HEADER TRANSPORT 10-FEB-06 2CEX
TITLE STRUCTURE OF A SIALIC ACID BINDING PROTEIN (SIAP) IN THE PRESENCE OF
TITLE 2 THE SIALIC ACID ACID ANALOGUE NEU5AC2EN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN HI0146;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: SIAP;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;
SOURCE 3 ORGANISM_TAXID: 727;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS ESR, PERIPLASMIC BINDING PROTEIN, TRIPARTITE ATP-INDEPENDENT
KEYWDS 2 PERIPLASMIC (TRAP)TRANSPORT, VIRULENCE FACTOR, TRANSPORT,
KEYWDS 3 PERIPLASMIC
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MULLER,E.SEVERI,C.MULLIGAN,A.G.WATTS,D.J.KELLY,K.S.WILSON,
AUTHOR 2 A.J.WILKINSON,G.H.THOMAS
REVDAT 5 29-JUL-20 2CEX 1 REMARK LINK SITE
REVDAT 4 13-JUL-11 2CEX 1 VERSN
REVDAT 3 24-FEB-09 2CEX 1 VERSN
REVDAT 2 02-AUG-06 2CEX 1 JRNL
REVDAT 1 15-MAY-06 2CEX 0
JRNL AUTH A.MULLER,E.SEVERI,C.MULLIGAN,A.G.WATTS,D.J.KELLY,K.S.WILSON,
JRNL AUTH 2 A.J.WILKINSON,G.H.THOMAS
JRNL TITL CONSERVATION OF STRUCTURE AND MECHANISM IN PRIMARY AND
JRNL TITL 2 SECONDARY TRANSPORTERS EXEMPLIFIED BY SIAP, A SIALIC ACID
JRNL TITL 3 BINDING VIRULENCE FACTOR FROM HAEMOPHILUS INFLUENZAE
JRNL REF J.BIOL.CHEM. V. 281 22212 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16702222
JRNL DOI 10.1074/JBC.M603463200
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 111.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 75.6
REMARK 3 NUMBER OF REFLECTIONS : 46872
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2500
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 519
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 11.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE SET COUNT : 32
REMARK 3 BIN FREE R VALUE : 0.5380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9515
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 455
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.12000
REMARK 3 B22 (A**2) : 0.32000
REMARK 3 B33 (A**2) : -0.39000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.10000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.588
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.319
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.239
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.616
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.877
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9745 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 8677 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13156 ; 1.727 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20357 ; 0.985 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1211 ; 7.370 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 447 ;39.814 ;25.928
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1727 ;18.282 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;11.805 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1456 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10829 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1865 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2330 ; 0.198 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 9009 ; 0.182 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4651 ; 0.177 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 5407 ; 0.093 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 524 ; 0.194 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.015 ; 0.200
