HEADER HYDROLASE 13-JUN-08 2VVZ
TITLE STRUCTURE OF THE CATALYTIC DOMAIN OF STREPTOCOCCUS
TITLE 2 PNEUMONIAE SIALIDASE NANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIALIDASE A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 319-822;
COMPND 5 SYNONYM: NANA SIALIDASE, NEURAMINIDASE A;
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: 1313;
SOURCE 4 STRAIN: R36A;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS SECRETED, CELL WALL, SIALIDASE, HYDROLASE,
KEYWDS 2 PEPTIDOGLYCAN-ANCHOR, GLYCOSIDASE, NEURAMINIDASE,
KEYWDS 3 VIRULENCE FACTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR G.XU,X.LI,P.W.ANDREW,G.L.TAYLOR
REVDAT 3 24-FEB-09 2VVZ 1 VERSN
REVDAT 2 16-SEP-08 2VVZ 1 JRNL
REVDAT 1 24-JUN-08 2VVZ 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. 2.5 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 34868
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) : 0.246
REMARK 3 R VALUE (WORKING SET) : 0.243
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1830
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2076
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3270
REMARK 3 BIN FREE R VALUE SET COUNT : 87
REMARK 3 BIN FREE R VALUE : 0.4590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7442
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 124
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.29000
REMARK 3 B22 (A**2) : 0.72000
REMARK 3 B33 (A**2) : -0.43000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.818
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.358
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.257
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.482
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.903
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.852
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7644 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10326 ; 1.145 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 938 ; 7.367 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 366 ;34.184 ;24.426
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1344 ;14.443 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;14.829 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1092 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5842 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3453 ; 0.206 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5031 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 385 ; 0.145 ; 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): 34 ; 0.187 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.123 ; 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): 4788 ; 0.358 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7482 ; 0.633 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3292 ; 0.642 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2844 ; 1.063 ; 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 : 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 2VVZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-08.
