HEADER STRUCTURAL PROTEIN 10-DEC-10 2Y1V
TITLE FULL LENGTH STRUCTURE OF RRGB PILUS PROTEIN FROM STREPTOCOCCUS
TITLE 2 PNEUMONIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL WALL SURFACE ANCHOR FAMILY PROTEIN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: RESIDUES 30-633;
COMPND 5 SYNONYM: RRGB;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: ISOPEPTIDE BONDS K41 AND N184, K193 AND N318, K349 AND
COMPND 8 N428, K453 AND N623
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: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIL (INVITROGEN);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PLIM (PROTEIN EXPERT, GRENOBLE)
KEYWDS STRUCTURAL PROTEIN, MAJOR PILIN, PILUS ASSEMBLY
EXPDTA X-RAY DIFFRACTION
AUTHOR L.EL-MORTAJI,C.CONTRERAS-MARTEL,C.MANZANO,T.VERNET,A.DESSEN,
AUTHOR 2 A.M.DIGUILMI
REVDAT 4 20-DEC-23 2Y1V 1 REMARK LINK
REVDAT 3 30-OCT-19 2Y1V 1 REMARK LINK
REVDAT 2 25-JAN-12 2Y1V 1 JRNL
REVDAT 1 09-NOV-11 2Y1V 0
JRNL AUTH L.EL MORTAJI,C.CONTRERAS-MARTEL,M.MOSCHIONI,I.FERLENGHI,
JRNL AUTH 2 C.MANZANO,T.VERNET,A.DESSEN,A.M.DI GUILMI
JRNL TITL THE FULL-LENGTH STREPTOCOCCUS PNEUMONIAE MAJOR PILIN RRGB
JRNL TITL 2 CRYSTALLIZES IN A FIBRE-LIKE STRUCTURE, WHICH PRESENTS THE
JRNL TITL 3 D1 ISOPEPTIDE BOND AND PROVIDES DETAILS ON THE MECHANISM OF
JRNL TITL 4 PILUS POLYMERIZATION.
JRNL REF BIOCHEM.J. V. 441 833 2012
JRNL REFN ISSN 0264-6021
JRNL PMID 22013894
JRNL DOI 10.1042/BJ20111397
REMARK 2
REMARK 2 RESOLUTION. 2.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 113.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 74075
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.300
REMARK 3 FREE R VALUE TEST SET COUNT : 8548
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) : 2.39
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.45
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4801
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.45
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 528
REMARK 3 BIN FREE R VALUE : 0.3350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13728
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 430
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.74
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 30.78000
REMARK 3 B22 (A**2) : 30.78000
REMARK 3 B33 (A**2) : -61.57000
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): 0.087
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.053
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.186
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.266
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13965 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18990 ; 1.146 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1809 ; 5.364 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 603 ;36.623 ;26.915
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2349 ;14.840 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;12.886 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2229 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10530 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 9006 ; 1.150 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14547 ; 2.035 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4959 ; 3.740 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4443 ; 5.648 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 29 A 632 5
REMARK 3 1 B 29 B 632 5
REMARK 3 2 A 800 A 802 6
REMARK 3 2 B 800 B 802 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2416 ; 0.14 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 2416 ; 0.14 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 2163 ; 0.28 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 B (A): 2163 ; 0.28 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2416 ; 1.99 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 2416 ; 1.99 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 2163 ; 2.98 ; 10.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 2163 ; 2.98 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 29 B 632 5
REMARK 3 1 C 29 C 632 5
REMARK 3 2 B 800 B 802 6
REMARK 3 2 C 800 C 802 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 B (A): 2416 ; 0.34 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 C (A): 2416 ; 0.34 ; 0.50
REMARK 3 LOOSE POSITIONAL 2 B (A): 2163 ; 0.44 ; 5.00
REMARK 3 LOOSE POSITIONAL 2 C (A): 2163 ; 0.44 ; 5.00
REMARK 3 MEDIUM THERMAL 2 B (A**2): 2416 ; 3.54 ; 2.00
REMARK 3 MEDIUM THERMAL 2 C (A**2): 2416 ; 3.54 ; 2.00
REMARK 3 LOOSE THERMAL 2 B (A**2): 2163 ; 3.98 ; 10.00
REMARK 3 LOOSE THERMAL 2 C (A**2): 2163 ; 3.98 ; 10.00
