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HEADER HYDROLASE 13-APR-23 8J1O
TITLE CRYSTAL STRUCTURE OF HALOTAG COMPLEXED WITH BTTA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP. (IN: HIGH G+C GRAM-POSITIVE
SOURCE 3 BACTERIA);
SOURCE 4 ORGANISM_TAXID: 1831;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.KIM,H.RHEE,C.LEE
REVDAT 1 17-APR-24 8J1O 0
JRNL AUTH H.KIM,C.LEE,H.RHEE
JRNL TITL CRYSTAL STRUCTURE OF HALOTAG COMPLEXED WITH BTTA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.14_3260: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.16
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 23477
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1173
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 30.1550 - 3.9792 0.99 2977 157 0.1510 0.1581
REMARK 3 2 3.9792 - 3.1595 1.00 2827 148 0.1415 0.1843
REMARK 3 3 3.1595 - 2.7604 1.00 2796 148 0.1662 0.2368
REMARK 3 4 2.7604 - 2.5082 1.00 2756 144 0.1673 0.2224
REMARK 3 5 2.5082 - 2.3285 1.00 2753 146 0.1601 0.2169
REMARK 3 6 2.3285 - 2.1912 1.00 2737 144 0.1512 0.2018
REMARK 3 7 2.1912 - 2.0815 1.00 2733 143 0.1581 0.2193
REMARK 3 8 2.0815 - 1.9910 1.00 2725 143 0.1709 0.2348
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.400
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.012 2478
REMARK 3 ANGLE : 0.963 3385
REMARK 3 CHIRALITY : 0.062 355
REMARK 3 PLANARITY : 0.006 442
REMARK 3 DIHEDRAL : 7.962 2021
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 80 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.6744 -10.1781 -11.3370
REMARK 3 T TENSOR
REMARK 3 T11: 0.0869 T22: 0.1057
REMARK 3 T33: 0.1242 T12: -0.0010
REMARK 3 T13: -0.0057 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.6231 L22: 0.6850
REMARK 3 L33: 0.9514 L12: 0.0353
REMARK 3 L13: -0.0251 L23: -0.0944
REMARK 3 S TENSOR
REMARK 3 S11: -0.0455 S12: 0.0775 S13: -0.0045
REMARK 3 S21: 0.0211 S22: 0.0320 S23: -0.0504
REMARK 3 S31: 0.0060 S32: 0.0097 S33: 0.0035
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 81 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.6281 0.2498 -4.2880
REMARK 3 T TENSOR
REMARK 3 T11: 0.1775 T22: 0.1028
REMARK 3 T33: 0.1555 T12: -0.0104
REMARK 3 T13: -0.0320 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 2.7961 L22: 1.4286
REMARK 3 L33: 1.3857 L12: 0.5408
REMARK 3 L13: -0.8534 L23: -0.4753
REMARK 3 S TENSOR
REMARK 3 S11: -0.0603 S12: 0.0088 S13: 0.1072
REMARK 3 S21: 0.0949 S22: 0.1306 S23: -0.1333
REMARK 3 S31: -0.3305 S32: 0.0161 S33: -0.0818
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 100 THROUGH 129 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.8601 2.5130 -11.6565
REMARK 3 T TENSOR
REMARK 3 T11: 0.1543 T22: 0.1189
REMARK 3 T33: 0.1143 T12: 0.0521
REMARK 3 T13: -0.0109 T23: 0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 1.0064 L22: 0.6878
REMARK 3 L33: 1.8755 L12: -0.3578
REMARK 3 L13: -0.0777 L23: 0.3117
REMARK 3 S TENSOR
REMARK 3 S11: -0.0027 S12: 0.0687 S13: 0.1511
REMARK 3 S21: -0.0283 S22: 0.0236 S23: 0.0148
REMARK 3 S31: -0.3083 S32: -0.2976 S33: -0.0082
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 130 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1959 -8.2082 -5.5307
REMARK 3 T TENSOR
REMARK 3 T11: 0.1024 T22: 0.4339
REMARK 3 T33: 0.2450 T12: 0.0125
REMARK 3 T13: 0.0163 T23: 0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 0.2725 L22: 0.2924
REMARK 3 L33: 0.7037 L12: 0.0145
REMARK 3 L13: -0.1944 L23: -0.4161
REMARK 3 S TENSOR
REMARK 3 S11: 0.0415 S12: 0.2247 S13: 0.1078