REMARK 100 THE PDBE ID CODE IS EBI-36556.
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 : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MRICOMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (SATURN 944)
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200 DATA SCALING SOFTWARE : HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36773
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.50
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 2.9
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.5
REMARK 200 R MERGE FOR SHELL (I) : 0.25
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.60
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: PDB ENTRY 2BF6
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.1M MES PH 6.4
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 24.60300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.29800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.81300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.29800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.60300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.81300
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 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: PQS
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: PQS
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 GLU A 319
REMARK 465 GLY A 320
REMARK 465 ALA A 321
REMARK 465 ASP A 792
REMARK 465 LEU A 793
REMARK 465 ILE A 794
REMARK 465 SER A 795
REMARK 465 PRO A 796
REMARK 465 THR A 797
REMARK 465 GLU A 798
REMARK 465 ALA A 799
REMARK 465 LYS A 800
REMARK 465 VAL A 801
REMARK 465 LYS A 802
REMARK 465 ARG A 803
REMARK 465 THR A 804
REMARK 465 ARG A 805
REMARK 465 GLU A 806
REMARK 465 MET A 807
REMARK 465 GLY A 808
REMARK 465 LYS A 809
REMARK 465 GLY A 810
REMARK 465 VAL A 811
REMARK 465 ILE A 812
REMARK 465 GLY A 813
REMARK 465 LEU A 814
REMARK 465 GLU A 815
REMARK 465 PHE A 816
REMARK 465 ASP A 817
REMARK 465 SER A 818
REMARK 465 GLU A 819
REMARK 465 VAL A 820
REMARK 465 LEU A 821
REMARK 465 VAL A 822
REMARK 465 GLU B 319
REMARK 465 GLY B 320
REMARK 465 ALA B 321
REMARK 465 ASP B 792
REMARK 465 LEU B 793
REMARK 465 ILE B 794
REMARK 465 SER B 795
REMARK 465 PRO B 796
REMARK 465 THR B 797
REMARK 465 GLU B 798
REMARK 465 ALA B 799
REMARK 465 LYS B 800
REMARK 465 VAL B 801
REMARK 465 LYS B 802
REMARK 465 ARG B 803
REMARK 465 THR B 804
REMARK 465 ARG B 805
REMARK 465 GLU B 806
REMARK 465 MET B 807
REMARK 465 GLY B 808
REMARK 465 LYS B 809
REMARK 465 GLY B 810
REMARK 465 VAL B 811
REMARK 465 ILE B 812
REMARK 465 GLY B 813
REMARK 465 LEU B 814
REMARK 465 GLU B 815
REMARK 465 PHE B 816
REMARK 465 ASP B 817
REMARK 465 SER B 818
REMARK 465 GLU B 819
REMARK 465 VAL B 820
REMARK 465 LEU B 821
REMARK 465 VAL B 822
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 OG SER A 332 - O HOH A 2002 2.15
REMARK 500 O THR A 703 - O GLU A 709 1.96
REMARK 500 N ALA A 776 - O HOH A 2002 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 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 ARG A 347 -88.10 -141.38
