HEADER HYDROLASE 13-MAR-12 4E4P
TITLE SECOND NATIVE STRUCTURE OF XYLANASE A1 FROM PAENIBACILLUS SP. JDR-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE A;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 1,4-BETA-D-XYLAN XYLANOHYDROLASE A;
COMPND 5 EC: 3.2.1.8;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PAENIBACILLUS SP.;
SOURCE 3 ORGANISM_TAXID: 324057;
SOURCE 4 STRAIN: JDR-2;
SOURCE 5 GENE: PJDR2_0221, XYNA, XYNA1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETXYNA1CD
KEYWDS XYLANASE, PAENIBACILLUS, TIM BARREL, BETA/ALPHA 8 FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.POZHARSKI,F.J.ST JOHN
REVDAT 5 28-FEB-24 4E4P 1 REMARK SEQADV LINK
REVDAT 4 15-NOV-17 4E4P 1 REMARK
REVDAT 3 14-NOV-12 4E4P 1 JRNL
REVDAT 2 10-OCT-12 4E4P 1 JRNL
REVDAT 1 18-APR-12 4E4P 0
JRNL AUTH F.J.ST JOHN,J.F.PRESTON,E.POZHARSKI
JRNL TITL NOVEL STRUCTURAL FEATURES OF XYLANASE A1 FROM PAENIBACILLUS
JRNL TITL 2 SP. JDR-2.
JRNL REF J.STRUCT.BIOL. V. 180 303 2012
JRNL REFN ISSN 1047-8477
JRNL PMID 23000703
JRNL DOI 10.1016/J.JSB.2012.09.007
REMARK 2
REMARK 2 RESOLUTION. 1.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 1.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 48381
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) : 0.256
REMARK 3 R VALUE (WORKING SET) : 0.253
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2440
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.92
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3062
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.4800
REMARK 3 BIN FREE R VALUE SET COUNT : 153
REMARK 3 BIN FREE R VALUE : 0.5430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4644
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 225
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.81000
REMARK 3 B22 (A**2) : -1.81000
REMARK 3 B33 (A**2) : 1.81000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.24000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.214
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.188
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.157
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.726
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4748 ; 0.024 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6452 ; 1.903 ; 1.931
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 582 ; 6.351 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 242 ;40.328 ;25.702
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 788 ;16.408 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;13.058 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 706 ; 0.141 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3658 ; 0.010 ; 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): 2914 ; 1.130 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4678 ; 1.911 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1834 ; 3.525 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1774 ; 5.378 ; 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 : 12
