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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 22-MAY-07 2Q0X
TITLE ALPHA/BETA HYDROLASE FOLD PROTEIN OF UNKNOWN FUNCTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PROTEIN DUF1749;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI;
SOURCE 3 ORGANISM_COMMON: AFRICAN SLEEPING SICKNESS PARASITE;
SOURCE 4 STRAIN: TREU927, 927/4 GUTAT10.1;
SOURCE 5 GENE: TB10.6K15.0140;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS ALPHA/BETA HYDROLASE FOLD, STRUCTURAL GENOMICS, STRUCTURAL
KEYWDS 2 GENOMICS OF PATHOGENIC PROTOZOA CONSORTIUM, SGPP, PSI,
KEYWDS 3 PROTEIN STRUCTURE INITIATIVE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.A.MERRITT,STRUCTURAL GENOMICS OF PATHOGENIC PROTOZOA
AUTHOR 2 CONSORTIUM (SGPP)
REVDAT 1 26-JUN-07 2Q0X 0
JRNL AUTH E.A.MERRITT,M.A.HOLMES,F.S.BUCKNER,
JRNL AUTH 2 W.C.E.VAN VOORHIS,E.QUARTLY,E.M.PHIZICKY,
JRNL AUTH 3 A.LAURICELLA,J.LUFT,G.DETITTA,W.G.J.HOL
JRNL TITL CRYSTAL STRUCTURE OF ALPHA/BETA HYDROLASE FOLD
JRNL TITL 2 PROTEIN OF UNKNOWN FUNCTION.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 101.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 37326
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) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1866
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2516
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE SET COUNT : 129
REMARK 3 BIN FREE R VALUE : 0.3430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 4674
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.24
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.63000
REMARK 3 B22 (A**2) : 0.63000
REMARK 3 B33 (A**2) : -0.94000
REMARK 3 B12 (A**2) : 0.31000
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): 0.244
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.203
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.159
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.554
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4654 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3077 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6332 ; 1.247 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7508 ; 0.915 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 589 ; 6.264 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 215 ;35.024 ;24.093
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 743 ;15.936 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;16.397 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 717 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5240 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 932 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 951 ; 0.195 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3270 ; 0.196 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2259 ; 0.170 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2427 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 191 ; 0.180 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 12 ; 0.185 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 34 ; 0.364 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.131 ; 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): 3026 ; 0.374 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1184 ; 0.053 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4722 ; 0.642 ; 3.