REMARK 500 HIS A 369 -136.34 -165.05
REMARK 500 ASP A 372 40.46 -78.18
REMARK 500 ASP A 385 32.17 -91.86
REMARK 500 ASP A 417 112.13 66.48
REMARK 500 ILE A 442 -39.52 98.94
REMARK 500 ALA A 472 -99.28 -40.31
REMARK 500 TYR A 473 119.11 66.47
REMARK 500 GLU A 477 -103.19 44.84
REMARK 500 VAL A 481 -82.40 -62.59
REMARK 500 TYR A 482 131.16 97.39
REMARK 500 ALA A 488 76.76 -67.80
REMARK 500 ASP A 490 -152.92 -60.93
REMARK 500 TYR A 491 -56.91 66.11
REMARK 500 LYS A 499 -83.65 169.72
REMARK 500 PRO A 500 -147.49 -75.73
REMARK 500 ALA A 501 34.64 -78.80
REMARK 500 LEU A 514 -120.53 -69.13
REMARK 500 LYS A 564 -82.60 -89.30
REMARK 500 HIS A 597 -112.06 47.51
REMARK 500 THR A 646 -118.95 -118.56
REMARK 500 TYR A 695 61.68 69.51
REMARK 500 GLU A 709 -55.89 -141.67
REMARK 500 TYR A 710 144.34 69.09
REMARK 500 LYS A 720 177.33 78.46
REMARK 500 GLU A 732 -91.75 -79.26
REMARK 500 GLU A 733 -61.89 -140.97
REMARK 500 ALA A 751 -118.66 -124.40
REMARK 500 ALA A 776 103.24 112.21
REMARK 500 ASN B 339 -166.64 -72.09
REMARK 500 ILE B 348 83.08 62.52
REMARK 500 ASP B 372 43.65 -77.60
REMARK 500 ASP B 385 40.23 -102.78
REMARK 500 ASP B 417 123.20 67.42
REMARK 500 PRO B 437 -176.23 -65.90
REMARK 500 ILE B 442 -43.30 99.82
REMARK 500 LYS B 459 95.56 56.96
REMARK 500 ALA B 472 -92.48 -51.75
REMARK 500 TYR B 473 121.85 73.55
REMARK 500 ARG B 476 -150.84 -103.36
REMARK 500 ASP B 490 -51.48 57.52
REMARK 500 LYS B 499 -77.76 -110.58
REMARK 500 PRO B 500 -109.71 -38.64
REMARK 500 ASP B 543 41.70 -96.24
REMARK 500 LYS B 564 -73.26 -88.65
REMARK 500 HIS B 597 -123.34 45.87
REMARK 500 THR B 646 -116.85 -109.49
REMARK 500 TYR B 695 71.11 62.32
REMARK 500 GLU B 709 -30.11 -136.77
REMARK 500 TYR B 710 125.04 70.33
REMARK 500 ASN B 715 -167.06 -163.33
REMARK 500 LYS B 720 178.24 85.26
REMARK 500 LEU B 740 -66.39 -103.59
REMARK 500 ALA B 751 -100.20 -132.64
REMARK 500 ALA B 776 112.08 79.03
REMARK 500 LEU B 779 95.08 48.74
REMARK 500 PHE B 784 149.93 163.07
REMARK 500 TRP B 786 -38.43 154.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 368 HIS A 369 74.19
REMARK 500 VAL A 498 LYS A 499 -45.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 LYS A 499 21.8 L L OUTSIDE RANGE
REMARK 500 LYS B 459 24.9 L L OUTSIDE RANGE
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 DAN A1792
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN B1792
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1793
DBREF 2VVZ A 319 822 UNP P62575 NANA_STRPN 319 822
DBREF 2VVZ B 319 822 UNP P62575 NANA_STRPN 319 822
SEQRES 1 A 504 GLU GLY ALA ALA LEU THR GLU LYS THR ASP ILE PHE GLU
SEQRES 2 A 504 SER GLY ARG ASN GLY LYS PRO ASN LYS ASP GLY ILE LYS
SEQRES 3 A 504 SER TYR ARG ILE PRO ALA LEU LEU LYS THR ASP LYS GLY
SEQRES 4 A 504 THR LEU ILE ALA GLY ALA ASP GLU ARG ARG LEU HIS SER
SEQRES 5 A 504 SER ASP TRP GLY ASP ILE GLY MET VAL ILE ARG ARG SER
SEQRES 6 A 504 GLU ASP ASN GLY LYS THR TRP GLY ASP ARG VAL THR ILE
SEQRES 7 A 504 THR ASN LEU ARG ASP ASN PRO LYS ALA SER ASP PRO SER
SEQRES 8 A 504 ILE GLY SER PRO VAL ASN ILE ASP MET VAL LEU VAL GLN
