HEADER CHAPERONE 12-MAY-19 6OWX
TITLE SPY H96L:IM7 L18PI-PHE COMPLEX; MULTIPLE ANOMALOUS DATASETS CONTAINED
TITLE 2 HEREIN FOR ELEMENT IDENTIFICATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PERIPLASMIC CHAPERONE SPY;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: SPHEROPLAST PROTEIN Y;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PERIPLASMIC, CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.ROCCHIO,R.DUMAN,K.EL OMARI,V.MYKHAYLYK,Z.YAN,A.WAGNER,
AUTHOR 2 J.C.A.BARDWELL,S.HOROWITZ
REVDAT 6 11-OCT-23 6OWX 1 LINK
REVDAT 5 11-DEC-19 6OWX 1 JRNL
REVDAT 4 20-NOV-19 6OWX 1 REMARK
REVDAT 3 09-OCT-19 6OWX 1 REMARK LINK SITE CRYST1
REVDAT 3 2 1 ATOM
REVDAT 2 05-JUN-19 6OWX 1 AUTHOR JRNL
REVDAT 1 29-MAY-19 6OWX 0
JRNL AUTH S.ROCCHIO,R.DUMAN,K.EL OMARI,V.MYKHAYLYK,C.ORR,Z.YAN,
JRNL AUTH 2 L.SALMON,A.WAGNER,J.C.A.BARDWELL,S.HOROWITZ
JRNL TITL IDENTIFYING DYNAMIC, PARTIALLY OCCUPIED RESIDUES USING
JRNL TITL 2 ANOMALOUS SCATTERING.
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 75 1084 2019
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 31793902
JRNL DOI 10.1107/S2059798319014475
REMARK 2
REMARK 2 RESOLUTION. 2.06 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.910
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 27823
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.243
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.170
REMARK 3 FREE R VALUE TEST SET COUNT : 1716
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 40.5600 - 4.7100 1.00 2179 142 0.2293 0.2805
REMARK 3 2 4.7100 - 3.7400 1.00 2195 141 0.2024 0.2468
REMARK 3 3 3.7400 - 3.2700 1.00 2165 145 0.2356 0.2681
REMARK 3 4 3.2700 - 2.9700 1.00 2182 148 0.2571 0.2876
REMARK 3 5 2.9700 - 2.7600 1.00 2161 142 0.2577 0.2784
REMARK 3 6 2.7600 - 2.6000 1.00 2181 143 0.2648 0.3251
REMARK 3 7 2.6000 - 2.4700 1.00 2195 147 0.2605 0.2650
REMARK 3 8 2.4700 - 2.3600 1.00 2157 145 0.2644 0.2999
REMARK 3 9 2.3600 - 2.2700 1.00 2166 137 0.2767 0.2893
REMARK 3 10 2.2700 - 2.1900 1.00 2212 147 0.3029 0.2879
REMARK 3 11 2.1900 - 2.1200 1.00 2134 139 0.3481 0.3318
REMARK 3 12 2.1200 - 2.0600 0.99 2180 140 0.3474 0.3936
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.312
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.167
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.05
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.97
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 1410
REMARK 3 ANGLE : 1.216 1887
REMARK 3 CHIRALITY : 0.052 214
REMARK 3 PLANARITY : 0.008 254
REMARK 3 DIHEDRAL : 19.770 522
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 28 THROUGH 36 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.2523 -4.1001 254.3307
REMARK 3 T TENSOR
REMARK 3 T11: 0.4613 T22: 1.0288
REMARK 3 T33: 0.6969 T12: -0.0208
REMARK 3 T13: 0.0552 T23: 0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 5.9181 L22: 7.0158
REMARK 3 L33: 1.9298 L12: -3.8376
REMARK 3 L13: 4.7008 L23: 1.6573
REMARK 3 S TENSOR
REMARK 3 S11: 0.6081 S12: 1.0070 S13: 0.1128
REMARK 3 S21: -0.5010 S22: 0.1094 S23: -1.5219
REMARK 3 S31: -0.4369 S32: 1.4573 S33: -0.4918
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 37 THROUGH 50 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.7821 1.4079 260.5421
REMARK 3 T TENSOR
REMARK 3 T11: 0.4096 T22: 0.5211
REMARK 3 T33: 0.5184 T12: -0.0335
