HEADER TRANSFERASE 15-NOV-15 5ERQ
TITLE GEPHYRIN E DOMAIN AT 1.55 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GEPHYRIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 318-736;
COMPND 5 SYNONYM: PUTATIVE GLYCINE RECEPTOR-TUBULIN LINKER PROTEIN;
COMPND 6 EC: 2.7.7.75,2.10.1.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: GPHN, GPH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS MOLYBDENUM COFACTOR, TUNGSTEN COFACTOR, MOCO BIOSYNTHESIS,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.B.KASARAGOD,H.SCHINDELIN
REVDAT 3 10-JAN-24 5ERQ 1 ATOM
REVDAT 2 11-MAY-16 5ERQ 1 JRNL
REVDAT 1 04-MAY-16 5ERQ 0
JRNL AUTH V.B.KASARAGOD,H.SCHINDELIN
JRNL TITL STRUCTURAL FRAMEWORK FOR METAL INCORPORATION DURING
JRNL TITL 2 MOLYBDENUM COFACTOR BIOSYNTHESIS.
JRNL REF STRUCTURE V. 24 782 2016
JRNL REFN ISSN 0969-2126
JRNL PMID 27112598
JRNL DOI 10.1016/J.STR.2016.02.023
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 71069
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3553
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 40.3969 - 4.5302 0.98 2866 144 0.1567 0.1667
REMARK 3 2 4.5302 - 3.5965 1.00 2814 124 0.1159 0.1561
REMARK 3 3 3.5965 - 3.1421 0.99 2762 140 0.1309 0.1791
REMARK 3 4 3.1421 - 2.8549 1.00 2766 142 0.1445 0.2009
REMARK 3 5 2.8549 - 2.6503 1.00 2719 149 0.1459 0.1782
REMARK 3 6 2.6503 - 2.4940 0.99 2753 127 0.1515 0.1877
REMARK 3 7 2.4940 - 2.3692 1.00 2701 169 0.1391 0.1732
REMARK 3 8 2.3692 - 2.2660 0.98 2710 147 0.1398 0.1952
REMARK 3 9 2.2660 - 2.1788 0.99 2690 146 0.1425 0.1473
REMARK 3 10 2.1788 - 2.1036 0.99 2740 125 0.1490 0.1708
REMARK 3 11 2.1036 - 2.0379 0.99 2695 153 0.1444 0.1656
REMARK 3 12 2.0379 - 1.9796 0.98 2692 138 0.1595 0.1634
REMARK 3 13 1.9796 - 1.9275 0.99 2695 136 0.1701 0.2173
REMARK 3 14 1.9275 - 1.8805 0.99 2700 132 0.1731 0.2195
REMARK 3 15 1.8805 - 1.8377 0.99 2665 151 0.1814 0.2057
REMARK 3 16 1.8377 - 1.7986 0.97 2646 130 0.1924 0.2343
REMARK 3 17 1.7986 - 1.7626 0.98 2650 171 0.1902 0.2291
REMARK 3 18 1.7626 - 1.7294 0.98 2687 136 0.2040 0.2257
REMARK 3 19 1.7294 - 1.6985 0.98 2661 139 0.2162 0.2828
REMARK 3 20 1.6985 - 1.6697 0.98 2652 131 0.2289 0.2359
REMARK 3 21 1.6697 - 1.6428 0.98 2663 144 0.2372 0.2429
REMARK 3 22 1.6428 - 1.6175 0.98 2663 132 0.2485 0.3002
REMARK 3 23 1.6175 - 1.5937 0.98 2657 143 0.2517 0.2993
REMARK 3 24 1.5937 - 1.5712 0.98 2658 161 0.2607 0.2474
REMARK 3 25 1.5712 - 1.5500 0.98 2611 143 0.2770 0.2868
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) : 18.530
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 : 0.010 3437
REMARK 3 ANGLE : 1.334 4697
REMARK 3 CHIRALITY : 0.056 546
REMARK 3 PLANARITY : 0.008 626
REMARK 3 DIHEDRAL : 12.710 1326
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 319 THROUGH 349 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8504 130.0945 108.0056
REMARK 3 T TENSOR
REMARK 3 T11: 0.1544 T22: 0.1405
REMARK 3 T33: 0.1583 T12: 0.0471
REMARK 3 T13: -0.0127 T23: 0.0465
REMARK 3 L TENSOR
REMARK 3 L11: 1.8848 L22: 3.5909
REMARK 3 L33: 7.1365 L12: -1.1328