REMARK 3 S21: -0.0483 S22: 0.0658 S23: 0.3268
REMARK 3 S31: -0.0020 S32: -0.4985 S33: -0.0022
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 153 THROUGH 195 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1853 -21.2078 -4.6249
REMARK 3 T TENSOR
REMARK 3 T11: 0.1295 T22: 0.2050
REMARK 3 T33: 0.1726 T12: -0.0609
REMARK 3 T13: 0.0117 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 0.3971 L22: 0.7312
REMARK 3 L33: 1.2730 L12: -0.1961
REMARK 3 L13: 0.1767 L23: 0.2300
REMARK 3 S TENSOR
REMARK 3 S11: -0.1040 S12: 0.1120 S13: -0.0652
REMARK 3 S21: 0.0786 S22: 0.0304 S23: 0.0619
REMARK 3 S31: 0.2787 S32: -0.3692 S33: 0.0262
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 196 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8899 -10.1804 2.6279
REMARK 3 T TENSOR
REMARK 3 T11: 0.1164 T22: 0.1896
REMARK 3 T33: 0.1290 T12: 0.0010
REMARK 3 T13: 0.0211 T23: 0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 1.2620 L22: 1.6826
REMARK 3 L33: 1.8904 L12: -0.2425
REMARK 3 L13: 0.3893 L23: -0.3596
REMARK 3 S TENSOR
REMARK 3 S11: -0.0800 S12: 0.0107 S13: -0.0153
REMARK 3 S21: 0.2050 S22: 0.0508 S23: 0.0722
REMARK 3 S31: -0.0730 S32: -0.3303 S33: 0.0327
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 216 THROUGH 231 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8641 7.2968 -6.0308
REMARK 3 T TENSOR
REMARK 3 T11: 0.2338 T22: 0.2443
REMARK 3 T33: 0.2003 T12: 0.1535
REMARK 3 T13: -0.0176 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.9311 L22: 0.8722
REMARK 3 L33: 2.8573 L12: 0.0922
REMARK 3 L13: -0.1708 L23: -0.9510
REMARK 3 S TENSOR
REMARK 3 S11: -0.0406 S12: 0.0398 S13: 0.1561
REMARK 3 S21: 0.0195 S22: -0.0548 S23: 0.2156
REMARK 3 S31: -0.3910 S32: -0.2799 S33: -0.0972
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 232 THROUGH 248 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3819 -1.4610 -18.8462
REMARK 3 T TENSOR
REMARK 3 T11: 0.1054 T22: 0.3524
REMARK 3 T33: 0.1820 T12: 0.0436
REMARK 3 T13: -0.0172 T23: 0.0616
REMARK 3 L TENSOR
REMARK 3 L11: 0.3959 L22: 0.0533
REMARK 3 L33: 0.7345 L12: 0.0426
REMARK 3 L13: -0.3041 L23: -0.1891
REMARK 3 S TENSOR
REMARK 3 S11: 0.0463 S12: 0.0019 S13: 0.0517
REMARK 3 S21: 0.0098 S22: 0.0441 S23: 0.1400
REMARK 3 S31: -0.0071 S32: -0.4031 S33: 0.0348
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 249 THROUGH 278 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.3721 -3.1659 -20.6740
REMARK 3 T TENSOR
REMARK 3 T11: 0.1267 T22: 0.3817
REMARK 3 T33: 0.1673 T12: 0.0339
REMARK 3 T13: -0.0372 T23: 0.0611
REMARK 3 L TENSOR
REMARK 3 L11: 0.3396 L22: 0.6431
REMARK 3 L33: 0.4453 L12: -0.2363
REMARK 3 L13: 0.1077 L23: -0.5189
REMARK 3 S TENSOR
REMARK 3 S11: 0.0360 S12: 0.1447 S13: -0.0025
REMARK 3 S21: -0.0427 S22: 0.0900 S23: 0.1588
REMARK 3 S31: -0.0623 S32: -0.4235 S33: -0.0533
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 279 THROUGH 297 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.7267 -0.9881 -28.1181
REMARK 3 T TENSOR
REMARK 3 T11: 0.1248 T22: 0.2370
REMARK 3 T33: 0.0949 T12: 0.0235
REMARK 3 T13: -0.0111 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 2.0232 L22: 2.9091
REMARK 3 L33: 2.5209 L12: 0.4801
REMARK 3 L13: -0.3514 L23: -1.1329
REMARK 3 S TENSOR
REMARK 3 S11: -0.0032 S12: -0.0007 S13: 0.0335
REMARK 3 S21: -0.0427 S22: 0.0608 S23: 0.0755
REMARK 3 S31: -0.1753 S32: -0.1123 S33: -0.0306
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8J1O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-APR-23.