REMARK 3 T13: 0.0217 T23: -0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 2.7781 L22: 2.5056
REMARK 3 L33: 10.0173 L12: -4.0998
REMARK 3 L13: -2.1074 L23: 1.7177
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: 0.1211 S13: 0.1800
REMARK 3 S21: -0.0825 S22: -0.5246 S23: 0.1594
REMARK 3 S31: -1.0029 S32: -0.5788 S33: 0.6061
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 57 THROUGH 71 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8054 27.4044 274.6150
REMARK 3 T TENSOR
REMARK 3 T11: 0.4465 T22: 0.5278
REMARK 3 T33: 0.5938 T12: -0.1231
REMARK 3 T13: -0.0370 T23: 0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 9.0336 L22: 6.2742
REMARK 3 L33: 6.7302 L12: -0.6475
REMARK 3 L13: -0.1315 L23: -3.2414
REMARK 3 S TENSOR
REMARK 3 S11: 0.5287 S12: 0.5716 S13: -0.4535
REMARK 3 S21: 0.1287 S22: 0.1492 S23: 1.4916
REMARK 3 S31: 1.4592 S32: -1.0184 S33: -0.4970
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 72 THROUGH 108 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.0252 9.8652 275.2673
REMARK 3 T TENSOR
REMARK 3 T11: 0.4923 T22: 0.4392
REMARK 3 T33: 0.4956 T12: -0.1110
REMARK 3 T13: -0.0455 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 3.8781 L22: 7.9830
REMARK 3 L33: 2.1537 L12: 5.4492
REMARK 3 L13: 3.5515 L23: 5.0214
REMARK 3 S TENSOR
REMARK 3 S11: -0.2236 S12: 0.1205 S13: 0.4969
REMARK 3 S21: -0.1230 S22: 0.0399 S23: 0.6247
REMARK 3 S31: -0.1562 S32: 0.1548 S33: 0.2040
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 29 THROUGH 36 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0633 29.9865 261.1707
REMARK 3 T TENSOR
REMARK 3 T11: 0.8003 T22: 0.9767
REMARK 3 T33: 0.9778 T12: -0.2431
REMARK 3 T13: 0.0839 T23: -0.2160
REMARK 3 L TENSOR
REMARK 3 L11: 2.0640 L22: 8.5116
REMARK 3 L33: 2.0649 L12: 1.5150
REMARK 3 L13: -0.6393 L23: -4.3847
REMARK 3 S TENSOR
REMARK 3 S11: -0.8977 S12: 2.0231 S13: -1.3924
REMARK 3 S21: -1.6443 S22: 0.7389 S23: 1.0494
REMARK 3 S31: 0.5565 S32: 0.7316 S33: 0.2853
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 37 THROUGH 52 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.6132 20.7639 271.7826
REMARK 3 T TENSOR
REMARK 3 T11: 0.7133 T22: 0.6580
REMARK 3 T33: 1.8651 T12: -0.0897
REMARK 3 T13: 0.0431 T23: 0.0553
REMARK 3 L TENSOR
REMARK 3 L11: 1.8869 L22: 2.0830
REMARK 3 L33: 2.1318 L12: 1.9369
REMARK 3 L13: 1.5460 L23: 2.0164
REMARK 3 S TENSOR
REMARK 3 S11: 0.1895 S12: -0.7141 S13: -2.7222
REMARK 3 S21: 0.8381 S22: -1.0207 S23: -2.9674
REMARK 3 S31: 0.3105 S32: 1.3766 S33: 1.8602
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 57 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5347 1.2345 276.6368
REMARK 3 T TENSOR
REMARK 3 T11: 1.6951 T22: 1.1363
REMARK 3 T33: 1.2457 T12: -0.3421
REMARK 3 T13: 0.0466 T23: -0.1584
REMARK 3 L TENSOR
REMARK 3 L11: 1.9824 L22: 6.1190
REMARK 3 L33: 4.3429 L12: 9.4408
REMARK 3 L13: 7.9181 L23: 5.1019
REMARK 3 S TENSOR
REMARK 3 S11: 0.2534 S12: -0.4108 S13: 1.7631
REMARK 3 S21: 0.4754 S22: -0.0985 S23: -2.1288
REMARK 3 S31: -0.0007 S32: -0.3142 S33: -0.2493
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 62 THROUGH 72 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1948 -5.5311 273.4679
REMARK 3 T TENSOR
REMARK 3 T11: 0.4401 T22: 0.5283
REMARK 3 T33: 0.4814 T12: -0.1175
REMARK 3 T13: -0.0832 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 6.8120 L22: 7.9311
REMARK 3 L33: 8.3936 L12: 2.2507