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 4 ; 0.164 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 25 ; 0.153 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 74 ; 0.222 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.168 ; 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): 6307 ; 0.629 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2452 ; 0.143 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9703 ; 0.997 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4035 ; 1.678 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3453 ; 2.492 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 125
REMARK 3 RESIDUE RANGE : A 213 A 254
REMARK 3 ORIGIN FOR THE GROUP (A): 21.4131 22.8058 5.1413
REMARK 3 T TENSOR
REMARK 3 T11: -0.0156 T22: 0.0907
REMARK 3 T33: -0.0542 T12: -0.0376
REMARK 3 T13: 0.0120 T23: -0.0824
REMARK 3 L TENSOR
REMARK 3 L11: 2.4700 L22: 2.3482
REMARK 3 L33: 3.1825 L12: 0.7342
REMARK 3 L13: 0.3119 L23: 1.6397
REMARK 3 S TENSOR
REMARK 3 S11: -0.1434 S12: 0.5214 S13: -0.3669
REMARK 3 S21: -0.3648 S22: 0.2476 S23: -0.1980
REMARK 3 S31: 0.0224 S32: 0.2084 S33: -0.1043
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 126 A 210
REMARK 3 RESIDUE RANGE : A 256 A 288
REMARK 3 ORIGIN FOR THE GROUP (A): 29.1313 34.0147 29.4307
REMARK 3 T TENSOR
REMARK 3 T11: -0.1334 T22: 0.0595
REMARK 3 T33: -0.0598 T12: -0.0147
REMARK 3 T13: 0.0184 T23: -0.0754
REMARK 3 L TENSOR
REMARK 3 L11: 1.3339 L22: 1.2433
REMARK 3 L33: 2.0520 L12: 0.5987
REMARK 3 L13: -0.0373 L23: -0.4611
REMARK 3 S TENSOR
REMARK 3 S11: -0.1345 S12: -0.1668 S13: -0.0784
REMARK 3 S21: -0.0831 S22: 0.0471 S23: -0.2092
REMARK 3 S31: 0.0862 S32: 0.2716 S33: 0.0874
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 125
REMARK 3 RESIDUE RANGE : B 213 B 254
REMARK 3 ORIGIN FOR THE GROUP (A): 55.7230 9.2720 17.9220
REMARK 3 T TENSOR
REMARK 3 T11: -0.1417 T22: -0.0337
REMARK 3 T33: -0.1273 T12: -0.0252
REMARK 3 T13: 0.0083 T23: 0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 1.9184 L22: 2.1295
REMARK 3 L33: 1.4042 L12: -0.0403
REMARK 3 L13: -0.0801 L23: 0.1777
REMARK 3 S TENSOR
REMARK 3 S11: -0.0496 S12: 0.2123 S13: 0.2263
REMARK 3 S21: -0.1921 S22: 0.0495 S23: 0.0951
REMARK 3 S31: -0.1736 S32: -0.1349 S33: 0.0001
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 126 B 210
REMARK 3 RESIDUE RANGE : B 256 B 300
REMARK 3 ORIGIN FOR THE GROUP (A): 63.7782 -4.0356 34.3025
REMARK 3 T TENSOR
REMARK 3 T11: -0.1447 T22: -0.0417
REMARK 3 T33: -0.1082 T12: -0.0173
REMARK 3 T13: 0.0227 T23: -0.0300
REMARK 3 L TENSOR
REMARK 3 L11: 2.3832 L22: 1.6256
REMARK 3 L33: 1.1658 L12: 0.3349
REMARK 3 L13: 0.6427 L23: 0.5118
REMARK 3 S TENSOR
REMARK 3 S11: -0.0048 S12: -0.1325 S13: 0.0594
REMARK 3 S21: 0.1637 S22: 0.0170 S23: -0.0346
REMARK 3 S31: 0.0461 S32: -0.0429 S33: -0.0121
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 2 C 125
REMARK 3 RESIDUE RANGE : C 213 C 254
REMARK 3 ORIGIN FOR THE GROUP (A): 24.8345 -15.5269 24.6442
REMARK 3 T TENSOR
REMARK 3 T11: -0.0954 T22: 0.2432
REMARK 3 T33: -0.0037 T12: -0.1301
REMARK 3 T13: 0.0289 T23: -0.0763
REMARK 3 L TENSOR
