS B 769 -1 O TYR B 763 N PHE B 784
SHEET 4 BA 4 ASN B 753 GLY B 759 -1 O SER B 754 N LEU B 766
SHEET 1 BB 4 SER B 345 LYS B 353 0
SHEET 2 BB 4 LEU B 359 ARG B 366 -1 O ILE B 360 N LEU B 352
SHEET 3 BB 4 ILE B 376 SER B 383 -1 O GLY B 377 N GLU B 365
SHEET 4 BB 4 VAL B 394 THR B 397 -1 O VAL B 394 N ILE B 380
SHEET 1 BC 5 GLN B 552 ASP B 553 0
SHEET 2 BC 5 TYR B 535 SER B 541 -1 O MET B 538 N GLN B 552
SHEET 3 BC 5 ILE B 429 PHE B 436 -1 O ILE B 429 N SER B 541
SHEET 4 BC 5 VAL B 414 GLN B 422 -1 O VAL B 414 N PHE B 436
SHEET 5 BC 5 GLY B 571 THR B 572 1 O GLY B 571 N LEU B 420
SHEET 1 BD 7 TYR B 453 ILE B 456 0
SHEET 2 BD 7 LYS B 459 ARG B 466 -1 O LYS B 459 N ILE B 456
SHEET 3 BD 7 TYR B 473 ILE B 475 -1 O TYR B 473 N LEU B 464
SHEET 4 BD 7 THR B 480 TYR B 482 -1 O TYR B 482 N THR B 474
SHEET 5 BD 7 ALA B 488 VAL B 493 -1 N THR B 489 O VAL B 481
SHEET 6 BD 7 ASP B 507 LYS B 510 -1 O TYR B 509 N ARG B 492
SHEET 7 BD 7 GLN B 513 ASN B 517 -1 O GLN B 513 N LYS B 510
SHEET 1 BE 3 TYR B 453 ILE B 456 0
SHEET 2 BE 3 LYS B 459 ARG B 466 -1 O LYS B 459 N ILE B 456
SHEET 3 BE 3 PHE B 528 ARG B 529 -1 O ARG B 529 N TYR B 465
SHEET 1 BF 7 LEU B 566 VAL B 568 0
SHEET 2 BF 7 ILE B 585 THR B 591 -1 O TYR B 590 N GLY B 567
SHEET 3 BF 7 ILE B 574 VAL B 575 -1 O ILE B 574 N LEU B 586
SHEET 4 BF 7 ILE B 585 THR B 591 -1 O LEU B 586 N ILE B 574
SHEET 5 BF 7 HIS B 617 ALA B 618
SHEET 6 BF 7 SER B 603 SER B 609 -1 O TYR B 608 N HIS B 617
SHEET 7 BF 7 ILE B 585 THR B 591 -1 O ILE B 585 N SER B 609
SHEET 1 BG 2 ARG B 626 VAL B 628 0
SHEET 2 BG 2 GLN B 631 ILE B 633 -1 O GLN B 631 N VAL B 628
SHEET 1 BH 4 SER B 648 GLN B 652 0
SHEET 2 BH 4 VAL B 658 MET B 662 -1 O LYS B 659 N VAL B 651
SHEET 3 BH 4 ASP B 668 SER B 674 -1 O GLN B 670 N MET B 662
SHEET 4 BH 4 LYS B 686 LYS B 692 -1 O LYS B 686 N VAL B 671
SHEET 1 BI 4 SER B 699 HIS B 705 0
SHEET 2 BI 4 LYS B 708 ALA B 716 -1 O LYS B 708 N HIS B 705
SHEET 3 BI 4 GLU B 722 VAL B 731 -1 O MET B 725 N ASN B 715
SHEET 4 BI 4 LEU B 737 GLU B 749 -1 O THR B 738 N ARG B 730
CISPEP 1 GLY A 718 PRO A 719 0 6.25
CISPEP 2 ASN A 734 GLY A 735 0 0.36
CISPEP 3 ALA A 776 TYR A 777 0 -12.76
CISPEP 4 GLY B 718 PRO B 719 0 5.75
CISPEP 5 ALA B 776 TYR B 777 0 -6.02
SITE 1 AC1 10 TYR A 465 ARG A 466 GLU A 467 GLY A 468
SITE 2 AC1 10 GLU A 469 ARG A 529 HOH A2559 HOH A2560
SITE 3 AC1 10 ASN B 625 LYS B 632
SITE 1 AC2 12 ASN A 625 LYS A 632 GLU B 450 TYR B 465
SITE 2 AC2 12 ARG B 466 GLU B 467 GLY B 468 GLU B 469
SITE 3 AC2 12 LYS B 470 ARG B 529 GOL B1793 HOH B2465
SITE 1 AC3 4 ASN B 517 LYS B 524 THR B 525 SER B 526
SITE 1 AC4 5 GLY A 516 ASN A 517 LYS A 524 THR A 525
SITE 2 AC4 5 SER A 526
SITE 1 AC5 4 VAL A 628 GLN A 631 HOH A2396 HOH A2403
SITE 1 AC6 6 GLN A 627 LYS A 632 LYS A 683 GLU B 469
SITE 2 AC6 6 LYS B 470 MES B1791
SITE 1 AC7 7 ASP A 385 ASN A 386 GLU A 762 LYS A 783
SITE 2 AC7 7 HOH A2057 ASP B 490 LYS B 510
SITE 1 AC8 6 SER A 371 TRP A 373 SER A 409 ILE A 410
SITE 2 AC8 6 GLU A 425 HIS A 612
CRYST1 47.200 96.600 218.200 90.00 90.00 90.00 P 21 21 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 0.021186 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010352 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004583 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