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 5 A 46
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7800 -36.4890 24.2060
REMARK 3 T TENSOR
REMARK 3 T11: 0.4848 T22: 0.5423
REMARK 3 T33: 0.2897 T12: 0.2187
REMARK 3 T13: 0.0264 T23: 0.1572
REMARK 3 L TENSOR
REMARK 3 L11: 9.8585 L22: 5.3483
REMARK 3 L33: 4.5922 L12: 3.1219
REMARK 3 L13: 1.3472 L23: -1.7332
REMARK 3 S TENSOR
REMARK 3 S11: 0.1860 S12: -0.0127 S13: -1.2806
REMARK 3 S21: -0.2308 S22: -0.4552 S23: -1.0896
REMARK 3 S31: 0.9256 S32: 1.2959 S33: 0.2692
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 47 A 146
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2390 -26.9240 17.7320
REMARK 3 T TENSOR
REMARK 3 T11: 0.2564 T22: 0.1699
REMARK 3 T33: 0.0294 T12: -0.0151
REMARK 3 T13: -0.0041 T23: -0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 1.0660 L22: 1.9043
REMARK 3 L33: 3.5953 L12: 0.3690
REMARK 3 L13: 0.3490 L23: -1.1281
REMARK 3 S TENSOR
REMARK 3 S11: 0.0781 S12: 0.0468 S13: -0.1592
REMARK 3 S21: -0.0975 S22: -0.0986 S23: -0.0084
REMARK 3 S31: 0.3187 S32: 0.0452 S33: 0.0204
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 147 A 176
REMARK 3 ORIGIN FOR THE GROUP (A): 3.3150 -12.5510 15.1510
REMARK 3 T TENSOR
REMARK 3 T11: 0.2210 T22: 0.1588
REMARK 3 T33: 0.0679 T12: 0.0075
REMARK 3 T13: 0.0016 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 2.3018 L22: 2.9833
REMARK 3 L33: 4.8537 L12: 1.2122
REMARK 3 L13: -1.1548 L23: -2.4649
REMARK 3 S TENSOR
REMARK 3 S11: 0.1420 S12: 0.1832 S13: 0.2289
REMARK 3 S21: 0.1160 S22: 0.0047 S23: 0.0414
REMARK 3 S31: -0.6125 S32: -0.0931 S33: -0.1467
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 177 A 213
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0190 -15.4540 22.5730
REMARK 3 T TENSOR
REMARK 3 T11: 0.2016 T22: 0.1824
REMARK 3 T33: 0.0159 T12: -0.0517
REMARK 3 T13: -0.0760 T23: 0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 3.0952 L22: 4.8394
REMARK 3 L33: 8.1663 L12: 2.0240
REMARK 3 L13: -3.2639 L23: -4.1908
REMARK 3 S TENSOR
REMARK 3 S11: 0.0431 S12: -0.0709 S13: -0.0233
REMARK 3 S21: 0.2478 S22: -0.2362 S23: 0.0023
REMARK 3 S31: -0.1226 S32: 0.3697 S33: 0.1932
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 214 A 268
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9730 -15.1540 20.0120
REMARK 3 T TENSOR
REMARK 3 T11: 0.2594 T22: 0.3641
REMARK 3 T33: 0.0624 T12: -0.0699
REMARK 3 T13: -0.0636 T23: 0.1037
REMARK 3 L TENSOR
REMARK 3 L11: 4.9572 L22: 3.8900
REMARK 3 L33: 4.5255 L12: -2.3476
REMARK 3 L13: -2.5552 L23: 1.5593
REMARK 3 S TENSOR