REMARK 3 L11: 3.1587 L22: 0.7805
REMARK 3 L33: 2.3253 L12: 1.3037
REMARK 3 L13: -0.5802 L23: -0.1161
REMARK 3 S TENSOR
REMARK 3 S11: -0.3140 S12: 0.8929 S13: -0.3740
REMARK 3 S21: -0.2513 S22: 0.2326 S23: -0.0758
REMARK 3 S31: 0.2737 S32: -0.4371 S33: 0.0814
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 126 C 210
REMARK 3 RESIDUE RANGE : C 256 C 300
REMARK 3 ORIGIN FOR THE GROUP (A): 30.9496 -5.2642 48.0820
REMARK 3 T TENSOR
REMARK 3 T11: -0.1294 T22: -0.0141
REMARK 3 T33: -0.0834 T12: 0.0069
REMARK 3 T13: -0.0084 T23: -0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 2.1874 L22: 1.0202
REMARK 3 L33: 2.5331 L12: 0.6629
REMARK 3 L13: -0.8149 L23: -1.0746
REMARK 3 S TENSOR
REMARK 3 S11: 0.0142 S12: -0.0111 S13: -0.0928
REMARK 3 S21: -0.0366 S22: -0.0338 S23: -0.1291
REMARK 3 S31: 0.0159 S32: 0.2036 S33: 0.0197
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 2 D 125
REMARK 3 RESIDUE RANGE : D 213 D 254
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6894 3.7238 30.6403
REMARK 3 T TENSOR
REMARK 3 T11: -0.0855 T22: -0.1015
REMARK 3 T33: -0.0660 T12: -0.0237
REMARK 3 T13: 0.0010 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 0.9770 L22: 1.6865
REMARK 3 L33: 1.0796 L12: 0.0694
REMARK 3 L13: 0.0420 L23: -0.7756
REMARK 3 S TENSOR
REMARK 3 S11: -0.0625 S12: -0.0055 S13: 0.0878
REMARK 3 S21: -0.1681 S22: 0.0288 S23: 0.1582
REMARK 3 S31: 0.0234 S32: -0.0916 S33: 0.0337
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 126 D 210
REMARK 3 RESIDUE RANGE : D 256 D 300
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8558 -7.0892 54.8517
REMARK 3 T TENSOR
REMARK 3 T11: -0.0949 T22: -0.0148
REMARK 3 T33: -0.0809 T12: -0.0062
REMARK 3 T13: 0.0329 T23: 0.0569
REMARK 3 L TENSOR
REMARK 3 L11: 1.5804 L22: 0.4838
REMARK 3 L33: 2.6641 L12: 0.2440
REMARK 3 L13: 0.6871 L23: 0.6958
REMARK 3 S TENSOR
REMARK 3 S11: -0.0162 S12: -0.3416 S13: 0.0700
REMARK 3 S21: 0.1093 S22: -0.0817 S23: 0.1835
REMARK 3 S31: 0.0247 S32: -0.3106 S33: 0.0979
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2CEX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1290027691.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97624
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49350
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 75.7
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 12.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.30
REMARK 200 R MERGE FOR SHELL (I) : 0.56000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5 MM NEU5AC2EN, 5 MM ZINC ACETATE,0.1
REMARK 280 M TRIS-HCL PH 8.5, 0.2 M MAGNESIUM CHLORIDE, 25 % PEG 3350, PH
REMARK 280 8.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 65.72400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.35050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 65.72400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 44.35050
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, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 1
REMARK 465 PRO A 306
REMARK 465 ALA B 1
REMARK 465 ALA C 1
REMARK 465 SER C 32
REMARK 465 GLN C 33
REMARK 465 GLY C 34
REMARK 465 LYS C 35
REMARK 465 PRO C 306
REMARK 465 PRO D 306
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 GLU A 30 CD OE1 OE2
REMARK 470 ARG A 50 CZ NH1 NH2