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1840 ; 0.752 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1608 ; 1.145 ; 6.000
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 : 0
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 8 A 26
REMARK 3 ORIGIN FOR THE GROUP (A): 44.9990 20.3790 123.5450
REMARK 3 T TENSOR
REMARK 3 T11: 0.1621 T22: 0.1288
REMARK 3 T33: -0.0052 T12: -0.0397
REMARK 3 T13: 0.1247 T23: 0.0867
REMARK 3 L TENSOR
REMARK 3 L11: 6.2167 L22: 8.7346
REMARK 3 L33: 10.2389 L12: 0.3021
REMARK 3 L13: -1.7621 L23: 2.7775
REMARK 3 S TENSOR
REMARK 3 S11: 0.0455 S12: -0.1442 S13: -0.4972
REMARK 3 S21: 0.4732 S22: -0.2718 S23: 0.2860
REMARK 3 S31: 0.7694 S32: -0.5467 S33: 0.2263
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 27 A 107
REMARK 3 ORIGIN FOR THE GROUP (A): 51.0500 23.7990 117.7140
REMARK 3 T TENSOR
REMARK 3 T11: 0.1430 T22: 0.1061
REMARK 3 T33: -0.0186 T12: -0.0128
REMARK 3 T13: 0.0305 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 3.2853 L22: 3.7187
REMARK 3 L33: 4.4481 L12: -0.4873
REMARK 3 L13: -1.9535 L23: -0.0450
REMARK 3 S TENSOR
REMARK 3 S11: 0.0997 S12: 0.1171 S13: 0.0107
REMARK 3 S21: 0.0747 S22: -0.0254 S23: 0.2263
REMARK 3 S31: 0.0510 S32: -0.3018 S33: -0.0743
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 108 A 150
REMARK 3 ORIGIN FOR THE GROUP (A): 62.0750 23.0330 111.2180
REMARK 3 T TENSOR
REMARK 3 T11: 0.1308 T22: 0.1009
REMARK 3 T33: -0.0344 T12: 0.0014
REMARK 3 T13: 0.0106 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 5.0230 L22: 0.9531
REMARK 3 L33: 3.2691 L12: -0.5642
REMARK 3 L13: -1.0056 L23: -0.5109
REMARK 3 S TENSOR
REMARK 3 S11: 0.0220 S12: 0.2496 S13: -0.1059
REMARK 3 S21: -0.0338 S22: -0.0538 S23: -0.0337
REMARK 3 S31: 0.0292 S32: 0.0231 S33: 0.0318
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 151 A 211
REMARK 3 ORIGIN FOR THE GROUP (A): 70.8560 9.3790 116.9250
REMARK 3 T TENSOR
REMARK 3 T11: 0.1167 T22: 0.1084
REMARK 3 T33: 0.0432 T12: 0.1595
REMARK 3 T13: 0.1291 T23: 0.1010
REMARK 3 L TENSOR
REMARK 3 L11: 4.4449 L22: 4.5668
REMARK 3 L33: 1.8333 L12: 3.2927
REMARK 3 L13: -1.7537 L23: -1.5905
REMARK 3 S TENSOR
REMARK 3 S11: -0.3152 S12: -0.3722 S13: -0.9214
REMARK 3 S21: -0.1694 S22: -0.2998 S23: -0.6186
REMARK 3 S31: 0.6381 S32: 0.7452 S33: 0.6150
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 212 A 243
REMARK 3 ORIGIN FOR THE GROUP (A): 73.6190 25.5670 111.1200
REMARK 3 T TENSOR
REMARK 3 T11: 0.0366 T22: 0.2217
REMARK 3 T33: -0.0491 T12: -0.0434
REMARK 3 T13: 0.0318 T23: 0.0655
REMARK 3 L TENSOR