REMARK 3 S11: 0.0470 S12: 0.0117 S13: 0.1745
REMARK 3 S21: 0.0565 S22: -0.2648 S23: -0.2291
REMARK 3 S31: -0.2725 S32: 0.5998 S33: 0.2178
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 277 A 305
REMARK 3 ORIGIN FOR THE GROUP (A): 30.5340 -23.2360 18.8960
REMARK 3 T TENSOR
REMARK 3 T11: 0.1815 T22: 0.6921
REMARK 3 T33: 0.1840 T12: 0.0616
REMARK 3 T13: -0.0145 T23: 0.2217
REMARK 3 L TENSOR
REMARK 3 L11: 4.8061 L22: 3.5300
REMARK 3 L33: 13.0138 L12: -0.2561
REMARK 3 L13: -1.4128 L23: 0.8318
REMARK 3 S TENSOR
REMARK 3 S11: -0.1967 S12: 0.0835 S13: 0.0098
REMARK 3 S21: -0.1822 S22: -0.1402 S23: -0.4686
REMARK 3 S31: 0.0410 S32: 1.8567 S33: 0.3369
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 5 B 42
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3410 -7.3210 55.5880
REMARK 3 T TENSOR
REMARK 3 T11: 0.4881 T22: 0.5955
REMARK 3 T33: 0.2708 T12: 0.2368
REMARK 3 T13: 0.0884 T23: 0.1926
REMARK 3 L TENSOR
REMARK 3 L11: 9.6547 L22: 10.6198
REMARK 3 L33: 4.8537 L12: 3.2669
REMARK 3 L13: 1.8916 L23: -1.6555
REMARK 3 S TENSOR
REMARK 3 S11: 0.0813 S12: -0.0655 S13: -1.3953
REMARK 3 S21: -0.0347 S22: -0.4746 S23: -1.2462
REMARK 3 S31: 1.0811 S32: 1.3959 S33: 0.3933
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 43 B 143
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3810 1.6050 48.7120
REMARK 3 T TENSOR
REMARK 3 T11: 0.2604 T22: 0.1516
REMARK 3 T33: 0.0237 T12: -0.0260
REMARK 3 T13: -0.0014 T23: -0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 2.0418 L22: 1.8939
REMARK 3 L33: 4.0021 L12: -0.1248
REMARK 3 L13: 0.7165 L23: -1.1828
REMARK 3 S TENSOR
REMARK 3 S11: 0.1196 S12: 0.0258 S13: -0.0901
REMARK 3 S21: -0.1270 S22: -0.1138 S23: -0.0380
REMARK 3 S31: 0.3753 S32: 0.0341 S33: -0.0058
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 144 B 175
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3680 17.6010 44.2790
REMARK 3 T TENSOR
REMARK 3 T11: 0.2520 T22: 0.1579
REMARK 3 T33: 0.0680 T12: 0.0122
REMARK 3 T13: -0.0118 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 3.5135 L22: 2.4445
REMARK 3 L33: 5.2629 L12: 2.8193
REMARK 3 L13: -1.8797 L23: -3.9912
REMARK 3 S TENSOR
REMARK 3 S11: 0.1194 S12: 0.2602 S13: 0.2987
REMARK 3 S21: 0.2764 S22: 0.0032 S23: 0.2925
REMARK 3 S31: -0.6155 S32: -0.0184 S33: -0.1226
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 176 B 211
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4650 13.3540 53.5420
REMARK 3 T TENSOR
REMARK 3 T11: 0.1882 T22: 0.1832
REMARK 3 T33: 0.0181 T12: -0.0528
REMARK 3 T13: -0.0713 T23: 0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 3.3283 L22: 5.4892
REMARK 3 L33: 8.3968 L12: 2.0813
REMARK 3 L13: -3.6120 L23: -4.5234
REMARK 3 S TENSOR
REMARK 3 S11: 0.0664 S12: -0.0874 S13: 0.0242
REMARK 3 S21: 0.2527 S22: -0.2129 S23: -0.0197