REMARK 470 LYS A 54 CE NZ
REMARK 470 LYS A 57 CE NZ
REMARK 470 GLU A 101 CG CD OE1 OE2
REMARK 470 LYS A 145 CE NZ
REMARK 470 LEU A 175 CD1 CD2
REMARK 470 GLU A 221 CD OE1 OE2
REMARK 470 GLU A 228 CG CD OE1 OE2
REMARK 470 LYS A 247 CE NZ
REMARK 470 GLN A 289 CD OE1 NE2
REMARK 470 LYS A 299 CG CD CE NZ
REMARK 470 LYS C 6 CD CE NZ
REMARK 470 LYS C 26 CG CD CE NZ
REMARK 470 GLU C 37 CG CD OE1 OE2
REMARK 470 GLU C 295 CG CD OE1 OE2
REMARK 470 LYS C 299 O
REMARK 470 GLU C 302 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 113 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP C 99 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 111 -71.09 -78.26
REMARK 500 ASN A 187 156.43 159.97
REMARK 500 LYS A 196 31.56 70.10
REMARK 500 ILE A 304 -85.84 -82.44
REMARK 500 TYR B 85 -11.76 68.64
REMARK 500 ASN B 187 149.93 169.39
REMARK 500 TYR C 3 93.97 59.07
REMARK 500 LYS C 29 76.39 -63.33
REMARK 500 TYR C 85 -2.60 72.05
REMARK 500 LYS C 145 98.60 -69.41
REMARK 500 MET C 168 142.41 -179.66
REMARK 500 ASN C 187 163.47 168.26
REMARK 500 ASN C 208 43.42 39.98
REMARK 500 GLN C 292 11.32 -60.15
REMARK 500 LYS C 293 41.39 -96.78
REMARK 500 ALA C 303 -26.00 -39.70
REMARK 500 ILE C 304 -52.02 -134.55
REMARK 500 MET D 168 136.45 -170.51
REMARK 500 ASN D 187 155.65 169.62
REMARK 500 GLN D 292 -43.69 -29.76
REMARK 500 ILE D 304 2.79 -63.18
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 GLU C 30 LYS C 31 -135.09
REMARK 500 GLN C 292 LYS C 293 149.84
REMARK 500 LYS C 293 GLY C 294 130.67
REMARK 500 ALA D 1 ASP D 2 35.08
REMARK 500 GLU D 186 ASN D 187 -145.66
REMARK 500 GLY D 291 GLN D 292 147.74
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 ZN A1306 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 2 OD1
REMARK 620 2 ASP A 2 OD2 58.1
REMARK 620 3 ASP A 4 OD1 86.4 102.4
REMARK 620 4 ASP A 4 OD2 133.4 99.8 56.8
REMARK 620 5 HOH A2088 O 117.3 149.9 107.0 101.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1310 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 269 NE2
REMARK 620 2 HIS B 269 NE2 106.7
REMARK 620 3 HOH B2145 O 114.8 105.2
REMARK 620 4 HOH B2146 O 113.8 101.5 113.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1311 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 2 OD1
REMARK 620 2 ASP B 2 OD2 56.1
REMARK 620 3 ASP B 4 OD2 113.4 103.6
REMARK 620 4 HOH B2147 O 140.7 131.4 102.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1307 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 2 OD1
REMARK 620 2 ASP C 2 OD2 56.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1306 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 269 NE2
REMARK 620 2 HOH C2096 O 104.1
REMARK 620 3 HOH C2097 O 101.2 116.5
REMARK 620 4 HIS D 269 NE2 117.1 114.7 102.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1307 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 2 OD2
REMARK 620 2 ASP D 2 OD1 56.6
REMARK 620 3 ASP D 4 OD1 100.1 83.0
REMARK 620 4 ASP D 4 OD2 96.8 129.4 58.2
REMARK 620 5 HOH D2122 O 168.8 122.7 90.8 91.4
REMARK 620 N 1 2 3 4
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CEY RELATED DB: PDB
REMARK 900 APO STRUCTURE OF SIAP
DBREF 2CEX A 1 306 UNP P44542 Y146_HAEIN 24 329
DBREF 2CEX B 1 306 UNP P44542 Y146_HAEIN 24 329
DBREF 2CEX C 1 306 UNP P44542 Y146_HAEIN 24 329