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.592
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : K, H, -L
REMARK 3 TWIN FRACTION : 0.408
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 29 A 188
REMARK 3 RESIDUE RANGE : B 29 B 188
REMARK 3 RESIDUE RANGE : C 29 C 188
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7127 -0.1029 -11.6597
REMARK 3 T TENSOR
REMARK 3 T11: 0.0734 T22: 0.2568
REMARK 3 T33: 0.4319 T12: 0.0567
REMARK 3 T13: 0.0148 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 0.3894 L22: -0.0075
REMARK 3 L33: 0.5693 L12: -0.1012
REMARK 3 L13: -0.0688 L23: -0.0869
REMARK 3 S TENSOR
REMARK 3 S11: 0.0109 S12: 0.0520 S13: -0.0541
REMARK 3 S21: -0.0528 S22: -0.0455 S23: 0.0055
REMARK 3 S31: 0.0811 S32: 0.0838 S33: 0.0346
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 6
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 189 A 329
REMARK 3 RESIDUE RANGE : A 433 A 446
REMARK 3 RESIDUE RANGE : B 189 B 329
REMARK 3 RESIDUE RANGE : B 433 B 446
REMARK 3 RESIDUE RANGE : C 189 C 329
REMARK 3 RESIDUE RANGE : C 433 C 446
REMARK 3 ORIGIN FOR THE GROUP (A): 24.2250 2.6966 0.4910
REMARK 3 T TENSOR
REMARK 3 T11: 0.0079 T22: 0.2905
REMARK 3 T33: 0.3744 T12: 0.0214
REMARK 3 T13: -0.0028 T23: -0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 0.0353 L22: 0.1040
REMARK 3 L33: 0.2718 L12: -0.0641
REMARK 3 L13: 0.0669 L23: -0.0418
REMARK 3 S TENSOR
REMARK 3 S11: 0.0518 S12: -0.0333 S13: -0.0362
REMARK 3 S21: -0.0550 S22: -0.0594 S23: -0.0477
REMARK 3 S31: 0.0852 S32: 0.1510 S33: 0.0075
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 330 A 432
REMARK 3 RESIDUE RANGE : B 330 B 432
REMARK 3 RESIDUE RANGE : C 330 C 432
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5504 -3.3126 1.0343
REMARK 3 T TENSOR
REMARK 3 T11: -0.0020 T22: 0.2222
REMARK 3 T33: 0.3366 T12: -0.0201
REMARK 3 T13: -0.0500 T23: -0.0399
REMARK 3 L TENSOR
REMARK 3 L11: 0.3198 L22: 0.2503
REMARK 3 L33: 0.5386 L12: -0.0552
REMARK 3 L13: -0.2555 L23: -0.0679
REMARK 3 S TENSOR
REMARK 3 S11: 0.0112 S12: 0.0568 S13: -0.0325
REMARK 3 S21: -0.0624 S22: 0.0256 S23: 0.0088
REMARK 3 S31: 0.1359 S32: -0.0446 S33: -0.0367
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 447 A 633
REMARK 3 RESIDUE RANGE : B 447 B 633
REMARK 3 RESIDUE RANGE : C 447 C 633
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8495 1.3101 14.2856
REMARK 3 T TENSOR
REMARK 3 T11: 0.2098 T22: 0.2085
REMARK 3 T33: 0.2093 T12: -0.0003
REMARK 3 T13: -0.0064 T23: 0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.1720 L22: 0.0857
REMARK 3 L33: 0.2528 L12: 0.0540
REMARK 3 L13: -0.1158 L23: -0.1555
REMARK 3 S TENSOR
REMARK 3 S11: 0.0816 S12: -0.0671 S13: 0.0027
REMARK 3 S21: -0.0418 S22: -0.0575 S23: -0.0007
REMARK 3 S31: 0.0742 S32: 0.0753 S33: -0.0241
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES WITH TLS ADDED
REMARK 4
REMARK 4 2Y1V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1290046553.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97485
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 164140
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.390
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.39
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.900
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 2X9W
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23% PEG 8000, 0.1M TRIS PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 227.01800
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 113.50900
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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 GLY A 633
REMARK 465 GLY B 633
REMARK 465 GLY C 633
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASN A 184 ND2
REMARK 470 ASN A 318 ND2
REMARK 470 ASN A 428 ND2
REMARK 470 ASN A 623 ND2
REMARK 470 ASN B 184 ND2
REMARK 470 ASN B 318 ND2
REMARK 470 ASN B 428 ND2
REMARK 470 ASN B 623 ND2
REMARK 470 ASN C 184 ND2
REMARK 470 ASN C 318 ND2
REMARK 470 ASN C 428 ND2
REMARK 470 ASN C 623 ND2
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 NZ LYS A 41 CG ASN A 184 1.32
REMARK 500 NZ LYS B 41 CG ASN B 184 1.33
REMARK 500 NZ LYS A 193 CG ASN A 318 1.33
REMARK 500 NZ LYS C 453 CG ASN C 623 1.33
REMARK 500 NZ LYS C 41 CG ASN C 184 1.33
REMARK 500 NZ LYS C 193 CG ASN C 318 1.33
REMARK 500 NZ LYS A 349 CG ASN A 428 1.33
REMARK 500 NZ LYS A 453 CG ASN A 623 1.33
REMARK 500 NZ LYS C 349 CG ASN C 428 1.33
REMARK 500 NZ LYS B 453 CG ASN B 623 1.33
REMARK 500 NZ LYS B 349 CG ASN B 428 1.33
REMARK 500 NZ LYS B 193 CG ASN B 318 1.33
REMARK 500 NZ LYS C 453 CB ASN C 623 1.96
REMARK 500 OG SER C 486 O HOH C 2091 1.97