REMARK 3 S31: -0.1119 S32: 0.3940 S33: 0.1465
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 212 B 231
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1620 19.4550 59.3080
REMARK 3 T TENSOR
REMARK 3 T11: 0.3445 T22: 0.2246
REMARK 3 T33: 0.0527 T12: -0.1145
REMARK 3 T13: 0.0040 T23: -0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 7.2636 L22: 15.7569
REMARK 3 L33: 10.3103 L12: -9.9202
REMARK 3 L13: -5.1230 L23: 8.4387
REMARK 3 S TENSOR
REMARK 3 S11: -0.1248 S12: -0.3724 S13: 0.5017
REMARK 3 S21: 0.7830 S22: -0.0298 S23: -0.3222
REMARK 3 S31: -0.2416 S32: 0.0011 S33: 0.1546
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 232 B 305
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1190 8.9900 47.9280
REMARK 3 T TENSOR
REMARK 3 T11: 0.1766 T22: 0.5812
REMARK 3 T33: 0.0913 T12: -0.0192
REMARK 3 T13: -0.0572 T23: 0.1641
REMARK 3 L TENSOR
REMARK 3 L11: 4.2913 L22: 5.3916
REMARK 3 L33: 6.8634 L12: -1.1327
REMARK 3 L13: -1.7984 L23: 0.4320
REMARK 3 S TENSOR
REMARK 3 S11: -0.0333 S12: 0.0657 S13: 0.1010
REMARK 3 S21: -0.1329 S22: -0.1985 S23: -0.3670
REMARK 3 S31: -0.0398 S32: 1.1988 S33: 0.2318
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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
REMARK 4
REMARK 4 4E4P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071165.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 105
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : LIQUID NITROGEN-COOLED DOUBLE
REMARK 200 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48561
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.920
REMARK 200 RESOLUTION RANGE LOW (A) : 84.820
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.92
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.80500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM MGCL2, 100MM HEPES SODIUM SALT,
REMARK 280 25% PEG3350, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 294.5K
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 89.75900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.26400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 89.75900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.26400
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: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
REMARK 465 MET A 4
REMARK 465 ASN A 269
REMARK 465 ASN A 270
REMARK 465 TYR A 271
REMARK 465 THR A 272
REMARK 465 LEU A 273
REMARK 465 PRO A 274
REMARK 465 GLU A 275
REMARK 465 ASN A 276
REMARK 465 GLY A 306
REMARK 465 MET A 307
REMARK 465 ASP A 308
REMARK 465 ASP A 309
REMARK 465 ASN A 310
REMARK 465 THR A 311
REMARK 465 SER A 312
REMARK 465 TRP A 313
REMARK 465 ARG A 314
REMARK 465 ALA A 315
REMARK 465 GLU A 316
REMARK 465 ASN A 317
REMARK 465 ASN A 318
REMARK 465 PRO A 319
REMARK 465 LEU A 320
REMARK 465 LEU A 321