REMARK 3 L11: 4.9257 L22: 2.8457
REMARK 3 L33: 5.9084 L12: -1.1683
REMARK 3 L13: 0.0608 L23: -0.6574
REMARK 3 S TENSOR
REMARK 3 S11: 0.1868 S12: -0.2319 S13: 0.0446
REMARK 3 S21: 0.1036 S22: -0.2201 S23: -0.4156
REMARK 3 S31: 0.1633 S32: 1.0108 S33: 0.0333
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 244 A 301
REMARK 3 ORIGIN FOR THE GROUP (A): 67.6700 33.0400 114.7470
REMARK 3 T TENSOR
REMARK 3 T11: 0.1559 T22: 0.0831
REMARK 3 T33: 0.0056 T12: -0.1437
REMARK 3 T13: 0.0966 T23: -0.0408
REMARK 3 L TENSOR
REMARK 3 L11: 4.9528 L22: 2.3052
REMARK 3 L33: 4.4392 L12: -1.1621
REMARK 3 L13: -0.8949 L23: 0.1230
REMARK 3 S TENSOR
REMARK 3 S11: 0.3746 S12: -0.0525 S13: 0.5214
REMARK 3 S21: 0.0405 S22: -0.0818 S23: -0.0331
REMARK 3 S31: -0.5689 S32: 0.4706 S33: -0.2928
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 9 B 31
REMARK 3 ORIGIN FOR THE GROUP (A): 49.1420 22.4600 131.0700
REMARK 3 T TENSOR
REMARK 3 T11: 0.2299 T22: 0.0774
REMARK 3 T33: 0.0136 T12: -0.0779
REMARK 3 T13: 0.1442 T23: 0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 7.6197 L22: 8.5090
REMARK 3 L33: 15.4013 L12: -0.5579
REMARK 3 L13: 2.9946 L23: -3.1471
REMARK 3 S TENSOR
REMARK 3 S11: 0.3330 S12: -0.1561 S13: 0.0387
REMARK 3 S21: 0.3737 S22: -0.3774 S23: -0.5528
REMARK 3 S31: 0.1463 S32: 0.7607 S33: 0.0445
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 32 B 73
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1810 18.2380 132.5500
REMARK 3 T TENSOR
REMARK 3 T11: 0.0803 T22: 0.1476
REMARK 3 T33: -0.0235 T12: -0.1091
REMARK 3 T13: 0.1438 T23: -0.0497
REMARK 3 L TENSOR
REMARK 3 L11: 3.9468 L22: 6.1225
REMARK 3 L33: 6.6444 L12: -0.7923
REMARK 3 L13: -1.5546 L23: -1.6507
REMARK 3 S TENSOR
REMARK 3 S11: 0.3285 S12: 0.1372 S13: 0.3287
REMARK 3 S21: 0.3881 S22: -0.1482 S23: 0.6781
REMARK 3 S31: -0.2161 S32: -0.8247 S33: -0.1803
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 74 B 150
REMARK 3 ORIGIN FOR THE GROUP (A): 44.4290 10.0990 140.3570
REMARK 3 T TENSOR
REMARK 3 T11: 0.3765 T22: 0.0638
REMARK 3 T33: -0.1139 T12: -0.2350
REMARK 3 T13: 0.0842 T23: -0.0324
REMARK 3 L TENSOR
REMARK 3 L11: 1.4436 L22: 4.4884
REMARK 3 L33: 3.6147 L12: 0.6122
REMARK 3 L13: -0.6452 L23: -0.2822
REMARK 3 S TENSOR
REMARK 3 S11: 0.2650 S12: -0.2102 S13: 0.1810
REMARK 3 S21: 0.8611 S22: -0.3840 S23: -0.0269
REMARK 3 S31: -0.0366 S32: 0.2080 S33: 0.1190
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 151 B 211
REMARK 3 ORIGIN FOR THE GROUP (A): 49.1120 -6.3950 134.1720
REMARK 3 T TENSOR
REMARK 3 T11: 0.4229 T22: -0.0281
REMARK 3 T33: -0.0461 T12: -0.1093
REMARK 3 T13: 0.0686 T23: 0.0547
REMARK 3 L TENSOR
REMARK 3 L11: 5.7515 L22: 3.3292
REMARK 3 L33: 2.0239 L12: 1.6101
REMARK 3 L13: -1.6898 L23: -1.0674
REMARK 3 S TENSOR
REMARK 3 S11: 0.0567 S12: -0.0443 S13: -0.6390
REMARK 3 S21: 0.1596 S22: -0.4990 S23: -0.4846
REMARK 3 S31: 0.7646 S32: 0.0247 S33: 0.4423
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 243