REMARK 500 CE LYS C 453 CG ASN C 623 2.01
REMARK 500 OD1 ASN C 60 O ALA C 62 2.07
REMARK 500 O GLU C 423 O HOH C 2084 2.08
REMARK 500 OE1 GLU C 489 O HOH C 2091 2.10
REMARK 500 OD2 ASP B 92 O HOH B 2013 2.11
REMARK 500 CE LYS A 453 CG ASN A 623 2.12
REMARK 500 NZ LYS C 449 OE1 GLN C 605 2.13
REMARK 500 NZ LYS A 41 OD1 ASN A 184 2.14
REMARK 500 ND2 ASN C 238 O HOH C 2038 2.15
REMARK 500 CE LYS C 349 CG ASN C 428 2.18
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 ALA A 30 -29.22 -140.98
REMARK 500 ASP A 46 -143.93 -87.37
REMARK 500 ASN A 54 43.00 -83.51
REMARK 500 GLU A 55 -24.12 -150.39
REMARK 500 GLU A 57 -71.13 -59.76
REMARK 500 PRO A 70 154.41 -49.53
REMARK 500 ALA A 137 179.47 173.46
REMARK 500 THR A 159 -81.87 -109.97
REMARK 500 ASN A 173 -104.94 31.57
REMARK 500 LYS A 196 123.91 -34.81
REMARK 500 PRO A 229 170.90 -57.99
REMARK 500 ALA A 237 88.02 -164.15
REMARK 500 ASP A 260 -20.61 78.51
REMARK 500 TYR A 302 171.71 178.94
REMARK 500 PRO A 315 147.01 -39.37
REMARK 500 ASP A 319 107.56 -165.07
REMARK 500 ALA A 361 121.55 -39.36
REMARK 500 ALA A 363 -175.13 -178.61
REMARK 500 GLU A 432 39.24 70.85
REMARK 500 ASN A 473 -57.07 -130.42
REMARK 500 ALA A 474 -92.40 -109.02
REMARK 500 PRO A 629 -168.93 -76.64
REMARK 500 ASP B 46 -147.65 -90.94
REMARK 500 ASN B 60 -150.14 -123.82
REMARK 500 TYR B 61 -41.94 171.89
REMARK 500 ASN B 87 30.69 -98.98
REMARK 500 ALA B 137 172.95 175.84
REMARK 500 ASP B 154 35.74 38.32
REMARK 500 THR B 159 -78.90 -127.72
REMARK 500 SER B 161 116.50 -161.92
REMARK 500 ALA B 163 21.79 80.87
REMARK 500 ASN B 173 -89.43 66.77
REMARK 500 ASP B 260 -6.08 73.46
REMARK 500 TYR B 302 -170.73 -170.19
REMARK 500 GLU B 313 -13.97 76.96
REMARK 500 ASP B 319 106.24 -160.36
REMARK 500 GLN B 379 157.59 167.90
REMARK 500 THR B 385 -9.92 -59.01
REMARK 500 ASP B 458 19.18 51.94
REMARK 500 ASN B 473 -80.18 -127.56
REMARK 500 ALA B 474 -102.77 -84.27
REMARK 500 ALA C 62 -154.38 -155.47
REMARK 500 ASN C 85 -168.01 -76.15
REMARK 500 PHE C 107 -4.49 67.02
REMARK 500 GLU C 125 34.38 -97.01
REMARK 500 ALA C 137 165.21 173.37
REMARK 500 SER C 146 3.60 -68.31
REMARK 500 THR C 159 -85.45 -128.56
REMARK 500 ALA C 163 29.03 81.80
REMARK 500 ASN C 173 -131.13 48.14
REMARK 500
REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 802 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 245 OE2
REMARK 620 2 HOH A2069 O 86.0
REMARK 620 3 HOH A2093 O 86.1 68.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 801 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 308 OD2
REMARK 620 2 GLU A 489 OE2 152.7
REMARK 620 3 ALA A 536 O 84.0 82.3
REMARK 620 4 ASN A 539 OD1 82.9 113.5 68.8
REMARK 620 5 HOH A2136 O 90.9 112.2 150.9 82.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 800 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 319 OD1
REMARK 620 2 VAL A 320 O 91.6
REMARK 620 3 ASP A 438 OD1 109.0 69.9
REMARK 620 4 PRO A 439 O 151.6 109.2 96.6
REMARK 620 5 GLU A 441 OE1 80.1 131.2 157.9 71.6
REMARK 620 6 GLU A 441 OE2 90.6 84.3 147.5 73.1 48.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 801 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 308 OD2
REMARK 620 2 ALA B 536 O 87.2
REMARK 620 3 ASN B 539 OD1 84.4 77.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 800 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 319 OD1
REMARK 620 2 VAL B 320 O 84.0
REMARK 620 3 ASP B 438 OD1 98.3 72.6
REMARK 620 4 PRO B 439 O 164.5 110.9 82.6
REMARK 620 5 GLU B 441 OE1 91.7 136.6 150.2 80.5
REMARK 620 6 GLU B 441 OE2 106.4 89.2 147.5 79.0 50.7
REMARK 620 7 HOH B2104 O 91.1 143.8 72.7 74.3 79.2 126.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI C 802 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 245 OE2
REMARK 620 2 HOH C2070 O 91.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI C 801 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 308 OD2
REMARK 620 2 GLU C 489 OE2 143.9
REMARK 620 3 ALA C 536 O 79.1 82.8
REMARK 620 4 ASN C 539 OD1 96.1 106.9 70.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI C 800 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 319 OD1
REMARK 620 2 VAL C 320 O 97.8
REMARK 620 3 ASP C 438 OD1 123.7 74.1
REMARK 620 4 GLU C 441 OE2 78.8 75.8 144.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 802
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2X9Z RELATED DB: PDB
REMARK 900 STRUCTURE OF THE PILUS BACKBONE (RRGB) FROM STREPTOCOCCUS PNEUMONIAE
REMARK 900 RELATED ID: 2X9W RELATED DB: PDB
REMARK 900 STRUCTURE OF THE PILUS BACKBONE (RRGB) FROM STREPTOCOCCUS PNEUMONIAE
REMARK 900 RELATED ID: 2X9Y RELATED DB: PDB