REMARK 3 L13: -1.7874 L23: 4.3054
REMARK 3 S TENSOR
REMARK 3 S11: 0.0327 S12: 0.0402 S13: -0.1156
REMARK 3 S21: -0.1348 S22: 0.1957 S23: -0.2203
REMARK 3 S31: 0.0538 S32: 0.4491 S33: -0.2237
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 350 THROUGH 506 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.3492 131.1712 147.0035
REMARK 3 T TENSOR
REMARK 3 T11: 0.1397 T22: 0.1776
REMARK 3 T33: 0.1608 T12: -0.0198
REMARK 3 T13: -0.0004 T23: 0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 1.0713 L22: 0.3198
REMARK 3 L33: 1.8163 L12: 0.4523
REMARK 3 L13: -1.3569 L23: -0.4921
REMARK 3 S TENSOR
REMARK 3 S11: 0.0953 S12: -0.1810 S13: -0.0481
REMARK 3 S21: 0.0795 S22: -0.1007 S23: 0.0423
REMARK 3 S31: -0.0774 S32: 0.1045 S33: -0.0051
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 507 THROUGH 550 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2585 139.9978 93.4894
REMARK 3 T TENSOR
REMARK 3 T11: 0.1379 T22: 0.1761
REMARK 3 T33: 0.1548 T12: -0.0066
REMARK 3 T13: 0.0105 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.8931 L22: 0.9866
REMARK 3 L33: 3.7739 L12: -0.5467
REMARK 3 L13: 1.6914 L23: -0.8710
REMARK 3 S TENSOR
REMARK 3 S11: -0.0612 S12: 0.1612 S13: 0.0143
REMARK 3 S21: -0.0838 S22: -0.0326 S23: -0.0939
REMARK 3 S31: -0.1364 S32: 0.1754 S33: 0.0924
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 551 THROUGH 580 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4244 140.6559 92.6298
REMARK 3 T TENSOR
REMARK 3 T11: 0.2534 T22: 0.3508
REMARK 3 T33: 0.1938 T12: -0.0303
REMARK 3 T13: 0.0105 T23: 0.0345
REMARK 3 L TENSOR
REMARK 3 L11: 3.4909 L22: 4.3296
REMARK 3 L33: 1.7572 L12: 0.2453
REMARK 3 L13: 1.0974 L23: -1.5244
REMARK 3 S TENSOR
REMARK 3 S11: -0.1757 S12: 0.8871 S13: 0.1628
REMARK 3 S21: -0.7821 S22: 0.1017 S23: -0.1368
REMARK 3 S31: 0.0734 S32: 0.3343 S33: 0.0256
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 581 THROUGH 627 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.4246 133.0930 94.9431
REMARK 3 T TENSOR
REMARK 3 T11: 0.1335 T22: 0.2222
REMARK 3 T33: 0.1613 T12: 0.0234
REMARK 3 T13: 0.0453 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 3.3008 L22: 3.2055
REMARK 3 L33: 3.4478 L12: -0.1112
REMARK 3 L13: 0.2623 L23: 0.3020
REMARK 3 S TENSOR
REMARK 3 S11: 0.0209 S12: 0.3138 S13: 0.0681
REMARK 3 S21: -0.2854 S22: 0.0338 S23: -0.2785
REMARK 3 S31: -0.0259 S32: 0.3745 S33: -0.0205
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 628 THROUGH 686 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.4380 118.6488 104.1133
REMARK 3 T TENSOR
REMARK 3 T11: 0.2125 T22: 0.1450
REMARK 3 T33: 0.2113 T12: 0.0265
REMARK 3 T13: -0.0110 T23: -0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 1.5413 L22: 2.2129
REMARK 3 L33: 0.8245 L12: 1.3999
REMARK 3 L13: 0.3222 L23: -0.0594
REMARK 3 S TENSOR
REMARK 3 S11: -0.0702 S12: 0.0688 S13: -0.1284
REMARK 3 S21: -0.2268 S22: 0.0715 S23: 0.0634
REMARK 3 S31: 0.1973 S32: -0.0193 S33: -0.0087
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 687 THROUGH 712 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5949 117.6357 100.4648