REMARK 3 ORIGIN FOR THE GROUP (A): 33.4480 -3.8740 140.4720
REMARK 3 T TENSOR
REMARK 3 T11: 0.3267 T22: 0.1173
REMARK 3 T33: -0.0466 T12: -0.3966
REMARK 3 T13: 0.2488 T23: -0.0538
REMARK 3 L TENSOR
REMARK 3 L11: 2.5298 L22: 6.4273
REMARK 3 L33: 7.3542 L12: 0.4668
REMARK 3 L13: 1.4563 L23: 0.2384
REMARK 3 S TENSOR
REMARK 3 S11: 0.1057 S12: -0.1570 S13: -0.1527
REMARK 3 S21: 0.4745 S22: -0.0406 S23: 0.0664
REMARK 3 S31: 0.8776 S32: -0.1193 S33: -0.0651
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 244 B 301
REMARK 3 ORIGIN FOR THE GROUP (A): 28.6110 4.6050 137.7530
REMARK 3 T TENSOR
REMARK 3 T11: 0.0939 T22: 0.1837
REMARK 3 T33: -0.0036 T12: -0.3790
REMARK 3 T13: 0.2366 T23: -0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 1.3602 L22: 6.3850
REMARK 3 L33: 3.4451 L12: 2.1257
REMARK 3 L13: -0.5313 L23: -1.8817
REMARK 3 S TENSOR
REMARK 3 S11: 0.5915 S12: 0.2225 S13: 0.3215
REMARK 3 S21: 0.4732 S22: -0.0556 S23: 1.1883
REMARK 3 S31: 0.3450 S32: -1.0130 S33: -0.5359
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2Q0X COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB043010.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-2005
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97953
REMARK 200 MONOCHROMATOR : DOUBLE SI(111) CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37476
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 101.062
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : 0.06000
REMARK 200 FOR THE DATA SET : 8.1000
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) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 0.61200
REMARK 200 R SYM FOR SHELL (I) : 0.61200
REMARK 200 FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4 UL PROTEIN: 10.5 MG/ML, 0.4 UL
REMARK 280 CRYSTALLIZATION BUFFER: 35% PEG 400, 100 MM NACL, 100 MM MES
REMARK 280 PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,1/3+Z
REMARK 290 3555 -X+Y,-X,2/3+Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,2/3-Z
REMARK 290 6555 -X,-X+Y,1/3-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 -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 101.06200
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 202.12400
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 202.12400
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 101.06200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 PRO A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 MET A 5
REMARK 465 TYR A 6
REMARK 465 ARG A 7
REMARK 465 GLU A 302
REMARK 465 LYS A 303
REMARK 465 ASN A 304
REMARK 465 ASN A 305
REMARK 465 ARG A 306
REMARK 465 ILE A 307
REMARK 465 LYS A 308
REMARK 465 ALA A 309
REMARK 465 ALA A 310
REMARK 465 GLU A 311
REMARK 465 ASP A 312
REMARK 465 GLU A 313
REMARK 465 LYS A 314
REMARK 465 LYS A 315
REMARK 465 ARG A 316
REMARK 465 LYS A 317
REMARK 465 SER A 318
REMARK 465 VAL A 319
REMARK 465 LEU A 320
REMARK 465 GLN A 321
REMARK 465 VAL A 322
REMARK 465 SER A 323
REMARK 465 SER A 324