DBREF 2CEX D 1 306 UNP P44542 Y146_HAEIN 24 329
SEQRES 1 A 306 ALA ASP TYR ASP LEU LYS PHE GLY MET ASN ALA GLY THR
SEQRES 2 A 306 SER SER ASN GLU TYR LYS ALA ALA GLU MET PHE ALA LYS
SEQRES 3 A 306 GLU VAL LYS GLU LYS SER GLN GLY LYS ILE GLU ILE SER
SEQRES 4 A 306 LEU TYR PRO SER SER GLN LEU GLY ASP ASP ARG ALA MET
SEQRES 5 A 306 LEU LYS GLN LEU LYS ASP GLY SER LEU ASP PHE THR PHE
SEQRES 6 A 306 ALA GLU SER ALA ARG PHE GLN LEU PHE TYR PRO GLU ALA
SEQRES 7 A 306 ALA VAL PHE ALA LEU PRO TYR VAL ILE SER ASN TYR ASN
SEQRES 8 A 306 VAL ALA GLN LYS ALA LEU PHE ASP THR GLU PHE GLY LYS
SEQRES 9 A 306 ASP LEU ILE LYS LYS MET ASP LYS ASP LEU GLY VAL THR
SEQRES 10 A 306 LEU LEU SER GLN ALA TYR ASN GLY THR ARG GLN THR THR
SEQRES 11 A 306 SER ASN ARG ALA ILE ASN SER ILE ALA ASP MET LYS GLY
SEQRES 12 A 306 LEU LYS LEU ARG VAL PRO ASN ALA ALA THR ASN LEU ALA
SEQRES 13 A 306 TYR ALA LYS TYR VAL GLY ALA SER PRO THR PRO MET ALA
SEQRES 14 A 306 PHE SER GLU VAL TYR LEU ALA LEU GLN THR ASN ALA VAL
SEQRES 15 A 306 ASP GLY GLN GLU ASN PRO LEU ALA ALA VAL GLN ALA GLN
SEQRES 16 A 306 LYS PHE TYR GLU VAL GLN LYS PHE LEU ALA MET THR ASN
SEQRES 17 A 306 HIS ILE LEU ASN ASP GLN LEU TYR LEU VAL SER ASN GLU
SEQRES 18 A 306 THR TYR LYS GLU LEU PRO GLU ASP LEU GLN LYS VAL VAL
SEQRES 19 A 306 LYS ASP ALA ALA GLU ASN ALA ALA LYS TYR HIS THR LYS
SEQRES 20 A 306 LEU PHE VAL ASP GLY GLU LYS ASP LEU VAL THR PHE PHE
SEQRES 21 A 306 GLU LYS GLN GLY VAL LYS ILE THR HIS PRO ASP LEU VAL
SEQRES 22 A 306 PRO PHE LYS GLU SER MET LYS PRO TYR TYR ALA GLU PHE
SEQRES 23 A 306 VAL LYS GLN THR GLY GLN LYS GLY GLU SER ALA LEU LYS
SEQRES 24 A 306 GLN ILE GLU ALA ILE ASN PRO
SEQRES 1 B 306 ALA ASP TYR ASP LEU LYS PHE GLY MET ASN ALA GLY THR
SEQRES 2 B 306 SER SER ASN GLU TYR LYS ALA ALA GLU MET PHE ALA LYS
SEQRES 3 B 306 GLU VAL LYS GLU LYS SER GLN GLY LYS ILE GLU ILE SER
SEQRES 4 B 306 LEU TYR PRO SER SER GLN LEU GLY ASP ASP ARG ALA MET
SEQRES 5 B 306 LEU LYS GLN LEU LYS ASP GLY SER LEU ASP PHE THR PHE
SEQRES 6 B 306 ALA GLU SER ALA ARG PHE GLN LEU PHE TYR PRO GLU ALA
SEQRES 7 B 306 ALA VAL PHE ALA LEU PRO TYR VAL ILE SER ASN TYR ASN
SEQRES 8 B 306 VAL ALA GLN LYS ALA LEU PHE ASP THR GLU PHE GLY LYS
SEQRES 9 B 306 ASP LEU ILE LYS LYS MET ASP LYS ASP LEU GLY VAL THR
SEQRES 10 B 306 LEU LEU SER GLN ALA TYR ASN GLY THR ARG GLN THR THR
SEQRES 11 B 306 SER ASN ARG ALA ILE ASN SER ILE ALA ASP MET LYS GLY
SEQRES 12 B 306 LEU LYS LEU ARG VAL PRO ASN ALA ALA THR ASN LEU ALA
SEQRES 13 B 306 TYR ALA LYS TYR VAL GLY ALA SER PRO THR PRO MET ALA
SEQRES 14 B 306 PHE SER GLU VAL TYR LEU ALA LEU GLN THR ASN ALA VAL
SEQRES 15 B 306 ASP GLY GLN GLU ASN PRO LEU ALA ALA VAL GLN ALA GLN
SEQRES 16 B 306 LYS PHE TYR GLU VAL GLN LYS PHE LEU ALA MET THR ASN
SEQRES 17 B 306 HIS ILE LEU ASN ASP GLN LEU TYR LEU VAL SER ASN GLU
SEQRES 18 B 306 THR TYR LYS GLU LEU PRO GLU ASP LEU GLN LYS VAL VAL
SEQRES 19 B 306 LYS ASP ALA ALA GLU ASN ALA ALA LYS TYR HIS THR LYS
SEQRES 20 B 306 LEU PHE VAL ASP GLY GLU LYS ASP LEU VAL THR PHE PHE
SEQRES 21 B 306 GLU LYS GLN GLY VAL LYS ILE THR HIS PRO ASP LEU VAL
SEQRES 22 B 306 PRO PHE LYS GLU SER MET LYS PRO TYR TYR ALA GLU PHE
SEQRES 23 B 306 VAL LYS GLN THR GLY GLN LYS GLY GLU SER ALA LEU LYS
SEQRES 24 B 306 GLN ILE GLU ALA ILE ASN PRO
SEQRES 1 C 306 ALA ASP TYR ASP LEU LYS PHE GLY MET ASN ALA GLY THR