REMARK 3 L13: -0.4512 L23: 0.6088
REMARK 3 S TENSOR
REMARK 3 S11: 0.5891 S12: -0.6931 S13: 0.2244
REMARK 3 S21: 0.6475 S22: -0.5039 S23: 0.0996
REMARK 3 S31: 0.0339 S32: 0.3242 S33: -0.0310
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 73 THROUGH 108 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2736 14.7059 277.7956
REMARK 3 T TENSOR
REMARK 3 T11: 0.3955 T22: 0.4447
REMARK 3 T33: 0.4047 T12: -0.0978
REMARK 3 T13: -0.0270 T23: -0.0692
REMARK 3 L TENSOR
REMARK 3 L11: 7.7411 L22: 8.5970
REMARK 3 L33: 1.1129 L12: 8.2351
REMARK 3 L13: -2.3651 L23: -2.3212
REMARK 3 S TENSOR
REMARK 3 S11: -0.2915 S12: 0.5175 S13: -0.1465
REMARK 3 S21: -0.3345 S22: 0.4315 S23: -0.0541
REMARK 3 S31: 0.3566 S32: -0.1832 S33: -0.0267
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 109 THROUGH 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.2933 -7.8680 262.5639
REMARK 3 T TENSOR
REMARK 3 T11: 0.4761 T22: 0.6685
REMARK 3 T33: 0.4695 T12: 0.0039
REMARK 3 T13: -0.0023 T23: -0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 3.0177 L22: 10.0559
REMARK 3 L33: 3.0407 L12: 3.0815
REMARK 3 L13: 3.7932 L23: -0.1119
REMARK 3 S TENSOR
REMARK 3 S11: 0.3927 S12: 1.2172 S13: -0.1870
REMARK 3 S21: -0.3901 S22: 0.0163 S23: -0.3409
REMARK 3 S31: -0.1409 S32: 0.7841 S33: -0.2917
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 109 THROUGH 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.6987 32.5533 266.0448
REMARK 3 T TENSOR
REMARK 3 T11: 0.4158 T22: 0.6317
REMARK 3 T33: 0.3362 T12: -0.0519
REMARK 3 T13: 0.0055 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 8.8859 L22: 10.0045
REMARK 3 L33: 7.3745 L12: 3.6626
REMARK 3 L13: 0.9625 L23: -1.1200
REMARK 3 S TENSOR
REMARK 3 S11: -0.5455 S12: 1.1702 S13: -0.1136
REMARK 3 S21: -0.7784 S22: 0.2502 S23: -0.1591
REMARK 3 S31: 0.0092 S32: -0.3516 S33: 0.1862
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 6OWX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1000241496.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-17
REMARK 200 TEMPERATURE (KELVIN) : 75
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I23
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 2.3843
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15670
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060
REMARK 200 RESOLUTION RANGE LOW (A) : 42.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
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 <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: PHENIX
REMARK 200 STARTING MODEL: 5WNW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22-34% PEG 3000, 70-270 MM ZINC
REMARK 280 ACETATE, AND 0.1 M IMIDAZOLE, PH 8.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 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,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+3/4
REMARK 290 8555 -Y,-X,-Z+1/4
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 126.89000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 63.44500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 190.33500
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 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 126.89000
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 190.33500
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 63.44500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 ZN ZN A 209 LIES ON A SPECIAL POSITION.