REMARK 465 PHE A 325
REMARK 465 ALA A 326
REMARK 465 GLN A 327
REMARK 465 ALA A 328
REMARK 465 ALA A 329
REMARK 465 SER A 330
REMARK 465 SER A 331
REMARK 465 VAL A 332
REMARK 465 LYS A 333
REMARK 465 ALA A 334
REMARK 465 SER A 335
REMARK 465 GLY B 1
REMARK 465 PRO B 2
REMARK 465 GLY B 3
REMARK 465 SER B 4
REMARK 465 MET B 5
REMARK 465 TYR B 6
REMARK 465 ARG B 7
REMARK 465 SER B 8
REMARK 465 GLU B 302
REMARK 465 LYS B 303
REMARK 465 ASN B 304
REMARK 465 ASN B 305
REMARK 465 ARG B 306
REMARK 465 ILE B 307
REMARK 465 LYS B 308
REMARK 465 ALA B 309
REMARK 465 ALA B 310
REMARK 465 GLU B 311
REMARK 465 ASP B 312
REMARK 465 GLU B 313
REMARK 465 LYS B 314
REMARK 465 LYS B 315
REMARK 465 ARG B 316
REMARK 465 LYS B 317
REMARK 465 SER B 318
REMARK 465 VAL B 319
REMARK 465 LEU B 320
REMARK 465 GLN B 321
REMARK 465 VAL B 322
REMARK 465 SER B 323
REMARK 465 SER B 324
REMARK 465 PHE B 325
REMARK 465 ALA B 326
REMARK 465 GLN B 327
REMARK 465 ALA B 328
REMARK 465 ALA B 329
REMARK 465 SER B 330
REMARK 465 SER B 331
REMARK 465 VAL B 332
REMARK 465 LYS B 333
REMARK 465 ALA B 334
REMARK 465 SER B 335
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 ARG A 38 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 155 CG CD OE1 OE2
REMARK 470 LYS A 166 CG CD CE NZ
REMARK 470 GLN A 236 CG CD OE1 NE2
REMARK 470 LYS A 238 CD CE NZ
REMARK 470 GLU A 271 CG CD OE1 OE2
REMARK 470 GLU A 296 CG CD OE1 OE2
REMARK 470 GLU A 300 CG CD OE1 OE2
REMARK 470 THR A 301 OG1 CG2
REMARK 470 ARG B 38 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 155 CG CD OE1 OE2
REMARK 470 GLU B 162 CG CD OE1 OE2
REMARK 470 LYS B 166 CG CD CE NZ
REMARK 470 LYS B 238 CD CE NZ
REMARK 470 ASN B 258 CG OD1 ND2
REMARK 470 LYS B 277 CG CD CE NZ
REMARK 470 GLU B 296 CG CD OE1 OE2
REMARK 470 PHE B 297 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 300 CG CD OE1 OE2
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
REMARK 500 NH1 ARG A 137 O HOH 110 2.07
REMARK 500 OE2 GLU B 74 O HOH 11 2.09
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP B 253 CG ASP B 253 OD1 0.127
REMARK 500 ASP B 253 CG ASP B 253 OD2 0.107
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 23 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 108 DISTANCE = 9.57 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TBRU020260AAA RELATED DB: TARGETDB
DBREF 2Q0X A 5 335 UNP Q389W3 Q389W3_9TRYP 1 331
DBREF 2Q0X B 5 335 UNP Q389W3 Q389W3_9TRYP 1 331
SEQADV 2Q0X GLY A 1 UNP Q389W3 CLONING ARTIFACT
SEQADV 2Q0X PRO A 2 UNP Q389W3 CLONING ARTIFACT
SEQADV 2Q0X GLY A 3 UNP Q389W3 CLONING ARTIFACT
SEQADV 2Q0X SER A 4 UNP Q389W3 CLONING ARTIFACT
SEQADV 2Q0X GLY B 1 UNP Q389W3 CLONING ARTIFACT
SEQADV 2Q0X PRO B 2 UNP Q389W3 CLONING ARTIFACT
SEQADV 2Q0X GLY B 3 UNP Q389W3 CLONING ARTIFACT
SEQADV 2Q0X SER B 4 UNP Q389W3 CLONING ARTIFACT
SEQRES 1 A 335 GLY PRO GLY SER MET TYR ARG SER ARG PRO GLU PRO VAL
SEQRES 2 A 335 GLN GLY HIS LEU PHE THR TYR TYR LYS ASP PRO TYR CYS