SEQRES 2 C 306 SER SER ASN GLU TYR LYS ALA ALA GLU MET PHE ALA LYS
SEQRES 3 C 306 GLU VAL LYS GLU LYS SER GLN GLY LYS ILE GLU ILE SER
SEQRES 4 C 306 LEU TYR PRO SER SER GLN LEU GLY ASP ASP ARG ALA MET
SEQRES 5 C 306 LEU LYS GLN LEU LYS ASP GLY SER LEU ASP PHE THR PHE
SEQRES 6 C 306 ALA GLU SER ALA ARG PHE GLN LEU PHE TYR PRO GLU ALA
SEQRES 7 C 306 ALA VAL PHE ALA LEU PRO TYR VAL ILE SER ASN TYR ASN
SEQRES 8 C 306 VAL ALA GLN LYS ALA LEU PHE ASP THR GLU PHE GLY LYS
SEQRES 9 C 306 ASP LEU ILE LYS LYS MET ASP LYS ASP LEU GLY VAL THR
SEQRES 10 C 306 LEU LEU SER GLN ALA TYR ASN GLY THR ARG GLN THR THR
SEQRES 11 C 306 SER ASN ARG ALA ILE ASN SER ILE ALA ASP MET LYS GLY
SEQRES 12 C 306 LEU LYS LEU ARG VAL PRO ASN ALA ALA THR ASN LEU ALA
SEQRES 13 C 306 TYR ALA LYS TYR VAL GLY ALA SER PRO THR PRO MET ALA
SEQRES 14 C 306 PHE SER GLU VAL TYR LEU ALA LEU GLN THR ASN ALA VAL
SEQRES 15 C 306 ASP GLY GLN GLU ASN PRO LEU ALA ALA VAL GLN ALA GLN
SEQRES 16 C 306 LYS PHE TYR GLU VAL GLN LYS PHE LEU ALA MET THR ASN
SEQRES 17 C 306 HIS ILE LEU ASN ASP GLN LEU TYR LEU VAL SER ASN GLU
SEQRES 18 C 306 THR TYR LYS GLU LEU PRO GLU ASP LEU GLN LYS VAL VAL
SEQRES 19 C 306 LYS ASP ALA ALA GLU ASN ALA ALA LYS TYR HIS THR LYS
SEQRES 20 C 306 LEU PHE VAL ASP GLY GLU LYS ASP LEU VAL THR PHE PHE
SEQRES 21 C 306 GLU LYS GLN GLY VAL LYS ILE THR HIS PRO ASP LEU VAL
SEQRES 22 C 306 PRO PHE LYS GLU SER MET LYS PRO TYR TYR ALA GLU PHE
SEQRES 23 C 306 VAL LYS GLN THR GLY GLN LYS GLY GLU SER ALA LEU LYS
SEQRES 24 C 306 GLN ILE GLU ALA ILE ASN PRO
SEQRES 1 D 306 ALA ASP TYR ASP LEU LYS PHE GLY MET ASN ALA GLY THR
SEQRES 2 D 306 SER SER ASN GLU TYR LYS ALA ALA GLU MET PHE ALA LYS
SEQRES 3 D 306 GLU VAL LYS GLU LYS SER GLN GLY LYS ILE GLU ILE SER
SEQRES 4 D 306 LEU TYR PRO SER SER GLN LEU GLY ASP ASP ARG ALA MET
SEQRES 5 D 306 LEU LYS GLN LEU LYS ASP GLY SER LEU ASP PHE THR PHE
SEQRES 6 D 306 ALA GLU SER ALA ARG PHE GLN LEU PHE TYR PRO GLU ALA
SEQRES 7 D 306 ALA VAL PHE ALA LEU PRO TYR VAL ILE SER ASN TYR ASN
SEQRES 8 D 306 VAL ALA GLN LYS ALA LEU PHE ASP THR GLU PHE GLY LYS
SEQRES 9 D 306 ASP LEU ILE LYS LYS MET ASP LYS ASP LEU GLY VAL THR
SEQRES 10 D 306 LEU LEU SER GLN ALA TYR ASN GLY THR ARG GLN THR THR
SEQRES 11 D 306 SER ASN ARG ALA ILE ASN SER ILE ALA ASP MET LYS GLY
SEQRES 12 D 306 LEU LYS LEU ARG VAL PRO ASN ALA ALA THR ASN LEU ALA
SEQRES 13 D 306 TYR ALA LYS TYR VAL GLY ALA SER PRO THR PRO MET ALA
SEQRES 14 D 306 PHE SER GLU VAL TYR LEU ALA LEU GLN THR ASN ALA VAL
SEQRES 15 D 306 ASP GLY GLN GLU ASN PRO LEU ALA ALA VAL GLN ALA GLN
SEQRES 16 D 306 LYS PHE TYR GLU VAL GLN LYS PHE LEU ALA MET THR ASN
SEQRES 17 D 306 HIS ILE LEU ASN ASP GLN LEU TYR LEU VAL SER ASN GLU
SEQRES 18 D 306 THR TYR LYS GLU LEU PRO GLU ASP LEU GLN LYS VAL VAL
SEQRES 19 D 306 LYS ASP ALA ALA GLU ASN ALA ALA LYS TYR HIS THR LYS
SEQRES 20 D 306 LEU PHE VAL ASP GLY GLU LYS ASP LEU VAL THR PHE PHE
SEQRES 21 D 306 GLU LYS GLN GLY VAL LYS ILE THR HIS PRO ASP LEU VAL
SEQRES 22 D 306 PRO PHE LYS GLU SER MET LYS PRO TYR TYR ALA GLU PHE
SEQRES 23 D 306 VAL LYS GLN THR GLY GLN LYS GLY GLU SER ALA LEU LYS
SEQRES 24 D 306 GLN ILE GLU ALA ILE ASN PRO
HET ZN A1306 1
HET DAN B1307 20
HET GOL B1308 6
HET GOL B1309 6
HET ZN B1310 1
HET ZN B1311 1
HET ZN C1306 1