REMARK 100 THE DEPOSITION ID IS D_1300037036.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97960
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23615
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 30.155
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 22.0300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3M AMMONIUM SULFATE, 0.1M CITRIC
REMARK 280 ACID PH 5.3, 2% MPD, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 81.84050
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.54400
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.54400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 122.76075
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.54400
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.54400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.92025
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.54400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.54400
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 122.76075
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.54400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.54400
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.92025
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 81.84050
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 TOTAL BURIED SURFACE AREA: 280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 417 O HOH A 477 1.97
REMARK 500 O HOH A 401 O HOH A 621 2.06
REMARK 500 O HOH A 531 O HOH A 616 2.09
REMARK 500 OE2 GLU A 16 O HOH A 401 2.15
REMARK 500
REMARK 500 REMARK: NULL
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 O HOH A 406 O HOH A 512 4555 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
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 PRO A 9 54.71 -91.76
REMARK 500 PRO A 42 47.52 -105.67
REMARK 500 THR A 43 -157.58 -101.71
REMARK 500 GLU A 98 -92.25 -110.51
REMARK 500 ASP A 106 -127.80 58.25
REMARK 500 GLU A 130 61.63 39.25
REMARK 500 ARG A 153 42.86 -90.28
REMARK 500 VAL A 245 -67.10 -135.59
REMARK 500 LEU A 271 -97.76 -121.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 678 DISTANCE = 8.81 ANGSTROMS
DBREF 8J1O A 4 297 PDB 8J1O 8J1O 4 297
SEQRES 1 A 294 ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL GLU
SEQRES 2 A 294 VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY PRO
SEQRES 3 A 294 ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 A 294 THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS VAL
SEQRES 5 A 294 ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 A 294 MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE PHE
SEQRES 7 A 294 ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU ALA
SEQRES 8 A 294 LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP TRP
SEQRES 9 A 294 GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN PRO
SEQRES 10 A 294 GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE ARG
SEQRES 11 A 294 PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA ARG
SEQRES 12 A 294 GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY ARG
SEQRES 13 A 294 LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY THR
SEQRES 14 A 294 LEU PRO CYS GLY VAL VAL ARG PRO LEU THR GLU VAL GLU
SEQRES 15 A 294 MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL ASP
SEQRES 16 A 294 ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO ILE
SEQRES 17 A 294 ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU GLU
SEQRES 18 A 294 TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS LEU
SEQRES 19 A 294 LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO ALA
SEQRES 20 A 294 GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS LYS
SEQRES 21 A 294 ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN GLU
SEQRES 22 A 294 ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG TRP
SEQRES 23 A 294 LEU SER THR LEU GLU ILE SER GLY
HET TN9 A 301 34
HET CL A 302 1
HET SO4 A 303 5
HETNAM TN9 N-[[1-[2-[2-(2-HEXOXYETHOXY)ETHOXY]ETHYL]-1,2,3-
HETNAM 2 TN9 TRIAZOL-4-YL]METHYL]-1-(1H-1,2,3-TRIAZOL-4-YL)-N-(2H-
HETNAM 3 TN9 1,2,3-TRIAZOL-4-YLMETHYL)METHANAMINE
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
FORMUL 2 TN9 C21 H36 N10 O3
FORMUL 3 CL CL 1-
FORMUL 4 SO4 O4 S 2-
FORMUL 5 HOH *278(H2 O)
HELIX 1 AA1 SER A 44 ARG A 49 5 6
HELIX 2 AA2 ILE A 51 ALA A 56 1 6
HELIX 3 AA3 PHE A 80 LEU A 95 1 16
HELIX 4 AA4 ASP A 106 ASN A 119 1 14
HELIX 5 AA5 THR A 137 TRP A 141 5 5
HELIX 6 AA6 PRO A 142 ARG A 153 1 12
HELIX 7 AA7 THR A 155 ILE A 163 1 9
HELIX 8 AA8 ASN A 166 GLY A 171 1 6
HELIX 9 AA9 LEU A 173 VAL A 177 5 5
HELIX 10 AB1 THR A 182 GLU A 191 1 10
HELIX 11 AB2 PRO A 192 LEU A 194 5 3
HELIX 12 AB3 ASN A 195 ASP A 198 5 4
HELIX 13 AB4 ARG A 199 LEU A 209 1 11
HELIX 14 AB5 PRO A 215 SER A 232 1 18
HELIX 15 AB6 PRO A 248 LEU A 259 1 12
HELIX 16 AB7 LEU A 273 ASN A 278 1 6
HELIX 17 AB8 ASN A 278 LEU A 293 1 16
SHEET 1 AA1 8 HIS A 13 VAL A 17 0
SHEET 2 AA1 8 GLU A 20 VAL A 27 -1 O GLU A 20 N VAL A 17
SHEET 3 AA1 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 AA1 8 VAL A 35 LEU A 38 1 N PHE A 37 O ILE A 62
SHEET 5 AA1 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 AA1 8 VAL A 123 MET A 129 1 O ALA A 127 N LEU A 102
SHEET 7 AA1 8 LYS A 236 PRO A 243 1 O LEU A 237 N PHE A 128
SHEET 8 AA1 8 CYS A 262 GLY A 270 1 O LYS A 263 N LEU A 238
CISPEP 1 ASN A 41 PRO A 42 0 -1.60
CISPEP 2 GLU A 214 PRO A 215 0 -6.51
CISPEP 3 THR A 242 PRO A 243 0 1.71
CRYST1 63.088 63.088 163.681 90.00 90.00 90.00 P 43 21 2 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 0.015851 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015851 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006109 0.00000
TER 2359 GLY A 297
MASTER 437 0 3 17 8 0 0 6 2671 1 39 23
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