REMARK 3 T TENSOR
REMARK 3 T11: 0.3012 T22: 0.3159
REMARK 3 T33: 0.3474 T12: -0.0267
REMARK 3 T13: -0.0619 T23: 0.0613
REMARK 3 L TENSOR
REMARK 3 L11: 7.8075 L22: 7.0233
REMARK 3 L33: 0.6607 L12: -5.0654
REMARK 3 L13: -1.1700 L23: -0.1300
REMARK 3 S TENSOR
REMARK 3 S11: 0.2268 S12: 0.9667 S13: 0.2141
REMARK 3 S21: -0.6330 S22: 0.0261 S23: 0.9032
REMARK 3 S31: 0.0916 S32: -0.4184 S33: -0.2502
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 713 THROUGH 736 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2337 109.2908 100.0400
REMARK 3 T TENSOR
REMARK 3 T11: 0.3367 T22: 0.1275
REMARK 3 T33: 0.3001 T12: 0.0126
REMARK 3 T13: 0.0455 T23: -0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 3.9849 L22: 2.7550
REMARK 3 L33: 4.3806 L12: 2.0038
REMARK 3 L13: 2.3867 L23: -1.0705
REMARK 3 S TENSOR
REMARK 3 S11: 0.0399 S12: 0.1861 S13: -0.6103
REMARK 3 S21: -0.3883 S22: -0.0396 S23: -0.1147
REMARK 3 S31: 0.5662 S32: 0.0979 S33: 0.0779
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 5ERQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215419.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71703
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 43.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.80800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
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: 4PD0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, 25% MPD, PH 4.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 43.83450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.64350
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 56.86250
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 43.83450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.64350
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 56.86250
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 43.83450
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.64350
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 56.86250
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 43.83450
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 49.64350
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 56.86250
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: 10580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 227.45000
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 HOH A1069 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1284 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1306 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1324 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1334 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1403 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1413 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1417 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 MET A 696
REMARK 465 SER A 697
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 HZ3 LYS A 579 O HOH A 903 1.58
REMARK 500 O HOH A 929 O HOH A 1297 2.10