HET ZN C1307 1
HET GOL D1306 6
HET ZN D1307 1
HETNAM ZN ZINC ION
HETNAM DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 ZN 6(ZN 2+)
FORMUL 6 DAN C11 H17 N O8
FORMUL 7 GOL 3(C3 H8 O3)
FORMUL 15 HOH *455(H2 O)
HELIX 1 1 SER A 15 SER A 32 1 18
HELIX 2 2 ASP A 48 ASP A 58 1 11
HELIX 3 3 SER A 68 PHE A 74 5 7
HELIX 4 4 TYR A 75 LEU A 83 5 9
HELIX 5 5 ASN A 89 ASP A 99 1 11
HELIX 6 6 THR A 100 ASP A 113 1 14
HELIX 7 7 SER A 137 LYS A 142 5 6
HELIX 8 8 ALA A 151 VAL A 161 1 11
HELIX 9 9 ALA A 169 SER A 171 5 3
HELIX 10 10 GLU A 172 THR A 179 1 8
HELIX 11 11 LEU A 189 GLN A 195 1 7
HELIX 12 12 LYS A 196 VAL A 200 5 5
HELIX 13 13 ASN A 220 LYS A 224 1 5
HELIX 14 14 PRO A 227 GLN A 263 1 37
HELIX 15 15 LEU A 272 SER A 278 1 7
HELIX 16 16 MET A 279 ALA A 303 1 25
HELIX 17 17 SER B 15 SER B 32 1 18
HELIX 18 18 ASP B 48 ASP B 58 1 11
HELIX 19 19 GLU B 67 PHE B 74 5 8
HELIX 20 20 TYR B 75 LEU B 83 5 9
HELIX 21 21 ASN B 89 THR B 100 1 12
HELIX 22 22 THR B 100 ASP B 113 1 14
HELIX 23 23 SER B 137 LYS B 142 1 6
HELIX 24 24 ALA B 151 GLY B 162 1 12
HELIX 25 25 ALA B 169 SER B 171 5 3
HELIX 26 26 GLU B 172 THR B 179 1 8
HELIX 27 27 LEU B 189 GLN B 195 1 7
HELIX 28 28 ASN B 220 LYS B 224 1 5
HELIX 29 29 PRO B 227 GLN B 263 1 37
HELIX 30 30 ASP B 271 THR B 290 1 20
HELIX 31 31 GLY B 291 ILE B 304 1 14
HELIX 32 32 SER C 15 VAL C 28 1 14
HELIX 33 33 ASP C 48 ASP C 58 1 11
HELIX 34 34 GLU C 67 PHE C 74 5 8
HELIX 35 35 TYR C 75 LEU C 83 5 9
HELIX 36 36 ASN C 89 ASP C 99 1 11
HELIX 37 37 THR C 100 ASP C 113 1 14
HELIX 38 38 SER C 137 MET C 141 5 5
HELIX 39 39 ALA C 151 VAL C 161 1 11
HELIX 40 40 ALA C 169 SER C 171 5 3
HELIX 41 41 GLU C 172 THR C 179 1 8
HELIX 42 42 LEU C 189 GLN C 195 1 7
HELIX 43 43 LYS C 196 VAL C 200 5 5
HELIX 44 44 ASN C 220 LEU C 226 1 7
HELIX 45 45 PRO C 227 GLN C 263 1 37
HELIX 46 46 LEU C 272 SER C 278 1 7
HELIX 47 47 MET C 279 GLY C 291 1 13
HELIX 48 48 SER D 15 SER D 32 1 18
HELIX 49 49 ASP D 48 ASP D 58 1 11
HELIX 50 50 GLU D 67 LEU D 73 5 7
HELIX 51 51 TYR D 75 ALA D 82 5 8
HELIX 52 52 ASN D 89 ASP D 99 1 11
HELIX 53 53 THR D 100 ASP D 113 1 14
HELIX 54 54 ALA D 151 VAL D 161 1 11
HELIX 55 55 ALA D 169 SER D 171 5 3
HELIX 56 56 GLU D 172 THR D 179 1 8
HELIX 57 57 LEU D 189 GLN D 195 1 7
HELIX 58 58 ASN D 220 GLU D 225 1 6
HELIX 59 59 PRO D 227 GLN D 263 1 37
HELIX 60 60 LEU D 272 MET D 279 1 8
HELIX 61 61 MET D 279 THR D 290 1 12
HELIX 62 62 GLY D 291 ILE D 304 1 14
SHEET 1 AA 8 ILE A 36 TYR A 41 0
SHEET 2 AA 8 TYR A 3 GLY A 8 1 O TYR A 3 N GLU A 37
SHEET 3 AA 8 PHE A 63 ALA A 66 1 O PHE A 63 N GLY A 8
SHEET 4 AA 8 LEU A 211 SER A 219 -1 O LEU A 215 N ALA A 66
SHEET 5 AA 8 VAL A 116 SER A 131 -1 O THR A 117 N VAL A 218
SHEET 6 AA 8 GLY A 184 PRO A 188 -1 O GLN A 185 N THR A 130
SHEET 7 AA 8 LYS A 145 VAL A 148 1 O LYS A 145 N GLY A 184
SHEET 8 AA 8 SER A 164 PRO A 167 1 O SER A 164 N LEU A 146
SHEET 1 AB 7 ILE A 36 TYR A 41 0
SHEET 2 AB 7 TYR A 3 GLY A 8 1 O TYR A 3 N GLU A 37
SHEET 3 AB 7 PHE A 63 ALA A 66 1 O PHE A 63 N GLY A 8
SHEET 4 AB 7 LEU A 211 SER A 219 -1 O LEU A 215 N ALA A 66
SHEET 5 AB 7 VAL A 116 SER A 131 -1 O THR A 117 N VAL A 218
SHEET 6 AB 7 PHE A 203 ALA A 205 -1 O PHE A 203 N SER A 131
SHEET 7 AB 7 LYS A 266 THR A 268 1 O LYS A 266 N LEU A 204
SHEET 1 BA 6 ILE B 36 TYR B 41 0