REMARK 900 STRUCTURE OF THE PILUS BACKBONE (RRGB) FROM STREPTOCOCCUS PNEUMONIAE
REMARK 900 RELATED ID: 2X9X RELATED DB: PDB
REMARK 900 STRUCTURE OF THE PILUS BACKBONE (RRGB) FROM STREPTOCOCCUS PNEUMONIAE
DBREF 2Y1V A 30 633 UNP Q97SC2 Q97SC2_STRPN 30 633
DBREF 2Y1V B 30 633 UNP Q97SC2 Q97SC2_STRPN 30 633
DBREF 2Y1V C 30 633 UNP Q97SC2 Q97SC2_STRPN 30 633
SEQADV 2Y1V GLY A 29 UNP Q97SC2 EXPRESSION TAG
SEQADV 2Y1V GLY B 29 UNP Q97SC2 EXPRESSION TAG
SEQADV 2Y1V GLY C 29 UNP Q97SC2 EXPRESSION TAG
SEQRES 1 A 605 GLY ALA GLY THR THR THR THR SER VAL THR VAL HIS LYS
SEQRES 2 A 605 LEU LEU ALA THR ASP GLY ASP MSE ASP LYS ILE ALA ASN
SEQRES 3 A 605 GLU LEU GLU THR GLY ASN TYR ALA GLY ASN LYS VAL GLY
SEQRES 4 A 605 VAL LEU PRO ALA ASN ALA LYS GLU ILE ALA GLY VAL MSE
SEQRES 5 A 605 PHE VAL TRP THR ASN THR ASN ASN GLU ILE ILE ASP GLU
SEQRES 6 A 605 ASN GLY GLN THR LEU GLY VAL ASN ILE ASP PRO GLN THR
SEQRES 7 A 605 PHE LYS LEU SER GLY ALA MSE PRO ALA THR ALA MSE LYS
SEQRES 8 A 605 LYS LEU THR GLU ALA GLU GLY ALA LYS PHE ASN THR ALA
SEQRES 9 A 605 ASN LEU PRO ALA ALA LYS TYR LYS ILE TYR GLU ILE HIS
SEQRES 10 A 605 SER LEU SER THR TYR VAL GLY GLU ASP GLY ALA THR LEU
SEQRES 11 A 605 THR GLY SER LYS ALA VAL PRO ILE GLU ILE GLU LEU PRO
SEQRES 12 A 605 LEU ASN ASP VAL VAL ASP ALA HIS VAL TYR PRO LYS ASN
SEQRES 13 A 605 THR GLU ALA LYS PRO LYS ILE ASP LYS ASP PHE LYS GLY
SEQRES 14 A 605 LYS ALA ASN PRO ASP THR PRO ARG VAL ASP LYS ASP THR
SEQRES 15 A 605 PRO VAL ASN HIS GLN VAL GLY ASP VAL VAL GLU TYR GLU
SEQRES 16 A 605 ILE VAL THR LYS ILE PRO ALA LEU ALA ASN TYR ALA THR
SEQRES 17 A 605 ALA ASN TRP SER ASP ARG MSE THR GLU GLY LEU ALA PHE
SEQRES 18 A 605 ASN LYS GLY THR VAL LYS VAL THR VAL ASP ASP VAL ALA
SEQRES 19 A 605 LEU GLU ALA GLY ASP TYR ALA LEU THR GLU VAL ALA THR
SEQRES 20 A 605 GLY PHE ASP LEU LYS LEU THR ASP ALA GLY LEU ALA LYS
SEQRES 21 A 605 VAL ASN ASP GLN ASN ALA GLU LYS THR VAL LYS ILE THR
SEQRES 22 A 605 TYR SER ALA THR LEU ASN ASP LYS ALA ILE VAL GLU VAL
SEQRES 23 A 605 PRO GLU SER ASN ASP VAL THR PHE ASN TYR GLY ASN ASN
SEQRES 24 A 605 PRO ASP HIS GLY ASN THR PRO LYS PRO ASN LYS PRO ASN
SEQRES 25 A 605 GLU ASN GLY ASP LEU THR LEU THR LYS THR TRP VAL ASP
SEQRES 26 A 605 ALA THR GLY ALA PRO ILE PRO ALA GLY ALA GLU ALA THR
SEQRES 27 A 605 PHE ASP LEU VAL ASN ALA GLN THR GLY LYS VAL VAL GLN
SEQRES 28 A 605 THR VAL THR LEU THR THR ASP LYS ASN THR VAL THR VAL
SEQRES 29 A 605 ASN GLY LEU ASP LYS ASN THR GLU TYR LYS PHE VAL GLU
SEQRES 30 A 605 ARG SER ILE LYS GLY TYR SER ALA ASP TYR GLN GLU ILE
SEQRES 31 A 605 THR THR ALA GLY GLU ILE ALA VAL LYS ASN TRP LYS ASP
SEQRES 32 A 605 GLU ASN PRO LYS PRO LEU ASP PRO THR GLU PRO LYS VAL
SEQRES 33 A 605 VAL THR TYR GLY LYS LYS PHE VAL LYS VAL ASN ASP LYS
SEQRES 34 A 605 ASP ASN ARG LEU ALA GLY ALA GLU PHE VAL ILE ALA ASN
SEQRES 35 A 605 ALA ASP ASN ALA GLY GLN TYR LEU ALA ARG LYS ALA ASP
SEQRES 36 A 605 LYS VAL SER GLN GLU GLU LYS GLN LEU VAL VAL THR THR
SEQRES 37 A 605 LYS ASP ALA LEU ASP ARG ALA VAL ALA ALA TYR ASN ALA
SEQRES 38 A 605 LEU THR ALA GLN GLN GLN THR GLN GLN GLU LYS GLU LYS
SEQRES 39 A 605 VAL ASP LYS ALA GLN ALA ALA TYR ASN ALA ALA VAL ILE
SEQRES 40 A 605 ALA ALA ASN ASN ALA PHE GLU TRP VAL ALA ASP LYS ASP
SEQRES 41 A 605 ASN GLU ASN VAL VAL LYS LEU VAL SER ASP ALA GLN GLY
SEQRES 42 A 605 ARG PHE GLU ILE THR GLY LEU LEU ALA GLY THR TYR TYR
SEQRES 43 A 605 LEU GLU GLU THR LYS GLN PRO ALA GLY TYR ALA LEU LEU
SEQRES 44 A 605 THR SER ARG GLN LYS PHE GLU VAL THR ALA THR SER TYR
SEQRES 45 A 605 SER ALA THR GLY GLN GLY ILE GLU TYR THR ALA GLY SER
SEQRES 46 A 605 GLY LYS ASP ASP ALA THR LYS VAL VAL ASN LYS LYS ILE
SEQRES 47 A 605 THR ILE PRO GLN THR GLY GLY
SEQRES 1 B 605 GLY ALA GLY THR THR THR THR SER VAL THR VAL HIS LYS
SEQRES 2 B 605 LEU LEU ALA THR ASP GLY ASP MSE ASP LYS ILE ALA ASN
SEQRES 3 B 605 GLU LEU GLU THR GLY ASN TYR ALA GLY ASN LYS VAL GLY
SEQRES 4 B 605 VAL LEU PRO ALA ASN ALA LYS GLU ILE ALA GLY VAL MSE
SEQRES 5 B 605 PHE VAL TRP THR ASN THR ASN ASN GLU ILE ILE ASP GLU
SEQRES 6 B 605 ASN GLY GLN THR LEU GLY VAL ASN ILE ASP PRO GLN THR
SEQRES 7 B 605 PHE LYS LEU SER GLY ALA MSE PRO ALA THR ALA MSE LYS
SEQRES 8 B 605 LYS LEU THR GLU ALA GLU GLY ALA LYS PHE ASN THR ALA
SEQRES 9 B 605 ASN LEU PRO ALA ALA LYS TYR LYS ILE TYR GLU ILE HIS
SEQRES 10 B 605 SER LEU SER THR TYR VAL GLY GLU ASP GLY ALA THR LEU
SEQRES 11 B 605 THR GLY SER LYS ALA VAL PRO ILE GLU ILE GLU LEU PRO
SEQRES 12 B 605 LEU ASN ASP VAL VAL ASP ALA HIS VAL TYR PRO LYS ASN
SEQRES 13 B 605 THR GLU ALA LYS PRO LYS ILE ASP LYS ASP PHE LYS GLY
SEQRES 14 B 605 LYS ALA ASN PRO ASP THR PRO ARG VAL ASP LYS ASP THR