REMARK 465 PHE A 322
REMARK 465 ASP A 323
REMARK 465 LYS A 324
REMARK 465 ASN A 325
REMARK 465 LEU A 326
REMARK 465 GLN A 327
REMARK 465 ALA A 328
REMARK 465 LYS A 329
REMARK 465 PRO A 330
REMARK 465 ALA A 331
REMARK 465 TYR A 332
REMARK 465 TYR A 333
REMARK 465 GLY A 334
REMARK 465 VAL A 335
REMARK 465 ILE A 336
REMARK 465 ASP A 337
REMARK 465 PRO A 338
REMARK 465 ALA A 339
REMARK 465 GLU A 340
REMARK 465 GLN A 341
REMARK 465 GLY B 1
REMARK 465 SER B 2
REMARK 465 HIS B 3
REMARK 465 MET B 4
REMARK 465 ASN B 269
REMARK 465 ASN B 270
REMARK 465 TYR B 271
REMARK 465 THR B 272
REMARK 465 LEU B 273
REMARK 465 PRO B 274
REMARK 465 GLU B 275
REMARK 465 ASN B 276
REMARK 465 GLY B 306
REMARK 465 MET B 307
REMARK 465 ASP B 308
REMARK 465 ASP B 309
REMARK 465 ASN B 310
REMARK 465 THR B 311
REMARK 465 SER B 312
REMARK 465 TRP B 313
REMARK 465 ARG B 314
REMARK 465 ALA B 315
REMARK 465 GLU B 316
REMARK 465 ASN B 317
REMARK 465 ASN B 318
REMARK 465 PRO B 319
REMARK 465 LEU B 320
REMARK 465 LEU B 321
REMARK 465 PHE B 322
REMARK 465 ASP B 323
REMARK 465 LYS B 324
REMARK 465 ASN B 325
REMARK 465 LEU B 326
REMARK 465 GLN B 327
REMARK 465 ALA B 328
REMARK 465 LYS B 329
REMARK 465 PRO B 330
REMARK 465 ALA B 331
REMARK 465 TYR B 332
REMARK 465 TYR B 333
REMARK 465 GLY B 334
REMARK 465 VAL B 335
REMARK 465 ILE B 336
REMARK 465 ASP B 337
REMARK 465 PRO B 338
REMARK 465 ALA B 339
REMARK 465 GLU B 340
REMARK 465 GLN B 341
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OH TYR A 11 OH TYR B 283 4546 1.98
REMARK 500 OH TYR A 283 OH TYR B 11 4546 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP B 92 CB TRP B 92 CG 0.148
REMARK 500 PHE B 172 CE2 PHE B 172 CD2 0.124
REMARK 500 TYR B 191 CD1 TYR B 191 CE1 0.091
REMARK 500 TYR B 191 CE2 TYR B 191 CD2 0.095
REMARK 500 TYR B 292 CD1 TYR B 292 CE1 0.091
REMARK 500
REMARK 500 REMARK: NULL
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 ARG B 155 NE - CZ - NH1 ANGL. DEV. = -3.8 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 GLU A 262 44.20 -144.35
REMARK 500 ASN B 143 65.45 34.27
REMARK 500 GLU B 262 43.05 -146.80
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 MG A 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 14 O
REMARK 620 2 ALA A 296 O 93.3
REMARK 620 3 ILE A 299 O 103.6 99.9
REMARK 620 4 HOH A 588 O 152.4 88.6 103.2
REMARK 620 5 HOH A 604 O 73.8 79.6 177.3 79.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 60 O
REMARK 620 2 HOH A 612 O 122.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 14 O
REMARK 620 2 ALA B 296 O 95.2
REMARK 620 3 ILE B 299 O 94.2 84.0
REMARK 620 4 HOH B 579 O 169.0 89.2 76.2
REMARK 620 5 HOH B 593 O 78.7 94.6 172.6 111.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 60 O
REMARK 620 2 HOH B 609 O 119.9
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RO8 RELATED DB: PDB