SEQRES 9 A 504 ASP PRO GLU THR LYS ARG ILE PHE SER ILE TYR ASP MET
SEQRES 10 A 504 PHE PRO GLU GLY LYS GLY ILE PHE GLY MET SER SER GLN
SEQRES 11 A 504 LYS GLU GLU ALA TYR LYS LYS ILE ASP GLY LYS THR TYR
SEQRES 12 A 504 GLN ILE LEU TYR ARG GLU GLY GLU LYS GLY ALA TYR THR
SEQRES 13 A 504 ILE ARG GLU ASN GLY THR VAL TYR THR PRO ASP GLY LYS
SEQRES 14 A 504 ALA THR ASP TYR ARG VAL VAL VAL ASP PRO VAL LYS PRO
SEQRES 15 A 504 ALA TYR SER ASP LYS GLY ASP LEU TYR LYS GLY ASN GLN
SEQRES 16 A 504 LEU LEU GLY ASN ILE TYR PHE THR THR ASN LYS THR SER
SEQRES 17 A 504 PRO PHE ARG ILE ALA LYS ASP SER TYR LEU TRP MET SER
SEQRES 18 A 504 TYR SER ASP ASP ASP GLY LYS THR TRP SER ALA PRO GLN
SEQRES 19 A 504 ASP ILE THR PRO MET VAL LYS ALA ASP TRP MET LYS PHE
SEQRES 20 A 504 LEU GLY VAL GLY PRO GLY THR GLY ILE VAL LEU ARG ASN
SEQRES 21 A 504 GLY PRO HIS LYS GLY ARG ILE LEU ILE PRO VAL TYR THR
SEQRES 22 A 504 THR ASN ASN VAL SER HIS LEU ASN GLY SER GLN SER SER
SEQRES 23 A 504 ARG ILE ILE TYR SER ASP ASP HIS GLY LYS THR TRP HIS
SEQRES 24 A 504 ALA GLY GLU ALA VAL ASN ASP ASN ARG GLN VAL ASP GLY
SEQRES 25 A 504 GLN LYS ILE HIS SER SER THR MET ASN ASN ARG ARG ALA
SEQRES 26 A 504 GLN ASN THR GLU SER THR VAL VAL GLN LEU ASN ASN GLY
SEQRES 27 A 504 ASP VAL LYS LEU PHE MET ARG GLY LEU THR GLY ASP LEU
SEQRES 28 A 504 GLN VAL ALA THR SER LYS ASP GLY GLY VAL THR TRP GLU
SEQRES 29 A 504 LYS ASP ILE LYS ARG TYR PRO GLN VAL LYS ASP VAL TYR
SEQRES 30 A 504 VAL GLN MET SER ALA ILE HIS THR MET HIS GLU GLY LYS
SEQRES 31 A 504 GLU TYR ILE ILE LEU SER ASN ALA GLY GLY PRO LYS ARG
SEQRES 32 A 504 GLU ASN GLY MET VAL HIS LEU ALA ARG VAL GLU GLU ASN
SEQRES 33 A 504 GLY GLU LEU THR TRP LEU LYS HIS ASN PRO ILE GLN LYS
SEQRES 34 A 504 GLY GLU PHE ALA TYR ASN SER LEU GLN GLU LEU GLY ASN
SEQRES 35 A 504 GLY GLU TYR GLY ILE LEU TYR GLU HIS THR GLU LYS GLY
SEQRES 36 A 504 GLN ASN ALA TYR THR LEU SER PHE ARG LYS PHE ASN TRP
SEQRES 37 A 504 ASP PHE LEU SER LYS ASP LEU ILE SER PRO THR GLU ALA
SEQRES 38 A 504 LYS VAL LYS ARG THR ARG GLU MET GLY LYS GLY VAL ILE
SEQRES 39 A 504 GLY LEU GLU PHE ASP SER GLU VAL LEU VAL
SEQRES 1 B 504 GLU GLY ALA ALA LEU THR GLU LYS THR ASP ILE PHE GLU
SEQRES 2 B 504 SER GLY ARG ASN GLY LYS PRO ASN LYS ASP GLY ILE LYS
SEQRES 3 B 504 SER TYR ARG ILE PRO ALA LEU LEU LYS THR ASP LYS GLY
SEQRES 4 B 504 THR LEU ILE ALA GLY ALA ASP GLU ARG ARG LEU HIS SER
SEQRES 5 B 504 SER ASP TRP GLY ASP ILE GLY MET VAL ILE ARG ARG SER
SEQRES 6 B 504 GLU ASP ASN GLY LYS THR TRP GLY ASP ARG VAL THR ILE
SEQRES 7 B 504 THR ASN LEU ARG ASP ASN PRO LYS ALA SER ASP PRO SER
SEQRES 8 B 504 ILE GLY SER PRO VAL ASN ILE ASP MET VAL LEU VAL GLN
SEQRES 9 B 504 ASP PRO GLU THR LYS ARG ILE PHE SER ILE TYR ASP MET
SEQRES 10 B 504 PHE PRO GLU GLY LYS GLY ILE PHE GLY MET SER SER GLN
SEQRES 11 B 504 LYS GLU GLU ALA TYR LYS LYS ILE ASP GLY LYS THR TYR
SEQRES 12 B 504 GLN ILE LEU TYR ARG GLU GLY GLU LYS GLY ALA TYR THR
SEQRES 13 B 504 ILE ARG GLU ASN GLY THR VAL TYR THR PRO ASP GLY LYS
SEQRES 14 B 504 ALA THR ASP TYR ARG VAL VAL VAL ASP PRO VAL LYS PRO