SEQRES 15 B 605 PRO VAL ASN HIS GLN VAL GLY ASP VAL VAL GLU TYR GLU
SEQRES 16 B 605 ILE VAL THR LYS ILE PRO ALA LEU ALA ASN TYR ALA THR
SEQRES 17 B 605 ALA ASN TRP SER ASP ARG MSE THR GLU GLY LEU ALA PHE
SEQRES 18 B 605 ASN LYS GLY THR VAL LYS VAL THR VAL ASP ASP VAL ALA
SEQRES 19 B 605 LEU GLU ALA GLY ASP TYR ALA LEU THR GLU VAL ALA THR
SEQRES 20 B 605 GLY PHE ASP LEU LYS LEU THR ASP ALA GLY LEU ALA LYS
SEQRES 21 B 605 VAL ASN ASP GLN ASN ALA GLU LYS THR VAL LYS ILE THR
SEQRES 22 B 605 TYR SER ALA THR LEU ASN ASP LYS ALA ILE VAL GLU VAL
SEQRES 23 B 605 PRO GLU SER ASN ASP VAL THR PHE ASN TYR GLY ASN ASN
SEQRES 24 B 605 PRO ASP HIS GLY ASN THR PRO LYS PRO ASN LYS PRO ASN
SEQRES 25 B 605 GLU ASN GLY ASP LEU THR LEU THR LYS THR TRP VAL ASP
SEQRES 26 B 605 ALA THR GLY ALA PRO ILE PRO ALA GLY ALA GLU ALA THR
SEQRES 27 B 605 PHE ASP LEU VAL ASN ALA GLN THR GLY LYS VAL VAL GLN
SEQRES 28 B 605 THR VAL THR LEU THR THR ASP LYS ASN THR VAL THR VAL
SEQRES 29 B 605 ASN GLY LEU ASP LYS ASN THR GLU TYR LYS PHE VAL GLU
SEQRES 30 B 605 ARG SER ILE LYS GLY TYR SER ALA ASP TYR GLN GLU ILE
SEQRES 31 B 605 THR THR ALA GLY GLU ILE ALA VAL LYS ASN TRP LYS ASP
SEQRES 32 B 605 GLU ASN PRO LYS PRO LEU ASP PRO THR GLU PRO LYS VAL
SEQRES 33 B 605 VAL THR TYR GLY LYS LYS PHE VAL LYS VAL ASN ASP LYS
SEQRES 34 B 605 ASP ASN ARG LEU ALA GLY ALA GLU PHE VAL ILE ALA ASN
SEQRES 35 B 605 ALA ASP ASN ALA GLY GLN TYR LEU ALA ARG LYS ALA ASP
SEQRES 36 B 605 LYS VAL SER GLN GLU GLU LYS GLN LEU VAL VAL THR THR
SEQRES 37 B 605 LYS ASP ALA LEU ASP ARG ALA VAL ALA ALA TYR ASN ALA
SEQRES 38 B 605 LEU THR ALA GLN GLN GLN THR GLN GLN GLU LYS GLU LYS
SEQRES 39 B 605 VAL ASP LYS ALA GLN ALA ALA TYR ASN ALA ALA VAL ILE
SEQRES 40 B 605 ALA ALA ASN ASN ALA PHE GLU TRP VAL ALA ASP LYS ASP
SEQRES 41 B 605 ASN GLU ASN VAL VAL LYS LEU VAL SER ASP ALA GLN GLY
SEQRES 42 B 605 ARG PHE GLU ILE THR GLY LEU LEU ALA GLY THR TYR TYR
SEQRES 43 B 605 LEU GLU GLU THR LYS GLN PRO ALA GLY TYR ALA LEU LEU
SEQRES 44 B 605 THR SER ARG GLN LYS PHE GLU VAL THR ALA THR SER TYR
SEQRES 45 B 605 SER ALA THR GLY GLN GLY ILE GLU TYR THR ALA GLY SER
SEQRES 46 B 605 GLY LYS ASP ASP ALA THR LYS VAL VAL ASN LYS LYS ILE
SEQRES 47 B 605 THR ILE PRO GLN THR GLY GLY
SEQRES 1 C 605 GLY ALA GLY THR THR THR THR SER VAL THR VAL HIS LYS
SEQRES 2 C 605 LEU LEU ALA THR ASP GLY ASP MSE ASP LYS ILE ALA ASN
SEQRES 3 C 605 GLU LEU GLU THR GLY ASN TYR ALA GLY ASN LYS VAL GLY
SEQRES 4 C 605 VAL LEU PRO ALA ASN ALA LYS GLU ILE ALA GLY VAL MSE
SEQRES 5 C 605 PHE VAL TRP THR ASN THR ASN ASN GLU ILE ILE ASP GLU
SEQRES 6 C 605 ASN GLY GLN THR LEU GLY VAL ASN ILE ASP PRO GLN THR
SEQRES 7 C 605 PHE LYS LEU SER GLY ALA MSE PRO ALA THR ALA MSE LYS
SEQRES 8 C 605 LYS LEU THR GLU ALA GLU GLY ALA LYS PHE ASN THR ALA
SEQRES 9 C 605 ASN LEU PRO ALA ALA LYS TYR LYS ILE TYR GLU ILE HIS
SEQRES 10 C 605 SER LEU SER THR TYR VAL GLY GLU ASP GLY ALA THR LEU
SEQRES 11 C 605 THR GLY SER LYS ALA VAL PRO ILE GLU ILE GLU LEU PRO
SEQRES 12 C 605 LEU ASN ASP VAL VAL ASP ALA HIS VAL TYR PRO LYS ASN
SEQRES 13 C 605 THR GLU ALA LYS PRO LYS ILE ASP LYS ASP PHE LYS GLY
SEQRES 14 C 605 LYS ALA ASN PRO ASP THR PRO ARG VAL ASP LYS ASP THR
SEQRES 15 C 605 PRO VAL ASN HIS GLN VAL GLY ASP VAL VAL GLU TYR GLU
SEQRES 16 C 605 ILE VAL THR LYS ILE PRO ALA LEU ALA ASN TYR ALA THR
SEQRES 17 C 605 ALA ASN TRP SER ASP ARG MSE THR GLU GLY LEU ALA PHE
SEQRES 18 C 605 ASN LYS GLY THR VAL LYS VAL THR VAL ASP ASP VAL ALA
SEQRES 19 C 605 LEU GLU ALA GLY ASP TYR ALA LEU THR GLU VAL ALA THR
SEQRES 20 C 605 GLY PHE ASP LEU LYS LEU THR ASP ALA GLY LEU ALA LYS
SEQRES 21 C 605 VAL ASN ASP GLN ASN ALA GLU LYS THR VAL LYS ILE THR
SEQRES 22 C 605 TYR SER ALA THR LEU ASN ASP LYS ALA ILE VAL GLU VAL
SEQRES 23 C 605 PRO GLU SER ASN ASP VAL THR PHE ASN TYR GLY ASN ASN
SEQRES 24 C 605 PRO ASP HIS GLY ASN THR PRO LYS PRO ASN LYS PRO ASN
SEQRES 25 C 605 GLU ASN GLY ASP LEU THR LEU THR LYS THR TRP VAL ASP
SEQRES 26 C 605 ALA THR GLY ALA PRO ILE PRO ALA GLY ALA GLU ALA THR
SEQRES 27 C 605 PHE ASP LEU VAL ASN ALA GLN THR GLY LYS VAL VAL GLN
SEQRES 28 C 605 THR VAL THR LEU THR THR ASP LYS ASN THR VAL THR VAL
SEQRES 29 C 605 ASN GLY LEU ASP LYS ASN THR GLU TYR LYS PHE VAL GLU
SEQRES 30 C 605 ARG SER ILE LYS GLY TYR SER ALA ASP TYR GLN GLU ILE
SEQRES 31 C 605 THR THR ALA GLY GLU ILE ALA VAL LYS ASN TRP LYS ASP
SEQRES 32 C 605 GLU ASN PRO LYS PRO LEU ASP PRO THR GLU PRO LYS VAL
SEQRES 33 C 605 VAL THR TYR GLY LYS LYS PHE VAL LYS VAL ASN ASP LYS
SEQRES 34 C 605 ASP ASN ARG LEU ALA GLY ALA GLU PHE VAL ILE ALA ASN
SEQRES 35 C 605 ALA ASP ASN ALA GLY GLN TYR LEU ALA ARG LYS ALA ASP
SEQRES 36 C 605 LYS VAL SER GLN GLU GLU LYS GLN LEU VAL VAL THR THR