REMARK 900 ORIGINAL NATIVE XYNA1CD STRUCTURE
REMARK 900 RELATED ID: 3RDK RELATED DB: PDB
REMARK 900 LIGAND BOUND XYNA1CD STRUCTURE
DBREF 4E4P A 5 338 UNP C6CRV0 XYNA1_PAESJ 518 851
DBREF 4E4P B 5 338 UNP C6CRV0 XYNA1_PAESJ 518 851
SEQADV 4E4P GLY A 1 UNP C6CRV0 EXPRESSION TAG
SEQADV 4E4P SER A 2 UNP C6CRV0 EXPRESSION TAG
SEQADV 4E4P HIS A 3 UNP C6CRV0 EXPRESSION TAG
SEQADV 4E4P MET A 4 UNP C6CRV0 EXPRESSION TAG
SEQADV 4E4P ALA A 339 UNP C6CRV0 EXPRESSION TAG
SEQADV 4E4P GLU A 340 UNP C6CRV0 EXPRESSION TAG
SEQADV 4E4P GLN A 341 UNP C6CRV0 EXPRESSION TAG
SEQADV 4E4P GLY B 1 UNP C6CRV0 EXPRESSION TAG
SEQADV 4E4P SER B 2 UNP C6CRV0 EXPRESSION TAG
SEQADV 4E4P HIS B 3 UNP C6CRV0 EXPRESSION TAG
SEQADV 4E4P MET B 4 UNP C6CRV0 EXPRESSION TAG
SEQADV 4E4P ALA B 339 UNP C6CRV0 EXPRESSION TAG
SEQADV 4E4P GLU B 340 UNP C6CRV0 EXPRESSION TAG
SEQADV 4E4P GLN B 341 UNP C6CRV0 EXPRESSION TAG
SEQRES 1 A 341 GLY SER HIS MET ALA PRO LEU LYS ASP VAL TYR LYS ASN
SEQRES 2 A 341 ASP PHE LEU ILE GLY ASN ALA ILE SER ALA GLU ASP LEU
SEQRES 3 A 341 GLU GLY THR ARG LEU GLU LEU LEU LYS MET HIS HIS ASP
SEQRES 4 A 341 VAL VAL THR ALA GLY ASN ALA MET LYS PRO ASP ALA LEU
SEQRES 5 A 341 GLN PRO THR LYS GLY ASN PHE THR PHE THR ALA ALA ASP
SEQRES 6 A 341 ALA MET ILE ASP LYS VAL LEU ALA GLU GLY MET LYS MET
SEQRES 7 A 341 HIS GLY HIS VAL LEU VAL TRP HIS GLN GLN SER PRO ALA
SEQRES 8 A 341 TRP LEU ASN THR LYS LYS ASP ASP ASN ASN ASN THR VAL
SEQRES 9 A 341 PRO LEU GLY ARG ASP GLU ALA LEU ASP ASN LEU ARG THR
SEQRES 10 A 341 HIS ILE GLN THR VAL MET LYS HIS PHE GLY ASN LYS VAL
SEQRES 11 A 341 ILE SER TRP ASP VAL VAL ASN GLU ALA MET ASN ASP ASN
SEQRES 12 A 341 PRO SER ASN PRO ALA ASP TYR LYS ALA SER LEU ARG GLN
SEQRES 13 A 341 THR PRO TRP TYR GLN ALA ILE GLY SER ASP TYR VAL GLU
SEQRES 14 A 341 GLN ALA PHE LEU ALA ALA ARG GLU VAL LEU ASP GLU ASN
SEQRES 15 A 341 PRO SER TRP ASN ILE LYS LEU TYR TYR ASN ASP TYR ASN
SEQRES 16 A 341 GLU ASP ASN GLN ASN LYS ALA THR ALA ILE TYR ASN MET
SEQRES 17 A 341 VAL LYS ASP ILE ASN ASP ARG TYR ALA ALA ALA HIS ASN
SEQRES 18 A 341 GLY LYS LEU LEU ILE ASP GLY VAL GLY MET GLN GLY HIS
SEQRES 19 A 341 TYR ASN ILE ASN THR ASN PRO ASP ASN VAL LYS LEU SER
SEQRES 20 A 341 LEU GLU LYS PHE ILE SER LEU GLY VAL GLU VAL SER VAL
SEQRES 21 A 341 SER GLU LEU ASP VAL THR ALA GLY ASN ASN TYR THR LEU
SEQRES 22 A 341 PRO GLU ASN LEU ALA VAL GLY GLN ALA TYR LEU TYR ALA
SEQRES 23 A 341 GLN LEU PHE LYS LEU TYR LYS GLU HIS ALA ASP HIS ILE
SEQRES 24 A 341 ALA ARG VAL THR PHE TRP GLY MET ASP ASP ASN THR SER
SEQRES 25 A 341 TRP ARG ALA GLU ASN ASN PRO LEU LEU PHE ASP LYS ASN
SEQRES 26 A 341 LEU GLN ALA LYS PRO ALA TYR TYR GLY VAL ILE ASP PRO
SEQRES 27 A 341 ALA GLU GLN
SEQRES 1 B 341 GLY SER HIS MET ALA PRO LEU LYS ASP VAL TYR LYS ASN