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 ASP A 51
REMARK 465 GLN A 52
REMARK 465 MET A 53
REMARK 465 LYS A 54
REMARK 465 ARG A 55
REMARK 465 PRO A 56
REMARK 465 LEU A 123
REMARK 465 THR A 124
REMARK 465 SER B 28
REMARK 465 MET B 53
REMARK 465 LYS B 54
REMARK 465 ARG B 55
REMARK 465 PRO B 56
REMARK 465 LEU B 123
REMARK 465 THR B 124
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 PHE A 29 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 30 CG CD CE NZ
REMARK 470 ASP A 31 CG OD1 OD2
REMARK 470 GLN A 49 CG CD OE1 NE2
REMARK 470 ARG A 50 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 62 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 77 CG CD CE NZ
REMARK 470 GLN A 88 CG CD OE1 NE2
REMARK 470 LYS A 121 CG CD CE NZ
REMARK 470 ARG A 122 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 29 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 30 CG CD CE NZ
REMARK 470 ASP B 31 CG OD1 OD2
REMARK 470 LYS B 39 CG CD CE NZ
REMARK 470 ARG B 43 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 47 CG CD CE NZ
REMARK 470 GLN B 49 CG CD OE1 NE2
REMARK 470 ARG B 50 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 52 CG CD OE1 NE2
REMARK 470 LEU B 58 CG CD1 CD2
REMARK 470 ARG B 61 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 62 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 75 CG CD CE NZ
REMARK 470 GLU B 110 CG CD OE1 OE2
REMARK 470 LYS B 113 CG CD CE NZ
REMARK 470 LYS B 121 CG CD CE NZ
REMARK 470 ARG B 122 CG CD NE CZ NH1 NH2
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 H2 IMD A 214 O HOH A 316 1.17
REMARK 500 ZN ZN A 207 HN1 IMD B 201 1.39
REMARK 500 HZ2 LYS B 77 ZN ZN B 204 1.47
REMARK 500 ZN ZN A 201 HN1 IMD A 215 1.48
REMARK 500 OE2 GLU A 120 ZN ZN A 216 1.64
REMARK 500 OE2 GLU A 44 O HOH A 301 1.79
REMARK 500 OE1 GLN B 40 O HOH B 301 1.97
REMARK 500 C2 IMD A 214 O HOH A 316 2.11
REMARK 500 OE2 GLU A 98 O HOH A 302 2.14
REMARK 500 O HOH A 307 O HOH B 319 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 HZ1 LYS B 90 ZN ZN B 204 8557 1.47
REMARK 500 HZ3 LYS B 90 ZN ZN B 204 8557 1.56
REMARK 500 HN3 IMD A 212 ZN ZN B 203 1565 1.59
REMARK 500 OG SER A 28 OG SER A 28 5557 1.78
REMARK 500 NZ LYS B 77 OE1 GLU B 87 8557 2.10
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 A 43 CG - CD - NE ANGL. DEV. = -18.6 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 PHE A 29 -13.51 -43.15
REMARK 500 LEU B 58 -79.78 -110.02
REMARK 500 ARG B 61 7.45 -64.82
REMARK 500 LYS B 121 51.81 -102.49
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 A 208 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 36 OD1
REMARK 620 2 ASP A 36 OD2 51.1
REMARK 620 3 GLU A 44 OE1 32.6 41.7