SEQRES 3 A 335 LYS ILE PRO VAL PHE MET MET ASN MET ASP ALA ARG ARG
SEQRES 4 A 335 CYS VAL LEU TRP VAL GLY GLY GLN THR GLU SER LEU LEU
SEQRES 5 A 335 SER PHE ASP TYR PHE THR ASN LEU ALA GLU GLU LEU GLN
SEQRES 6 A 335 GLY ASP TRP ALA PHE VAL GLN VAL GLU VAL PRO SER GLY
SEQRES 7 A 335 LYS ILE GLY SER GLY PRO GLN ASP HIS ALA HIS ASP ALA
SEQRES 8 A 335 GLU ASP VAL ASP ASP LEU ILE GLY ILE LEU LEU ARG ASP
SEQRES 9 A 335 HIS CYS MET ASN GLU VAL ALA LEU PHE ALA THR SER THR
SEQRES 10 A 335 GLY THR GLN LEU VAL PHE GLU LEU LEU GLU ASN SER ALA
SEQRES 11 A 335 HIS LYS SER SER ILE THR ARG VAL ILE LEU HIS GLY VAL
SEQRES 12 A 335 VAL CYS ASP PRO GLU ASN PRO LEU PHE THR PRO GLU GLY
SEQRES 13 A 335 CYS ALA ALA ARG LYS GLU HIS VAL GLU LYS LEU MET ALA
SEQRES 14 A 335 GLU GLY ARG GLY GLU ASP SER LEU ALA MET LEU LYS HIS
SEQRES 15 A 335 TYR ASP ILE PRO ILE THR PRO ALA ARG LEU ALA GLY GLY
SEQRES 16 A 335 GLY PHE PRO THR LEU GLN GLU ALA VAL TRP ASN PRO CYS
SEQRES 17 A 335 ILE ARG LYS GLU PHE ASP VAL LEU ARG ARG SER VAL GLY
SEQRES 18 A 335 VAL ILE LYS VAL PRO LEU LEU LEU MET LEU ALA HIS ASN
SEQRES 19 A 335 VAL GLN TYR LYS PRO SER ASP GLU GLU VAL GLY THR VAL
SEQRES 20 A 335 LEU GLU GLY VAL ARG ASP HIS THR GLY CYS ASN ARG VAL
SEQRES 21 A 335 THR VAL SER TYR PHE ASN ASP THR CYS ASP GLU LEU ARG
SEQRES 22 A 335 ARG VAL LEU LYS ALA ALA GLU SER GLU HIS VAL ALA ALA
SEQRES 23 A 335 ILE LEU GLN PHE LEU ALA ASP GLU ASP GLU PHE ARG THR
SEQRES 24 A 335 GLU THR GLU LYS ASN ASN ARG ILE LYS ALA ALA GLU ASP
SEQRES 25 A 335 GLU LYS LYS ARG LYS SER VAL LEU GLN VAL SER SER PHE
SEQRES 26 A 335 ALA GLN ALA ALA SER SER VAL LYS ALA SER
SEQRES 1 B 335 GLY PRO GLY SER MET TYR ARG SER ARG PRO GLU PRO VAL
SEQRES 2 B 335 GLN GLY HIS LEU PHE THR TYR TYR LYS ASP PRO TYR CYS
SEQRES 3 B 335 LYS ILE PRO VAL PHE MET MET ASN MET ASP ALA ARG ARG
SEQRES 4 B 335 CYS VAL LEU TRP VAL GLY GLY GLN THR GLU SER LEU LEU
SEQRES 5 B 335 SER PHE ASP TYR PHE THR ASN LEU ALA GLU GLU LEU GLN
SEQRES 6 B 335 GLY ASP TRP ALA PHE VAL GLN VAL GLU VAL PRO SER GLY
SEQRES 7 B 335 LYS ILE GLY SER GLY PRO GLN ASP HIS ALA HIS ASP ALA
SEQRES 8 B 335 GLU ASP VAL ASP ASP LEU ILE GLY ILE LEU LEU ARG ASP
SEQRES 9 B 335 HIS CYS MET ASN GLU VAL ALA LEU PHE ALA THR SER THR
SEQRES 10 B 335 GLY THR GLN LEU VAL PHE GLU LEU LEU GLU ASN SER ALA
SEQRES 11 B 335 HIS LYS SER SER ILE THR ARG VAL ILE LEU HIS GLY VAL
SEQRES 12 B 335 VAL CYS ASP PRO GLU ASN PRO LEU PHE THR PRO GLU GLY
SEQRES 13 B 335 CYS ALA ALA ARG LYS GLU HIS VAL GLU LYS LEU MET ALA
SEQRES 14 B 335 GLU GLY ARG GLY GLU ASP SER LEU ALA MET LEU LYS HIS
SEQRES 15 B 335 TYR ASP ILE PRO ILE THR PRO ALA ARG LEU ALA GLY GLY
SEQRES 16 B 335 GLY PHE PRO THR LEU GLN GLU ALA VAL TRP ASN PRO CYS
SEQRES 17 B 335 ILE ARG LYS GLU PHE ASP VAL LEU ARG ARG SER VAL GLY
SEQRES 18 B 335 VAL ILE LYS VAL PRO LEU LEU LEU MET LEU ALA HIS ASN
SEQRES 19 B 335 VAL GLN TYR LYS PRO SER ASP GLU GLU VAL GLY THR VAL
SEQRES 20 B 335 LEU GLU GLY VAL ARG ASP HIS THR GLY CYS ASN ARG VAL