SEQRES 2 B 341 ASP PHE LEU ILE GLY ASN ALA ILE SER ALA GLU ASP LEU
SEQRES 3 B 341 GLU GLY THR ARG LEU GLU LEU LEU LYS MET HIS HIS ASP
SEQRES 4 B 341 VAL VAL THR ALA GLY ASN ALA MET LYS PRO ASP ALA LEU
SEQRES 5 B 341 GLN PRO THR LYS GLY ASN PHE THR PHE THR ALA ALA ASP
SEQRES 6 B 341 ALA MET ILE ASP LYS VAL LEU ALA GLU GLY MET LYS MET
SEQRES 7 B 341 HIS GLY HIS VAL LEU VAL TRP HIS GLN GLN SER PRO ALA
SEQRES 8 B 341 TRP LEU ASN THR LYS LYS ASP ASP ASN ASN ASN THR VAL
SEQRES 9 B 341 PRO LEU GLY ARG ASP GLU ALA LEU ASP ASN LEU ARG THR
SEQRES 10 B 341 HIS ILE GLN THR VAL MET LYS HIS PHE GLY ASN LYS VAL
SEQRES 11 B 341 ILE SER TRP ASP VAL VAL ASN GLU ALA MET ASN ASP ASN
SEQRES 12 B 341 PRO SER ASN PRO ALA ASP TYR LYS ALA SER LEU ARG GLN
SEQRES 13 B 341 THR PRO TRP TYR GLN ALA ILE GLY SER ASP TYR VAL GLU
SEQRES 14 B 341 GLN ALA PHE LEU ALA ALA ARG GLU VAL LEU ASP GLU ASN
SEQRES 15 B 341 PRO SER TRP ASN ILE LYS LEU TYR TYR ASN ASP TYR ASN
SEQRES 16 B 341 GLU ASP ASN GLN ASN LYS ALA THR ALA ILE TYR ASN MET
SEQRES 17 B 341 VAL LYS ASP ILE ASN ASP ARG TYR ALA ALA ALA HIS ASN
SEQRES 18 B 341 GLY LYS LEU LEU ILE ASP GLY VAL GLY MET GLN GLY HIS
SEQRES 19 B 341 TYR ASN ILE ASN THR ASN PRO ASP ASN VAL LYS LEU SER
SEQRES 20 B 341 LEU GLU LYS PHE ILE SER LEU GLY VAL GLU VAL SER VAL
SEQRES 21 B 341 SER GLU LEU ASP VAL THR ALA GLY ASN ASN TYR THR LEU
SEQRES 22 B 341 PRO GLU ASN LEU ALA VAL GLY GLN ALA TYR LEU TYR ALA
SEQRES 23 B 341 GLN LEU PHE LYS LEU TYR LYS GLU HIS ALA ASP HIS ILE
SEQRES 24 B 341 ALA ARG VAL THR PHE TRP GLY MET ASP ASP ASN THR SER
SEQRES 25 B 341 TRP ARG ALA GLU ASN ASN PRO LEU LEU PHE ASP LYS ASN
SEQRES 26 B 341 LEU GLN ALA LYS PRO ALA TYR TYR GLY VAL ILE ASP PRO
SEQRES 27 B 341 ALA GLU GLN
HET MG A 401 1
HET CL A 402 2
HET MG A 403 1
HET MG B 401 1
HET CL B 402 2
HET MG B 403 1
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
FORMUL 3 MG 4(MG 2+)
FORMUL 4 CL 2(CL 1-)
FORMUL 9 HOH *225(H2 O)
HELIX 1 1 PRO A 6 TYR A 11 1 6
HELIX 2 2 GLU A 27 HIS A 38 1 12
HELIX 3 3 LYS A 48 GLN A 53 1 6
HELIX 4 4 PHE A 61 GLU A 74 1 14
HELIX 5 5 PRO A 90 LEU A 93 5 4
HELIX 6 6 GLY A 107 GLY A 127 1 21
HELIX 7 7 ASN A 128 VAL A 130 5 3
HELIX 8 8 TYR A 150 LEU A 154 5 5
HELIX 9 9 THR A 157 GLY A 164 1 8
HELIX 10 10 ASP A 166 ASN A 182 1 17
HELIX 11 11 ASN A 198 HIS A 220 1 23
HELIX 12 12 ASN A 240 SER A 253 1 14
HELIX 13 13 ALA A 278 HIS A 295 1 18
HELIX 14 14 PRO B 6 TYR B 11 1 6
HELIX 15 15 GLU B 27 HIS B 38 1 12
HELIX 16 16 LYS B 48 GLN B 53 1 6
HELIX 17 17 PHE B 61 GLU B 74 1 14
HELIX 18 18 PRO B 90 LEU B 93 5 4
HELIX 19 19 GLY B 107 GLY B 127 1 21
HELIX 20 20 ASN B 128 VAL B 130 5 3
HELIX 21 21 ASP B 149 LEU B 154 1 6
HELIX 22 22 THR B 157 GLY B 164 1 8
HELIX 23 23 ASP B 166 ASN B 182 1 17
HELIX 24 24 ASN B 198 HIS B 220 1 23
HELIX 25 25 ASN B 240 SER B 253 1 14