REMARK 620 4 GLU A 44 OE2 40.6 42.8 8.0
REMARK 620 5 IMD A 214 N3 148.0 102.9 139.8 135.0
REMARK 620 6 HOH A 301 O 49.2 99.3 74.7 81.1 141.9
REMARK 620 7 HOH A 312 O 93.2 105.0 124.5 132.3 74.6 69.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 59 OE2
REMARK 620 2 IMD A 215 N1 84.2
REMARK 620 3 ASP B 71 OD1 98.2 36.8
REMARK 620 4 ASP B 71 OD2 96.8 34.4 2.5
REMARK 620 5 HOH B 316 O 129.0 124.4 89.7 92.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 207 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 65 ND1
REMARK 620 2 GLU B 120 OE2 89.8
REMARK 620 3 IMD B 201 N1 101.3 123.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 202 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 66 OD1
REMARK 620 2 ASP A 66 OD2 50.3
REMARK 620 3 ASP B 66 OD1 86.9 62.3
REMARK 620 4 ASP B 66 OD2 85.3 59.3 3.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 203 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 66 OD1
REMARK 620 2 IMD A 212 N3 87.9
REMARK 620 3 ASP B 66 OD2 23.4 96.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 203 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 71 OD2
REMARK 620 2 ASP A 74 OD2 103.9
REMARK 620 3 HOH A 319 O 116.2 59.1
REMARK 620 4 HOH A 321 O 97.9 158.1 112.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 205 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 86 OE1
REMARK 620 2 IMD A 213 N3 103.0
REMARK 620 3 GLU B 79 OE2 70.8 166.6
REMARK 620 4 HOH B 313 O 103.7 112.5 80.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 209 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 87 OE2
REMARK 620 2 GLU A 87 OE2 0.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 204 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 74 OD2
REMARK 620 2 LYS B 77 NZ 84.4
REMARK 620 3 GLU B 87 OE1 90.7 76.2
REMARK 620 4 LYS B 90 NZ 93.4 81.9 6.1
REMARK 620 5 HOH B 302 O 85.1 58.0 134.2 139.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 202 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 98 OE2
REMARK 620 2 HOH B 314 O 104.7
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 ZN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 209
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 213
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 214
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 215
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 216
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 205
DBREF 6OWX A 29 124 UNP P77754 SPY_ECOLI 52 147
DBREF 6OWX B 29 124 UNP P77754 SPY_ECOLI 52 147
SEQADV 6OWX SER A 28 UNP P77754 EXPRESSION TAG
SEQADV 6OWX LEU A 96 UNP P77754 HIS 119 ENGINEERED MUTATION
SEQADV 6OWX SER B 28 UNP P77754 EXPRESSION TAG
SEQADV 6OWX LEU B 96 UNP P77754 HIS 119 ENGINEERED MUTATION