SHEET 2 BA 6 TYR B 3 GLY B 8 1 O TYR B 3 N GLU B 37
SHEET 3 BA 6 PHE B 63 ALA B 66 1 O PHE B 63 N GLY B 8
SHEET 4 BA 6 PHE B 203 SER B 219 -1 O LEU B 215 N ALA B 66
SHEET 5 BA 6 VAL B 116 SER B 131 -1 O THR B 117 N VAL B 218
SHEET 6 BA 6 GLY B 184 PRO B 188 -1 O GLN B 185 N THR B 130
SHEET 1 BB 5 ILE B 36 TYR B 41 0
SHEET 2 BB 5 TYR B 3 GLY B 8 1 O TYR B 3 N GLU B 37
SHEET 3 BB 5 PHE B 63 ALA B 66 1 O PHE B 63 N GLY B 8
SHEET 4 BB 5 PHE B 203 SER B 219 -1 O LEU B 215 N ALA B 66
SHEET 5 BB 5 LYS B 266 THR B 268 1 O LYS B 266 N LEU B 204
SHEET 1 BC 2 LYS B 145 VAL B 148 0
SHEET 2 BC 2 SER B 164 PRO B 167 1 O SER B 164 N LEU B 146
SHEET 1 CA 8 ILE C 38 TYR C 41 0
SHEET 2 CA 8 LEU C 5 GLY C 8 1 O LEU C 5 N SER C 39
SHEET 3 CA 8 PHE C 63 ALA C 66 1 O PHE C 63 N GLY C 8
SHEET 4 CA 8 PHE C 203 SER C 219 -1 O LEU C 215 N ALA C 66
SHEET 5 CA 8 VAL C 116 SER C 131 -1 O THR C 117 N VAL C 218
SHEET 6 CA 8 GLY C 184 PRO C 188 -1 O GLN C 185 N THR C 130
SHEET 7 CA 8 LYS C 145 ARG C 147 1 O ARG C 147 N GLU C 186
SHEET 8 CA 8 SER C 164 THR C 166 1 O SER C 164 N LEU C 146
SHEET 1 CB 5 ILE C 38 TYR C 41 0
SHEET 2 CB 5 LEU C 5 GLY C 8 1 O LEU C 5 N SER C 39
SHEET 3 CB 5 PHE C 63 ALA C 66 1 O PHE C 63 N GLY C 8
SHEET 4 CB 5 PHE C 203 SER C 219 -1 O LEU C 215 N ALA C 66
SHEET 5 CB 5 LYS C 266 THR C 268 1 O LYS C 266 N LEU C 204
SHEET 1 DA11 ILE D 36 TYR D 41 0
SHEET 2 DA11 TYR D 3 GLY D 8 1 O TYR D 3 N GLU D 37
SHEET 3 DA11 PHE D 63 ALA D 66 1 O PHE D 63 N GLY D 8
SHEET 4 DA11 PHE D 203 SER D 219 -1 O LEU D 215 N ALA D 66
SHEET 5 DA11 SER D 164 THR D 166 0
SHEET 6 DA11 LYS D 145 ARG D 147 1 O LEU D 146 N THR D 166
SHEET 7 DA11 GLY D 184 PRO D 188 1 O GLY D 184 N ARG D 147
SHEET 8 DA11 VAL D 116 SER D 131 -1 O GLN D 128 N ASN D 187
SHEET 9 DA11 PHE D 203 SER D 219 -1 O PHE D 203 N SER D 131
SHEET 10 DA11 LYS D 266 THR D 268 1 O LYS D 266 N LEU D 204
SHEET 11 DA11 PHE D 203 SER D 219 1 O LEU D 204 N THR D 268
LINK OD1 ASP A 2 ZN ZN A1306 1555 1555 2.44
LINK OD2 ASP A 2 ZN ZN A1306 1555 1555 1.98
LINK OD1 ASP A 4 ZN ZN A1306 1555 1555 2.48
LINK OD2 ASP A 4 ZN ZN A1306 1555 1555 2.15
LINK NE2 HIS A 269 ZN ZN B1310 3545 1555 2.26
LINK ZN ZN A1306 O HOH A2088 1555 1555 2.45
LINK OD1 ASP B 2 ZN ZN B1311 1555 1555 2.33
LINK OD2 ASP B 2 ZN ZN B1311 1555 1555 2.24
LINK OD2 ASP B 4 ZN ZN B1311 1555 1555 1.90
LINK NE2 HIS B 269 ZN ZN B1310 1555 1555 2.19
LINK ZN ZN B1310 O HOH B2145 1555 1555 2.15
LINK ZN ZN B1310 O HOH B2146 1555 1555 2.22
LINK ZN ZN B1311 O HOH B2147 1555 1555 2.09
LINK OD1 ASP C 2 ZN ZN C1307 1555 1555 2.58
LINK OD2 ASP C 2 ZN ZN C1307 1555 1555 2.17
LINK NE2 HIS C 269 ZN ZN C1306 1555 1555 2.22
LINK ZN ZN C1306 O HOH C2096 1555 1555 2.24
LINK ZN ZN C1306 O HOH C2097 1555 1555 2.28
LINK ZN ZN C1306 NE2 HIS D 269 1555 1555 2.03
LINK OD2 ASP D 2 ZN ZN D1307 1555 1555 2.28
LINK OD1 ASP D 2 ZN ZN D1307 1555 1555 2.44
LINK OD1 ASP D 4 ZN ZN D1307 1555 1555 2.59
LINK OD2 ASP D 4 ZN ZN D1307 1555 1555 1.72
LINK ZN ZN D1307 O HOH D2122 1555 1555 2.48
CRYST1 131.448 88.701 115.912 90.00 105.33 90.00 C 1 2 1 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007608 0.000000 0.002085 0.00000
SCALE2 0.000000 0.011274 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008946 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