HELIX 26 26 ALA B 278 HIS B 295 1 18
SHEET 1 A10 HIS A 234 ASN A 236 0
SHEET 2 A10 GLU A 257 THR A 266 1 O THR A 266 N TYR A 235
SHEET 3 A10 ILE A 299 PHE A 304 1 O THR A 303 N VAL A 260
SHEET 4 A10 LEU A 16 ILE A 21 1 N LEU A 16 O ALA A 300
SHEET 5 A10 VAL A 40 ALA A 43 1 O THR A 42 N ILE A 21
SHEET 6 A10 LYS A 77 VAL A 84 1 O HIS A 79 N VAL A 41
SHEET 7 A10 SER A 132 ASN A 137 1 O SER A 132 N GLY A 80
SHEET 8 A10 LYS A 188 ASP A 193 1 O TYR A 190 N TRP A 133
SHEET 9 A10 GLY A 228 MET A 231 1 O GLY A 230 N TYR A 191
SHEET 10 A10 GLU A 257 THR A 266 1 O SER A 259 N MET A 231
SHEET 1 B 2 THR A 95 LYS A 97 0
SHEET 2 B 2 THR A 103 PRO A 105 -1 O VAL A 104 N LYS A 96
SHEET 1 C10 HIS B 234 ASN B 236 0
SHEET 2 C10 GLU B 257 THR B 266 1 O THR B 266 N TYR B 235
SHEET 3 C10 ILE B 299 PHE B 304 1 O THR B 303 N VAL B 260
SHEET 4 C10 LEU B 16 ILE B 21 1 N LEU B 16 O ALA B 300
SHEET 5 C10 VAL B 40 ALA B 43 1 O THR B 42 N ILE B 21
SHEET 6 C10 LYS B 77 VAL B 84 1 O HIS B 79 N VAL B 41
SHEET 7 C10 SER B 132 ASN B 137 1 O SER B 132 N GLY B 80
SHEET 8 C10 LYS B 188 ASP B 193 1 O TYR B 190 N TRP B 133
SHEET 9 C10 GLY B 228 MET B 231 1 O GLY B 230 N TYR B 191
SHEET 10 C10 GLU B 257 THR B 266 1 O SER B 259 N MET B 231
SHEET 1 D 2 THR B 95 LYS B 97 0
SHEET 2 D 2 THR B 103 PRO B 105 -1 O VAL B 104 N LYS B 96
LINK O ASP A 14 MG MG A 401 1555 1555 2.36
LINK O THR A 60 MG MG A 403 1555 1555 2.67
LINK O ALA A 296 MG MG A 401 1555 1555 2.26
LINK O ILE A 299 MG MG A 401 1555 1555 2.28
LINK MG MG A 401 O AHOH A 588 1555 1555 2.29
LINK MG MG A 401 O HOH A 604 1555 1555 2.23
LINK MG MG A 403 O HOH A 612 1555 1555 2.69
LINK O ASP B 14 MG MG B 401 1555 1555 2.28
LINK O THR B 60 MG MG B 403 1555 1555 2.74
LINK O ALA B 296 MG MG B 401 1555 1555 2.34
LINK O ILE B 299 MG MG B 401 1555 1555 2.36
LINK MG MG B 401 O HOH B 579 1555 1555 2.55
LINK MG MG B 401 O HOH B 593 1555 1555 2.53
LINK MG MG B 403 O HOH B 609 1555 1555 2.64
CISPEP 1 HIS A 81 VAL A 82 0 11.41
CISPEP 2 HIS B 81 VAL B 82 0 11.67
SITE 1 AC1 5 ASP A 14 ALA A 296 ILE A 299 HOH A 588
SITE 2 AC1 5 HOH A 604
SITE 1 AC2 7 THR A 60 PHE A 61 THR A 62 ALA A 63
SITE 2 AC2 7 MG A 403 ARG B 108 HOH B 538
SITE 1 AC3 7 THR A 60 PHE A 61 THR A 62 ALA A 63
SITE 2 AC3 7 ALA A 64 CL A 402 HOH A 612
SITE 1 AC4 5 ASP B 14 ALA B 296 ILE B 299 HOH B 579
SITE 2 AC4 5 HOH B 593
SITE 1 AC5 6 ARG A 108 HOH A 544 THR B 60 THR B 62
SITE 2 AC5 6 ALA B 63 MG B 403
SITE 1 AC6 7 THR B 60 PHE B 61 THR B 62 ALA B 63
SITE 2 AC6 7 ALA B 64 CL B 402 HOH B 609
CRYST1 179.518 58.528 65.024 90.00 108.81 90.00 C 1 2 1 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 0.005570 0.000000 0.001898 0.00000
SCALE2 0.000000 0.017086 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016247 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