SEQRES 1 A 97 SER PHE LYS ASP LEU ASN LEU THR ASP ALA GLN LYS GLN
SEQRES 2 A 97 GLN ILE ARG GLU ILE MET LYS GLY GLN ARG ASP GLN MET
SEQRES 3 A 97 LYS ARG PRO PRO LEU GLU GLU ARG ARG ALA MET HIS ASP
SEQRES 4 A 97 ILE ILE ALA SER ASP THR PHE ASP LYS VAL LYS ALA GLU
SEQRES 5 A 97 ALA GLN ILE ALA LYS MET GLU GLU GLN ARG LYS ALA ASN
SEQRES 6 A 97 MET LEU ALA LEU MET GLU THR GLN ASN LYS ILE TYR ASN
SEQRES 7 A 97 ILE LEU THR PRO GLU GLN LYS LYS GLN PHE ASN ALA ASN
SEQRES 8 A 97 PHE GLU LYS ARG LEU THR
SEQRES 1 B 97 SER PHE LYS ASP LEU ASN LEU THR ASP ALA GLN LYS GLN
SEQRES 2 B 97 GLN ILE ARG GLU ILE MET LYS GLY GLN ARG ASP GLN MET
SEQRES 3 B 97 LYS ARG PRO PRO LEU GLU GLU ARG ARG ALA MET HIS ASP
SEQRES 4 B 97 ILE ILE ALA SER ASP THR PHE ASP LYS VAL LYS ALA GLU
SEQRES 5 B 97 ALA GLN ILE ALA LYS MET GLU GLU GLN ARG LYS ALA ASN
SEQRES 6 B 97 MET LEU ALA LEU MET GLU THR GLN ASN LYS ILE TYR ASN
SEQRES 7 B 97 ILE LEU THR PRO GLU GLN LYS LYS GLN PHE ASN ALA ASN
SEQRES 8 B 97 PHE GLU LYS ARG LEU THR
HET ZN A 201 1
HET ZN A 202 1
HET ZN A 203 1
HET ZN A 204 1
HET ZN A 205 1
HET ZN A 206 1
HET ZN A 207 1
HET ZN A 208 1
HET ZN A 209 1
HET CL A 210 1
HET CL A 211 1
HET IMD A 212 10
HET IMD A 213 9
HET IMD A 214 9
HET IMD A 215 10
HET ZN A 216 1
HET IMD B 201 10
HET ZN B 202 1
HET ZN B 203 1
HET ZN B 204 1
HET IOD B 205 1
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM IMD IMIDAZOLE
HETNAM IOD IODIDE ION
FORMUL 3 ZN 13(ZN 2+)
FORMUL 12 CL 2(CL 1-)
FORMUL 14 IMD 5(C3 H5 N2 1+)
FORMUL 23 IOD I 1-
FORMUL 24 HOH *42(H2 O)
HELIX 1 AA1 THR A 35 GLN A 49 1 15
HELIX 2 AA2 LEU A 58 ALA A 69 1 12
HELIX 3 AA3 ASP A 74 MET A 85 1 12
HELIX 4 AA4 MET A 85 ASN A 105 1 21
HELIX 5 AA5 THR A 108 LYS A 121 1 14
HELIX 6 AA6 THR B 35 GLN B 49 1 15
HELIX 7 AA7 ARG B 61 ALA B 69 1 9
HELIX 8 AA8 ASP B 74 ASN B 105 1 32
HELIX 9 AA9 THR B 108 LYS B 121 1 14
LINK OD1 ASP A 36 ZN ZN A 208 1555 1555 2.66
LINK OD2 ASP A 36 ZN ZN A 208 1555 1555 2.23
LINK OE1 GLU A 44 ZN ZN A 208 1555 5457 2.17
LINK OE2 GLU A 44 ZN ZN A 208 1555 5457 1.99
LINK OE2 GLU A 59 ZN ZN A 201 1555 1555 2.22
LINK ND1 HIS A 65 ZN ZN A 207 1555 1555 2.12
LINK OD1 ASP A 66 ZN ZN A 202 1555 1555 2.60
LINK OD2 ASP A 66 ZN ZN A 202 1555 1555 2.55
LINK OD1 ASP A 66 ZN ZN B 203 1555 1565 2.04
LINK OD2 ASP A 71 ZN ZN A 203 1555 1555 1.96
LINK OD2 ASP A 74 ZN ZN A 203 1555 8667 1.92
LINK OE2 GLU A 79 ZN ZN A 204 1555 1555 2.13
LINK OE1 GLU A 86 ZN ZN A 205 1555 1555 2.01
LINK OE2 GLU A 87 ZN ZN A 209 1555 1555 2.53
LINK OE2 GLU A 87 ZN ZN A 209 1555 8557 2.53
LINK ZN ZN A 201 N1 IMD A 215 1555 1555 2.28
LINK ZN ZN A 201 OD1 ASP B 71 1545 1555 2.57
LINK ZN ZN A 201 OD2 ASP B 71 1545 1555 2.05