SEQRES 37 C 605 LYS ASP ALA LEU ASP ARG ALA VAL ALA ALA TYR ASN ALA
SEQRES 38 C 605 LEU THR ALA GLN GLN GLN THR GLN GLN GLU LYS GLU LYS
SEQRES 39 C 605 VAL ASP LYS ALA GLN ALA ALA TYR ASN ALA ALA VAL ILE
SEQRES 40 C 605 ALA ALA ASN ASN ALA PHE GLU TRP VAL ALA ASP LYS ASP
SEQRES 41 C 605 ASN GLU ASN VAL VAL LYS LEU VAL SER ASP ALA GLN GLY
SEQRES 42 C 605 ARG PHE GLU ILE THR GLY LEU LEU ALA GLY THR TYR TYR
SEQRES 43 C 605 LEU GLU GLU THR LYS GLN PRO ALA GLY TYR ALA LEU LEU
SEQRES 44 C 605 THR SER ARG GLN LYS PHE GLU VAL THR ALA THR SER TYR
SEQRES 45 C 605 SER ALA THR GLY GLN GLY ILE GLU TYR THR ALA GLY SER
SEQRES 46 C 605 GLY LYS ASP ASP ALA THR LYS VAL VAL ASN LYS LYS ILE
SEQRES 47 C 605 THR ILE PRO GLN THR GLY GLY
MODRES 2Y1V MSE A 49 MET SELENOMETHIONINE
MODRES 2Y1V MSE A 80 MET SELENOMETHIONINE
MODRES 2Y1V MSE A 113 MET SELENOMETHIONINE
MODRES 2Y1V MSE A 118 MET SELENOMETHIONINE
MODRES 2Y1V MSE A 243 MET SELENOMETHIONINE
MODRES 2Y1V MSE B 49 MET SELENOMETHIONINE
MODRES 2Y1V MSE B 80 MET SELENOMETHIONINE
MODRES 2Y1V MSE B 113 MET SELENOMETHIONINE
MODRES 2Y1V MSE B 118 MET SELENOMETHIONINE
MODRES 2Y1V MSE B 243 MET SELENOMETHIONINE
MODRES 2Y1V MSE C 49 MET SELENOMETHIONINE
MODRES 2Y1V MSE C 80 MET SELENOMETHIONINE
MODRES 2Y1V MSE C 113 MET SELENOMETHIONINE
MODRES 2Y1V MSE C 118 MET SELENOMETHIONINE
MODRES 2Y1V MSE C 243 MET SELENOMETHIONINE
HET MSE A 49 8
HET MSE A 80 8
HET MSE A 113 8
HET MSE A 118 8
HET MSE A 243 8
HET MSE B 49 8
HET MSE B 80 8
HET MSE B 113 8
HET MSE B 118 8
HET MSE B 243 8
HET MSE C 49 8
HET MSE C 80 8
HET MSE C 113 8
HET MSE C 118 8
HET MSE C 243 8
HET NI A 800 1
HET NI A 801 1
HET NI A 802 1
HET NI B 800 1
HET NI B 801 1
HET NI B 802 1
HET NI C 800 1
HET NI C 801 1
HET NI C 802 1
HETNAM MSE SELENOMETHIONINE
HETNAM NI NICKEL (II) ION
FORMUL 1 MSE 15(C5 H11 N O2 SE)
FORMUL 4 NI 9(NI 2+)
FORMUL 13 HOH *430(H2 O)
HELIX 1 1 MSE A 49 GLU A 57 1 9
HELIX 2 2 HIS A 145 SER A 148 5 4
HELIX 3 3 THR A 282 LYS A 288 1 7
HELIX 4 4 LYS A 481 VAL A 485 5 5
HELIX 5 5 SER A 486 ALA A 509 1 24
HELIX 6 6 THR A 516 ASN A 538 1 23
HELIX 7 7 ASP B 48 GLY B 59 1 12
HELIX 8 8 HIS B 145 SER B 148 5 4
HELIX 9 9 GLY B 152 ALA B 156 5 5
HELIX 10 10 GLU B 264 GLY B 266 5 3
HELIX 11 11 THR B 282 LYS B 288 1 7
HELIX 12 12 ALA B 482 VAL B 485 5 4
HELIX 13 13 SER B 486 LEU B 510 1 25
HELIX 14 14 THR B 516 ASN B 538 1 23
HELIX 15 15 MSE C 49 GLU C 57 1 9
HELIX 16 16 HIS C 145 SER C 148 5 4
HELIX 17 17 GLU C 153 GLY C 155 5 3
HELIX 18 18 GLU C 264 GLY C 266 5 3
HELIX 19 19 THR C 282 ALA C 287 1 6
HELIX 20 20 ALA C 482 VAL C 485 5 4
HELIX 21 21 GLU C 488 ALA C 509 1 22
HELIX 22 22 THR C 516 ASN C 538 1 23
SHEET 1 AA 3 ALA A 127 ASN A 130 0
SHEET 2 AA 3 SER A 36 VAL A 39 -1 O VAL A 37 N PHE A 129
SHEET 3 AA 3 ASP A 177 VAL A 180 1 O ALA A 178 N THR A 38
SHEET 1 AB 4 ALA A 73 GLU A 75 0
SHEET 2 AB 4 LEU A 42 ALA A 44 -1 O LEU A 43 N LYS A 74
SHEET 3 AB 4 LYS A 183 ALA A 187 1 O ASN A 184 N ALA A 44
SHEET 4 AB 4 THR A 157 LYS A 162 -1 O THR A 157 N ALA A 187
SHEET 1 AC 4 LYS A 119 LEU A 121 0
SHEET 2 AC 4 MSE A 80 ASN A 85 -1 O PHE A 81 N LYS A 120
SHEET 3 AC 4 ALA A 137 GLU A 143 -1 O LYS A 140 N THR A 84
SHEET 4 AC 4 ILE A 166 LEU A 170 -1 O ILE A 166 N ILE A 141
SHEET 1 AD 2 GLU A 89 ILE A 91 0
SHEET 2 AD 2 THR A 97 ASN A 101 -1 N LEU A 98 O ILE A 90
SHEET 1 AE 5 LYS A 190 PHE A 195 0
SHEET 2 AE 5 VAL A 219 ILE A 228 -1 O GLU A 223 N ASP A 194
SHEET 3 AE 5 LYS A 296 LEU A 306 -1 O LYS A 296 N ILE A 228
SHEET 4 AE 5 LYS A 255 VAL A 258 -1 O LYS A 255 N THR A 301
SHEET 5 AE 5 VAL A 261 ALA A 262 -1 O VAL A 261 N VAL A 258
SHEET 1 AF 4 LYS A 190 PHE A 195 0
SHEET 2 AF 4 VAL A 219 ILE A 228 -1 O GLU A 223 N ASP A 194
SHEET 3 AF 4 LYS A 296 LEU A 306 -1 O LYS A 296 N ILE A 228
SHEET 4 AF 4 LEU A 247 PHE A 249 -1 O ALA A 248 N THR A 305
SHEET 1 AG 3 VAL A 212 ASN A 213 0
SHEET 2 AG 3 LYS A 443 VAL A 445 1 O LYS A 443 N VAL A 212
SHEET 3 AG 3 GLU A 316 SER A 317 -1 O GLU A 316 N VAL A 444
SHEET 1 AH 4 TYR A 268 VAL A 273 0
SHEET 2 AH 4 GLY A 276 LEU A 281 -1 O GLY A 276 N VAL A 273
SHEET 3 AH 4 THR A 236 ARG A 242 -1 O ALA A 237 N LEU A 281
SHEET 4 AH 4 VAL A 320 GLY A 325 -1 O THR A 321 N SER A 240
SHEET 1 AI 4 THR A 389 VAL A 392 0
SHEET 2 AI 4 LEU A 345 ASP A 353 -1 O LEU A 345 N VAL A 392
SHEET 3 AI 4 GLU A 423 LYS A 430 1 O ILE A 424 N THR A 348
SHEET 4 AI 4 SER A 412 TYR A 415 -1 O SER A 412 N TRP A 429
SHEET 1 AJ 3 VAL A 377 LEU A 383 0
SHEET 2 AJ 3 ALA A 365 ASN A 371 -1 O ALA A 365 N LEU A 383
SHEET 3 AJ 3 TYR A 401 GLU A 405 -1 O LYS A 402 N VAL A 370
SHEET 1 AK 3 ARG A 562 LEU A 568 0