SEQRES 15 B 504 ALA TYR SER ASP LYS GLY ASP LEU TYR LYS GLY ASN GLN
SEQRES 16 B 504 LEU LEU GLY ASN ILE TYR PHE THR THR ASN LYS THR SER
SEQRES 17 B 504 PRO PHE ARG ILE ALA LYS ASP SER TYR LEU TRP MET SER
SEQRES 18 B 504 TYR SER ASP ASP ASP GLY LYS THR TRP SER ALA PRO GLN
SEQRES 19 B 504 ASP ILE THR PRO MET VAL LYS ALA ASP TRP MET LYS PHE
SEQRES 20 B 504 LEU GLY VAL GLY PRO GLY THR GLY ILE VAL LEU ARG ASN
SEQRES 21 B 504 GLY PRO HIS LYS GLY ARG ILE LEU ILE PRO VAL TYR THR
SEQRES 22 B 504 THR ASN ASN VAL SER HIS LEU ASN GLY SER GLN SER SER
SEQRES 23 B 504 ARG ILE ILE TYR SER ASP ASP HIS GLY LYS THR TRP HIS
SEQRES 24 B 504 ALA GLY GLU ALA VAL ASN ASP ASN ARG GLN VAL ASP GLY
SEQRES 25 B 504 GLN LYS ILE HIS SER SER THR MET ASN ASN ARG ARG ALA
SEQRES 26 B 504 GLN ASN THR GLU SER THR VAL VAL GLN LEU ASN ASN GLY
SEQRES 27 B 504 ASP VAL LYS LEU PHE MET ARG GLY LEU THR GLY ASP LEU
SEQRES 28 B 504 GLN VAL ALA THR SER LYS ASP GLY GLY VAL THR TRP GLU
SEQRES 29 B 504 LYS ASP ILE LYS ARG TYR PRO GLN VAL LYS ASP VAL TYR
SEQRES 30 B 504 VAL GLN MET SER ALA ILE HIS THR MET HIS GLU GLY LYS
SEQRES 31 B 504 GLU TYR ILE ILE LEU SER ASN ALA GLY GLY PRO LYS ARG
SEQRES 32 B 504 GLU ASN GLY MET VAL HIS LEU ALA ARG VAL GLU GLU ASN
SEQRES 33 B 504 GLY GLU LEU THR TRP LEU LYS HIS ASN PRO ILE GLN LYS
SEQRES 34 B 504 GLY GLU PHE ALA TYR ASN SER LEU GLN GLU LEU GLY ASN
SEQRES 35 B 504 GLY GLU TYR GLY ILE LEU TYR GLU HIS THR GLU LYS GLY
SEQRES 36 B 504 GLN ASN ALA TYR THR LEU SER PHE ARG LYS PHE ASN TRP
SEQRES 37 B 504 ASP PHE LEU SER LYS ASP LEU ILE SER PRO THR GLU ALA
SEQRES 38 B 504 LYS VAL LYS ARG THR ARG GLU MET GLY LYS GLY VAL ILE
SEQRES 39 B 504 GLY LEU GLU PHE ASP SER GLU VAL LEU VAL
HET DAN A1792 20
HET DAN B1792 20
HET CL A1793 1
HETNAM CL CHLORIDE ION
HETNAM DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID
FORMUL 3 CL CL 1-
FORMUL 4 DAN 2(C11 H17 N O8)
FORMUL 5 HOH *124(H2 O1)
HELIX 1 1 ILE A 554 LYS A 559 1 6
HELIX 2 2 TRP A 786 LYS A 791 1 6
HELIX 3 3 ASP B 407 GLY B 411 5 5
HELIX 4 4 ILE B 554 LYS B 559 1 6
HELIX 5 5 ASN B 578 LYS B 582 5 5
HELIX 6 6 SER B 596 SER B 601 1 6
HELIX 7 7 TRP B 786 LYS B 791 1 6
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 3 SER A 345 TYR A 346 0
SHEET 2 AB 3 LEU A 359 ARG A 366 -1 O ARG A 366 N SER A 345
SHEET 3 AB 3 ALA A 350 LYS A 353 -1 O ALA A 350 N GLY A 362
SHEET 1 AC 4 SER A 345 TYR A 346 0
SHEET 2 AC 4 LEU A 359 ARG A 366 -1 O ARG A 366 N SER A 345
SHEET 3 AC 4 ILE A 376 SER A 383 -1 O GLY A 377 N GLU A 365
SHEET 4 AC 4 VAL A 394 THR A 397 -1 O VAL A 394 N ILE A 380
SHEET 1 AD 5 GLN A 552 ASP A 553 0
SHEET 2 AD 5 TYR A 535 SER A 541 -1 O MET A 538 N GLN A 552
SHEET 3 AD 5 ILE A 429 PHE A 436 -1 O ILE A 429 N SER A 541
SHEET 4 AD 5 VAL A 414 GLN A 422 -1 O VAL A 414 N PHE A 436
SHEET 5 AD 5 GLY A 571 THR A 572 1 O GLY A 571 N LEU A 420
SHEET 1 AE 2 TYR A 453 ILE A 456 0
SHEET 2 AE 2 LYS A 459 GLN A 462 -1 O LYS A 459 N ILE A 456
SHEET 1 AF 2 TYR A 465 ARG A 466 0
SHEET 2 AF 2 PHE A 528 ARG A 529 -1 O ARG A 529 N TYR A 465
SHEET 1 AG 3 VAL A 493 VAL A 494 0