LINK ZN ZN A 201 O HOH B 316 1555 1565 2.07
LINK ZN ZN A 202 OD1 ASP B 66 1545 1555 2.24
LINK ZN ZN A 202 OD2 ASP B 66 1545 1555 2.63
LINK ZN ZN A 203 O HOH A 319 1555 8667 2.13
LINK ZN ZN A 203 O HOH A 321 1555 1555 2.56
LINK ZN ZN A 205 N3 IMD A 213 1555 1555 2.12
LINK ZN ZN A 205 OE2 GLU B 79 8557 1555 1.95
LINK ZN ZN A 205 O HOH B 313 1555 8557 1.92
LINK ZN ZN A 206 O HOH A 304 1555 1555 2.24
LINK ZN ZN A 207 OE2 GLU B 120 1555 1555 2.04
LINK ZN ZN A 207 N1 IMD B 201 1555 1555 2.01
LINK ZN ZN A 208 N3 IMD A 214 1555 1555 2.07
LINK ZN ZN A 208 O HOH A 301 1555 5457 2.68
LINK ZN ZN A 208 O HOH A 312 1555 1555 2.50
LINK N3 IMD A 212 ZN ZN B 203 1555 1565 2.45
LINK ZN ZN A 216 ND1 HIS B 65 1555 1555 2.20
LINK OD2 ASP B 66 ZN ZN B 203 1555 1555 2.09
LINK OD2 ASP B 74 ZN ZN B 204 1555 1555 2.00
LINK NZ LYS B 77 ZN ZN B 204 1555 1555 2.33
LINK OE1 GLU B 87 ZN ZN B 204 1555 8557 2.08
LINK NZ LYS B 90 ZN ZN B 204 1555 8557 1.84
LINK OE2 GLU B 98 ZN ZN B 202 1555 1555 2.23
LINK ZN ZN B 202 O HOH B 314 1555 1555 2.27
LINK ZN ZN B 204 O HOH B 302 1555 1555 2.55
SITE 1 AC1 4 GLU A 59 IMD A 215 ASP B 71 HOH B 316
SITE 1 AC2 7 ARG A 62 ASP A 66 IMD A 212 ASP B 66
SITE 2 AC2 7 IMD B 201 ZN B 203 HOH B 318
SITE 1 AC3 4 ASP A 71 ASP A 74 HOH A 319 HOH A 321
SITE 1 AC4 1 GLU A 79
SITE 1 AC5 4 GLU A 86 IMD A 213 GLU B 79 HOH B 313
SITE 1 AC6 3 GLU A 98 HOH A 302 HOH A 304
SITE 1 AC7 4 HIS A 65 CL A 211 GLU B 120 IMD B 201
SITE 1 AC8 5 ASP A 36 GLU A 44 IMD A 214 HOH A 301
SITE 2 AC8 5 HOH A 312
SITE 1 AC9 3 GLU A 87 LYS A 90 HOH A 311
SITE 1 AD1 2 GLU A 120 ZN A 216
SITE 1 AD2 7 ARG A 61 ARG A 62 HIS A 65 ZN A 207
SITE 2 AD2 7 PHE B 119 GLU B 120 IMD B 201
SITE 1 AD3 9 HIS A 65 ASP A 66 GLU A 120 ZN A 202
SITE 2 AD3 9 ZN A 216 HIS B 65 ASP B 66 IMD B 201
SITE 3 AD3 9 ZN B 203
SITE 1 AD4 4 ALA A 83 GLU A 86 ZN A 205 GLU B 79
SITE 1 AD5 9 ASP A 36 GLN A 41 GLU A 44 ZN A 208
SITE 2 AD5 9 HOH A 312 HOH A 316 ASN B 33 THR B 108
SITE 3 AD5 9 GLN B 111
SITE 1 AD6 6 GLU A 59 ZN A 201 GLN B 40 GLU B 44
SITE 2 AD6 6 ASP B 71 HOH B 301
SITE 1 AD7 4 GLU A 120 CL A 210 IMD A 212 HIS B 65
SITE 1 AD8 8 HIS A 65 ZN A 202 ZN A 207 CL A 211
SITE 2 AD8 8 IMD A 212 HIS B 65 ASP B 66 GLU B 120
SITE 1 AD9 3 LYS A 75 GLU B 98 HOH B 314
SITE 1 AE1 5 ASP A 66 ZN A 202 IMD A 212 ARG B 62
SITE 2 AE1 5 ASP B 66
SITE 1 AE2 5 ASP B 74 LYS B 77 GLU B 87 LYS B 90
SITE 2 AE2 5 HOH B 302
SITE 1 AE3 2 PHE B 115 PHE B 119
CRYST1 42.800 42.800 253.780 90.00 90.00 90.00 P 41 2 2 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 0.023364 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023364 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003940 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