SEQRES 21 B 335 THR VAL SER TYR PHE ASN ASP THR CYS ASP GLU LEU ARG
SEQRES 22 B 335 ARG VAL LEU LYS ALA ALA GLU SER GLU HIS VAL ALA ALA
SEQRES 23 B 335 ILE LEU GLN PHE LEU ALA ASP GLU ASP GLU PHE ARG THR
SEQRES 24 B 335 GLU THR GLU LYS ASN ASN ARG ILE LYS ALA ALA GLU ASP
SEQRES 25 B 335 GLU LYS LYS ARG LYS SER VAL LEU GLN VAL SER SER PHE
SEQRES 26 B 335 ALA GLN ALA ALA SER SER VAL LYS ALA SER
HET GOL 1 6
HET GOL 2 6
HETNAM GOL GLYCEROL
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 HOH *123(H2 O1)
HELIX 1 1 TYR A 56 GLN A 65 1 10
HELIX 2 2 VAL A 75 LYS A 79 5 5
HELIX 3 3 ASP A 86 HIS A 105 1 20
HELIX 4 4 GLY A 118 SER A 129 1 12
HELIX 5 5 HIS A 131 SER A 133 5 3
HELIX 6 6 THR A 153 GLY A 171 1 19
HELIX 7 7 ASP A 175 LEU A 180 5 6
HELIX 8 8 THR A 188 GLY A 194 1 7
HELIX 9 9 THR A 199 VAL A 204 1 6
HELIX 10 10 VAL A 204 ARG A 210 1 7
HELIX 11 11 GLU A 212 SER A 219 1 8
HELIX 12 12 VAL A 220 ILE A 223 5 4
HELIX 13 13 SER A 240 THR A 255 1 16
HELIX 14 14 ALA A 279 GLU A 300 1 22
HELIX 15 15 ASP B 55 GLN B 65 1 11
HELIX 16 16 VAL B 75 LYS B 79 5 5
HELIX 17 17 ASP B 86 HIS B 105 1 20
HELIX 18 18 THR B 117 SER B 129 1 13
HELIX 19 19 THR B 153 GLU B 170 1 18
HELIX 20 20 ASP B 175 LEU B 180 5 6
HELIX 21 21 THR B 188 GLY B 194 1 7
HELIX 22 22 THR B 199 VAL B 204 1 6
HELIX 23 23 VAL B 204 ARG B 210 1 7
HELIX 24 24 GLU B 212 SER B 219 1 8
HELIX 25 25 VAL B 220 ILE B 223 5 4
HELIX 26 26 SER B 240 THR B 255 1 16
HELIX 27 27 ALA B 279 GLU B 300 1 22
SHEET 1 A16 VAL A 260 TYR A 264 0
SHEET 2 A16 LEU A 227 ALA A 232 1 N LEU A 231 O SER A 263
SHEET 3 A16 ILE A 135 VAL A 143 1 N LEU A 140 O MET A 230
SHEET 4 A16 VAL A 110 THR A 115 1 N LEU A 112 O ILE A 139
SHEET 5 A16 CYS A 40 VAL A 44 1 N LEU A 42 O PHE A 113
SHEET 6 A16 ALA A 69 VAL A 73 1 O VAL A 71 N VAL A 41
SHEET 7 A16 CYS A 26 MET A 33 -1 N PHE A 31 O GLN A 72
SHEET 8 A16 VAL A 13 ASP A 23 -1 N PHE A 18 O VAL A 30
SHEET 9 A16 VAL B 13 TYR B 21 -1 O VAL B 13 N LEU A 17
SHEET 10 A16 LYS B 27 MET B 33 -1 O MET B 32 N HIS B 16
SHEET 11 A16 ALA B 69 VAL B 73 -1 O GLN B 72 N PHE B 31
SHEET 12 A16 CYS B 40 VAL B 44 1 N VAL B 41 O VAL B 71
SHEET 13 A16 VAL B 110 THR B 115 1 O ALA B 111 N LEU B 42
SHEET 14 A16 ILE B 135 VAL B 143 1 O ILE B 139 N LEU B 112
SHEET 15 A16 LEU B 227 ALA B 232 1 O MET B 230 N LEU B 140
SHEET 16 A16 VAL B 260 TYR B 264 1 O THR B 261 N LEU B 229
SHEET 1 B 2 THR A 268 CYS A 269 0
SHEET 2 B 2 VAL A 275 LYS A 277 -1 O LYS A 277 N THR A 268
SHEET 1 C 2 THR B 268 CYS B 269 0
SHEET 2 C 2 VAL B 275 LYS B 277 -1 O LYS B 277 N THR B 268
CISPEP 1 GLY A 83 PRO A 84 0 3.93
CISPEP 2 GLU A 300 THR A 301 0 -4.13
CISPEP 3 GLY B 83 PRO B 84 0 0.49
CRYST1 63.556 63.556 303.186 90.00 90.00 120.00 P 31 2 1 12
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 0.015734 0.009084 0.000000 0.00000
SCALE2 0.000000 0.018168 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003298 0.00000
TER 2277 THR A 301
TER 4541 THR B 301
MASTER 619 0 2 27 20 0 0 6 4674 2 12 52
END |