SHEET 2 AK 3 TYR A 447 VAL A 454 -1 O TYR A 447 N LEU A 568
SHEET 3 AK 3 THR A 619 VAL A 622 1 O THR A 619 N VAL A 452
SHEET 1 AL 4 LEU A 555 VAL A 556 0
SHEET 2 AL 4 GLU A 465 ALA A 469 -1 O PHE A 466 N LEU A 555
SHEET 3 AL 4 GLY A 571 LYS A 579 -1 O TYR A 574 N ALA A 469
SHEET 4 AL 4 GLN A 591 VAL A 595 -1 O GLN A 591 N LEU A 575
SHEET 1 AM 2 TYR A 477 ALA A 479 0
SHEET 2 AM 2 GLU A 542 VAL A 544 -1 O GLU A 542 N ALA A 479
SHEET 1 BA 3 ALA B 127 ASN B 130 0
SHEET 2 BA 3 SER B 36 VAL B 39 -1 O VAL B 37 N PHE B 129
SHEET 3 BA 3 ASP B 177 VAL B 180 1 O ALA B 178 N THR B 38
SHEET 1 BB 3 ALA B 73 GLU B 75 0
SHEET 2 BB 3 LEU B 42 ALA B 44 -1 O LEU B 43 N LYS B 74
SHEET 3 BB 3 LYS B 183 ASN B 184 1 O ASN B 184 N ALA B 44
SHEET 1 BC 4 LYS B 119 LEU B 121 0
SHEET 2 BC 4 MSE B 80 ASN B 85 -1 O PHE B 81 N LYS B 120
SHEET 3 BC 4 ALA B 137 ILE B 144 -1 O LYS B 140 N THR B 84
SHEET 4 BC 4 ILE B 166 LEU B 170 -1 O ILE B 166 N ILE B 141
SHEET 1 BD 2 GLU B 89 ILE B 91 0
SHEET 2 BD 2 THR B 97 ASN B 101 -1 N LEU B 98 O ILE B 90
SHEET 1 BE 2 THR B 157 LEU B 158 0
SHEET 2 BE 2 GLU B 186 ALA B 187 -1 O ALA B 187 N THR B 157
SHEET 1 BF 5 LYS B 190 PHE B 195 0
SHEET 2 BF 5 VAL B 219 ILE B 228 -1 O GLU B 223 N ASP B 194
SHEET 3 BF 5 LYS B 296 LEU B 306 -1 O LYS B 296 N ILE B 228
SHEET 4 BF 5 LYS B 255 VAL B 258 -1 O LYS B 255 N THR B 301
SHEET 5 BF 5 VAL B 261 ALA B 262 -1 O VAL B 261 N VAL B 258
SHEET 1 BG 4 LYS B 190 PHE B 195 0
SHEET 2 BG 4 VAL B 219 ILE B 228 -1 O GLU B 223 N ASP B 194
SHEET 3 BG 4 LYS B 296 LEU B 306 -1 O LYS B 296 N ILE B 228
SHEET 4 BG 4 LEU B 247 PHE B 249 -1 O ALA B 248 N THR B 305
SHEET 1 BH 2 VAL B 212 ASN B 213 0
SHEET 2 BH 2 VAL B 444 VAL B 445 1 N VAL B 445 O VAL B 212
SHEET 1 BI 4 TYR B 268 VAL B 273 0
SHEET 2 BI 4 GLY B 276 LEU B 281 -1 O GLY B 276 N VAL B 273
SHEET 3 BI 4 THR B 236 ARG B 242 -1 O ALA B 237 N LEU B 281
SHEET 4 BI 4 VAL B 320 GLY B 325 -1 O THR B 321 N SER B 240
SHEET 1 BJ 4 THR B 389 VAL B 392 0
SHEET 2 BJ 4 LEU B 345 ASP B 353 -1 O LEU B 345 N VAL B 392
SHEET 3 BJ 4 GLU B 423 LYS B 430 1 O ILE B 424 N THR B 348
SHEET 4 BJ 4 SER B 412 TYR B 415 -1 O SER B 412 N TRP B 429
SHEET 1 BK 3 VAL B 377 LEU B 383 0
SHEET 2 BK 3 ALA B 365 ASN B 371 -1 O ALA B 365 N LEU B 383
SHEET 3 BK 3 TYR B 401 GLU B 405 -1 O LYS B 402 N VAL B 370
SHEET 1 BL 3 ARG B 562 LEU B 568 0
SHEET 2 BL 3 TYR B 447 VAL B 454 -1 O TYR B 447 N LEU B 568
SHEET 3 BL 3 THR B 619 VAL B 622 1 O THR B 619 N VAL B 452
SHEET 1 BM 4 LEU B 555 VAL B 556 0
SHEET 2 BM 4 GLU B 465 ALA B 469 -1 O PHE B 466 N LEU B 555
SHEET 3 BM 4 GLY B 571 LYS B 579 -1 O TYR B 574 N ALA B 469
SHEET 4 BM 4 GLN B 591 VAL B 595 -1 O GLN B 591 N LEU B 575
SHEET 1 BN 2 TYR B 477 ARG B 480 0
SHEET 2 BN 2 PHE B 541 VAL B 544 -1 O GLU B 542 N ALA B 479
SHEET 1 CA 3 ALA C 127 ASN C 130 0
SHEET 2 CA 3 SER C 36 VAL C 39 -1 O VAL C 37 N PHE C 129
SHEET 3 CA 3 ASP C 177 VAL C 180 1 O ALA C 178 N THR C 38
SHEET 1 CB 4 ALA C 73 GLU C 75 0
SHEET 2 CB 4 LEU C 42 ALA C 44 -1 O LEU C 43 N LYS C 74
SHEET 3 CB 4 LYS C 183 ALA C 187 1 O ASN C 184 N ALA C 44
SHEET 4 CB 4 THR C 157 LYS C 162 -1 O THR C 157 N ALA C 187
SHEET 1 CC 4 LYS C 119 LEU C 121 0
SHEET 2 CC 4 MSE C 80 THR C 84 -1 O PHE C 81 N LYS C 120
SHEET 3 CC 4 ALA C 137 GLU C 143 -1 O LYS C 140 N THR C 84
SHEET 4 CC 4 ILE C 166 LEU C 170 -1 O ILE C 166 N ILE C 141
SHEET 1 CD 2 GLU C 89 ILE C 91 0
SHEET 2 CD 2 THR C 97 ASN C 101 -1 N LEU C 98 O ILE C 90
SHEET 1 CE 5 LYS C 190 PHE C 195 0
SHEET 2 CE 5 VAL C 219 ILE C 228 -1 O GLU C 223 N ASP C 194
SHEET 3 CE 5 LYS C 296 LEU C 306 -1 O LYS C 296 N ILE C 228
SHEET 4 CE 5 LYS C 255 VAL C 258 -1 O LYS C 255 N THR C 301
SHEET 5 CE 5 VAL C 261 ALA C 262 -1 O VAL C 261 N VAL C 258
SHEET 1 CF 4 LYS C 190 PHE C 195 0
SHEET 2 CF 4 VAL C 219 ILE C 228 -1 O GLU C 223 N ASP C 194
SHEET 3 CF 4 LYS C 296 LEU C 306 -1 O LYS C 296 N ILE C 228
SHEET 4 CF 4 LEU C 247 PHE C 249 -1 O ALA C 248 N THR C 305
SHEET 1 CG 2 VAL C 212 ASN C 213 0
SHEET 2 CG 2 VAL C 444 VAL C 445 1 N VAL C 445 O VAL C 212
SHEET 1 CH 4 TYR C 268 VAL C 273 0
SHEET 2 CH 4 GLY C 276 LEU C 281 -1 O GLY C 276 N VAL C 273
SHEET 3 CH 4 THR C 236 ARG C 242 -1 O ALA C 237 N LEU C 281
SHEET 4 CH 4 VAL C 320 GLY C 325 -1 O THR C 321 N SER C 240
SHEET 1 CI 4 THR C 389 VAL C 392 0
SHEET 2 CI 4 LEU C 345 VAL C 352 -1 O LEU C 345 N VAL C 392
SHEET 3 CI 4 GLU C 423 TRP C 429 1 O ILE C 424 N THR C 348
SHEET 4 CI 4 SER C 412 TYR C 415 -1 O SER C 412 N TRP C 429
SHEET 1 CJ 3 VAL C 377 LEU C 383 0
SHEET 2 CJ 3 ALA C 365 ASN C 371 -1 O ALA C 365 N LEU C 383
SHEET 3 CJ 3 TYR C 401 GLU C 405 -1 O LYS C 402 N VAL C 370
SHEET 1 CK 3 ARG C 562 LEU C 568 0