SHEET 2 AG 3 ASP A 507 TYR A 509 -1 O TYR A 509 N VAL A 493
SHEET 3 AG 3 LEU A 515 ASN A 517 -1 O GLY A 516 N LEU A 508
SHEET 1 AH 3 LEU A 566 VAL A 568 0
SHEET 2 AH 3 ILE A 585 THR A 591 -1 O TYR A 590 N GLY A 567
SHEET 3 AH 3 ILE A 574 VAL A 575 -1 O ILE A 574 N LEU A 586
SHEET 1 AI 4 LEU A 566 VAL A 568 0
SHEET 2 AI 4 ILE A 585 THR A 591 -1 O TYR A 590 N GLY A 567
SHEET 3 AI 4 SER A 603 SER A 609 -1 O SER A 603 N THR A 591
SHEET 4 AI 4 HIS A 617 ALA A 618 -1 O HIS A 617 N TYR A 608
SHEET 1 AJ 2 ARG A 626 VAL A 628 0
SHEET 2 AJ 2 GLN A 631 ILE A 633 -1 O GLN A 631 N VAL A 628
SHEET 1 AK 4 SER A 648 GLN A 652 0
SHEET 2 AK 4 VAL A 658 MET A 662 -1 O LYS A 659 N VAL A 651
SHEET 3 AK 4 ASP A 668 SER A 674 -1 O GLN A 670 N MET A 662
SHEET 4 AK 4 LYS A 686 LYS A 692 -1 O LYS A 686 N VAL A 671
SHEET 1 AL 4 SER A 699 HIS A 702 0
SHEET 2 AL 4 ILE A 711 ALA A 716 -1 O ILE A 712 N ILE A 701
SHEET 3 AL 4 GLU A 722 VAL A 731 -1 O MET A 725 N ASN A 715
SHEET 4 AL 4 LEU A 737 GLU A 749 -1 O THR A 738 N ARG A 730
SHEET 1 BA 7 THR B 327 ASP B 328 0
SHEET 2 BA 7 SER B 780 PHE B 784 -1 O PHE B 781 N THR B 327
SHEET 3 BA 7 GLU B 762 HIS B 769 -1 O TYR B 763 N PHE B 784
SHEET 4 BA 7 LEU B 737 GLY B 759 -1 N ALA B 751 O GLU B 768
SHEET 5 BA 7 GLU B 722 VAL B 731 -1 N ASN B 723 O GLY B 748
SHEET 6 BA 7 ILE B 711 ASN B 715 -1 O ILE B 711 N ALA B 729
SHEET 7 BA 7 SER B 699 HIS B 702 -1 O SER B 699 N SER B 714
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 LYS B 455 0
SHEET 2 BD 7 THR B 460 ARG B 466 -1 O TYR B 461 N LYS B 454
SHEET 3 BD 7 THR B 474 ILE B 475 -1 O ILE B 475 N GLN B 462
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 494 -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 VAL B 493
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 LYS B 455 0
SHEET 2 BE 3 THR B 460 ARG B 466 -1 O TYR B 461 N LYS B 454
SHEET 3 BE 3 PHE B 528 ILE B 530 -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
CISPEP 1 LYS A 708 GLU A 709 0 -18.28
CISPEP 2 GLY A 718 PRO A 719 0 -6.62
CISPEP 3 ASN A 734 GLY A 735 0 -10.72
CISPEP 4 ALA A 776 TYR A 777 0 -8.46
CISPEP 5 GLY B 458 LYS B 459 0 -9.99
CISPEP 6 LYS B 708 GLU B 709 0 1.77
CISPEP 7 GLY B 718 PRO B 719 0 -2.66
CISPEP 8 ASN B 734 GLY B 735 0 0.23
CISPEP 9 ALA B 776 TYR B 777 0 0.42
CISPEP 10 ASN B 785 TRP B 786 0 -7.97
SITE 1 AC1 16 ARG A 347 ILE A 348 ARG A 366 ASP A 372
SITE 2 AC1 16 ILE A 416 ASP A 417 ASP A 434 ILE A 442
SITE 3 AC1 16 TYR A 590 LEU A 598 GLN A 602 ARG A 663
SITE 4 AC1 16 TYR A 695 ARG A 721 TYR A 752 HOH A2094
SITE 1 AC2 14 ARG B 347 ILE B 348 ARG B 366 ASP B 372
SITE 2 AC2 14 ILE B 416 ASP B 417 ASP B 434 ILE B 442
SITE 3 AC2 14 TYR B 590 GLN B 602 ARG B 663 TYR B 695
SITE 4 AC2 14 ARG B 721 TYR B 752
SITE 1 AC3 6 GLY A 516 ASN A 517 PHE A 520 LYS A 524
SITE 2 AC3 6 THR A 525 SER A 526
CRYST1 49.206 95.626 226.596 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 0.020323 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010457 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004413 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