SHEET 2 CK 3 TYR C 447 VAL C 454 -1 O TYR C 447 N LEU C 568
SHEET 3 CK 3 THR C 619 VAL C 622 1 O THR C 619 N VAL C 452
SHEET 1 CL 4 LEU C 555 VAL C 556 0
SHEET 2 CL 4 GLU C 465 ALA C 469 -1 O PHE C 466 N LEU C 555
SHEET 3 CL 4 GLY C 571 LYS C 579 -1 O TYR C 574 N ALA C 469
SHEET 4 CL 4 GLN C 591 VAL C 595 -1 O GLN C 591 N LEU C 575
SHEET 1 CM 2 TYR C 477 ARG C 480 0
SHEET 2 CM 2 PHE C 541 VAL C 544 -1 O GLU C 542 N ALA C 479
LINK C ASP A 48 N MSE A 49 1555 1555 1.32
LINK C MSE A 49 N ASP A 50 1555 1555 1.33
LINK C VAL A 79 N MSE A 80 1555 1555 1.34
LINK C MSE A 80 N PHE A 81 1555 1555 1.33
LINK C ALA A 112 N MSE A 113 1555 1555 1.33
LINK C MSE A 113 N PRO A 114 1555 1555 1.34
LINK C ALA A 117 N MSE A 118 1555 1555 1.32
LINK C MSE A 118 N LYS A 119 1555 1555 1.33
LINK C ARG A 242 N MSE A 243 1555 1555 1.33
LINK C MSE A 243 N THR A 244 1555 1555 1.34
LINK C ASP B 48 N MSE B 49 1555 1555 1.33
LINK C MSE B 49 N ASP B 50 1555 1555 1.33
LINK C VAL B 79 N MSE B 80 1555 1555 1.33
LINK C MSE B 80 N PHE B 81 1555 1555 1.33
LINK C ALA B 112 N MSE B 113 1555 1555 1.33
LINK C MSE B 113 N PRO B 114 1555 1555 1.34
LINK C ALA B 117 N MSE B 118 1555 1555 1.32
LINK C MSE B 118 N LYS B 119 1555 1555 1.33
LINK C ARG B 242 N MSE B 243 1555 1555 1.32
LINK C MSE B 243 N THR B 244 1555 1555 1.33
LINK C ASP C 48 N MSE C 49 1555 1555 1.33
LINK C MSE C 49 N ASP C 50 1555 1555 1.33
LINK C VAL C 79 N MSE C 80 1555 1555 1.33
LINK C MSE C 80 N PHE C 81 1555 1555 1.33
LINK C ALA C 112 N MSE C 113 1555 1555 1.33
LINK C MSE C 113 N PRO C 114 1555 1555 1.35
LINK C ALA C 117 N MSE C 118 1555 1555 1.33
LINK C MSE C 118 N LYS C 119 1555 1555 1.34
LINK C ARG C 242 N MSE C 243 1555 1555 1.33
LINK C MSE C 243 N THR C 244 1555 1555 1.33
LINK OE2 GLU A 245 NI NI A 802 1555 1555 1.87
LINK OD2 ASP A 308 NI NI A 801 1555 1555 2.34
LINK OD1 ASP A 319 NI NI A 800 1555 1555 2.16
LINK O VAL A 320 NI NI A 800 1555 1555 2.65
LINK OD1 ASP A 438 NI NI A 800 1555 1555 2.40
LINK O PRO A 439 NI NI A 800 1555 1555 2.53
LINK OE1 GLU A 441 NI NI A 800 1555 1555 2.79
LINK OE2 GLU A 441 NI NI A 800 1555 1555 2.57
LINK OE2 GLU A 489 NI NI A 801 1555 1555 2.23
LINK O ALA A 536 NI NI A 801 1555 1555 2.52
LINK OD1 ASN A 539 NI NI A 801 1555 1555 2.61
LINK NI NI A 801 O HOH A2136 1555 1555 2.59
LINK NI NI A 802 O HOH A2069 1555 1555 2.48
LINK NI NI A 802 O HOH A2093 1555 1555 2.57
LINK OE2 GLU B 245 NI NI B 802 1555 1555 2.55
LINK OD2 ASP B 308 NI NI B 801 1555 1555 2.28
LINK OD1 ASP B 319 NI NI B 800 1555 1555 2.47
LINK O VAL B 320 NI NI B 800 1555 1555 2.58
LINK OD1 ASP B 438 NI NI B 800 1555 1555 2.46
LINK O PRO B 439 NI NI B 800 1555 1555 2.44
LINK OE1 GLU B 441 NI NI B 800 1555 1555 2.29
LINK OE2 GLU B 441 NI NI B 800 1555 1555 2.78
LINK O ALA B 536 NI NI B 801 1555 1555 2.26
LINK OD1 ASN B 539 NI NI B 801 1555 1555 2.55
LINK NI NI B 800 O HOH B2104 1555 1555 2.45
LINK OE2 GLU C 245 NI NI C 802 1555 1555 2.35
LINK OD2 ASP C 308 NI NI C 801 1555 1555 2.37
LINK OD1 ASP C 319 NI NI C 800 1555 1555 2.15
LINK O VAL C 320 NI NI C 800 1555 1555 2.64
LINK OD1 ASP C 438 NI NI C 800 1555 1555 2.27
LINK OE2 GLU C 441 NI NI C 800 1555 1555 2.37
LINK OE2 GLU C 489 NI NI C 801 1555 1555 2.59
LINK O ALA C 536 NI NI C 801 1555 1555 2.62
LINK OD1 ASN C 539 NI NI C 801 1555 1555 2.40
LINK NI NI C 802 O HOH C2070 1555 1555 2.74
CISPEP 1 VAL A 164 PRO A 165 0 -0.11
CISPEP 2 LEU A 170 PRO A 171 0 -0.82
CISPEP 3 VAL B 164 PRO B 165 0 1.18
CISPEP 4 LEU B 170 PRO B 171 0 2.61
CISPEP 5 VAL C 164 PRO C 165 0 5.08
CISPEP 6 LEU C 170 PRO C 171 0 3.66
SITE 1 AC1 5 ASP A 319 VAL A 320 ASP A 438 PRO A 439
SITE 2 AC1 5 GLU A 441
SITE 1 AC2 5 ASP A 308 GLU A 489 ALA A 536 ASN A 539
SITE 2 AC2 5 HOH A2136
SITE 1 AC3 3 GLU A 245 HOH A2069 HOH A2093
SITE 1 AC4 6 ASP B 319 VAL B 320 ASP B 438 PRO B 439
SITE 2 AC4 6 GLU B 441 HOH B2104
SITE 1 AC5 4 ASP B 308 GLU B 489 ALA B 536 ASN B 539
SITE 1 AC6 2 GLU B 245 HOH B2070
SITE 1 AC7 5 ASP C 319 VAL C 320 ASP C 438 PRO C 439
SITE 2 AC7 5 GLU C 441
SITE 1 AC8 4 ASP C 308 GLU C 489 ALA C 536 ASN C 539
SITE 1 AC9 2 GLU C 245 HOH C2070
CRYST1 74.619 74.619 340.527 90.00 90.00 120.00 P 32 9
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 0.013401 0.007737 0.000000 0.00000
SCALE2 0.000000 0.015475 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002937 0.00000
MTRIX1 1 0.999991 0.000886 -0.004114 -37.25830 1
MTRIX2 1 0.000896 -0.999997 0.002454 21.83410 1
MTRIX3 1 -0.004111 -0.002457 -0.999988 0.38649 1
MTRIX1 2 0.442967 0.896182 -0.025255 34.50905 1
MTRIX2 2 0.883768 -0.441221 -0.155812 -19.01812 1
MTRIX3 2 -0.150779 0.046700 -0.987464 -15.20364 1
(ATOM LINES ARE NOT SHOWN.)
END