REMARK 500 O HOH A 1158 O HOH A 1335 2.11
REMARK 500 O HOH A 1286 O HOH A 1394 2.16
REMARK 500 O HOH A 1019 O HOH A 1229 2.17
REMARK 500 O HOH A 930 O HOH A 1253 2.19
REMARK 500 O HOH A 1215 O HOH A 1305 2.19
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 945 O HOH A 1036 3557 2.11
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 SER A 319 102.11 174.49
REMARK 500 GLU A 578 64.96 -64.42
REMARK 500 LYS A 579 -46.18 -149.74
REMARK 500 LYS A 579 -52.10 -149.74
REMARK 500 ASP A 580 43.33 -65.34
REMARK 500 ASP A 580 39.77 -74.41
REMARK 500 HIS A 682 -113.94 40.90
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 A1415 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A1416 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A1417 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A1418 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH A1419 DISTANCE = 6.27 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 812
DBREF 5ERQ A 318 736 UNP Q03555 GEPH_RAT 318 736
SEQRES 1 A 419 MET SER PRO PHE PRO LEU THR SER MET ASP LYS ALA PHE
SEQRES 2 A 419 ILE THR VAL LEU GLU MET THR PRO VAL LEU GLY THR GLU
SEQRES 3 A 419 ILE ILE ASN TYR ARG ASP GLY MET GLY ARG VAL LEU ALA
SEQRES 4 A 419 GLN ASP VAL TYR ALA LYS ASP ASN LEU PRO PRO PHE PRO
SEQRES 5 A 419 ALA SER VAL LYS ASP GLY TYR ALA VAL ARG ALA ALA ASP
SEQRES 6 A 419 GLY PRO GLY ASP ARG PHE ILE ILE GLY GLU SER GLN ALA
SEQRES 7 A 419 GLY GLU GLN PRO THR GLN THR VAL MET PRO GLY GLN VAL
SEQRES 8 A 419 MET ARG VAL THR THR GLY ALA PRO ILE PRO CYS GLY ALA
SEQRES 9 A 419 ASP ALA VAL VAL GLN VAL GLU ASP THR GLU LEU ILE ARG
SEQRES 10 A 419 GLU SER ASP ASP GLY THR GLU GLU LEU GLU VAL ARG ILE
SEQRES 11 A 419 LEU VAL GLN ALA ARG PRO GLY GLN ASP ILE ARG PRO ILE
SEQRES 12 A 419 GLY HIS ASP ILE LYS ARG GLY GLU CYS VAL LEU ALA LYS
SEQRES 13 A 419 GLY THR HIS MET GLY PRO SER GLU ILE GLY LEU LEU ALA
SEQRES 14 A 419 THR VAL GLY VAL THR GLU VAL GLU VAL ASN LYS PHE PRO
SEQRES 15 A 419 VAL VAL ALA VAL MET SER THR GLY ASN GLU LEU LEU ASN
SEQRES 16 A 419 PRO GLU ASP ASP LEU LEU PRO GLY LYS ILE ARG ASP SER
SEQRES 17 A 419 ASN ARG SER THR LEU LEU ALA THR ILE GLN GLU HIS GLY
SEQRES 18 A 419 TYR PRO THR ILE ASN LEU GLY ILE VAL GLY ASP ASN PRO
SEQRES 19 A 419 ASP ASP LEU LEU ASN ALA LEU ASN GLU GLY ILE SER ARG
SEQRES 20 A 419 ALA ASP VAL ILE ILE THR SER GLY GLY VAL SER MET GLY
SEQRES 21 A 419 GLU LYS ASP TYR LEU LYS GLN VAL LEU ASP ILE ASP LEU
SEQRES 22 A 419 HIS ALA GLN ILE HIS PHE GLY ARG VAL PHE MET LYS PRO
SEQRES 23 A 419 GLY LEU PRO THR THR PHE ALA THR LEU ASP ILE ASP GLY
SEQRES 24 A 419 VAL ARG LYS ILE ILE PHE ALA LEU PRO GLY ASN PRO VAL
SEQRES 25 A 419 SER ALA VAL VAL THR CYS ASN LEU PHE VAL VAL PRO ALA
SEQRES 26 A 419 LEU ARG LYS MET GLN GLY ILE LEU ASP PRO ARG PRO THR
SEQRES 27 A 419 ILE ILE LYS ALA ARG LEU SER CYS ASP VAL LYS LEU ASP
SEQRES 28 A 419 PRO ARG PRO GLU TYR HIS ARG CYS ILE LEU THR TRP HIS
SEQRES 29 A 419 HIS GLN GLU PRO LEU PRO TRP ALA GLN SER THR GLY ASN
SEQRES 30 A 419 GLN MET SER SER ARG LEU MET SER MET ARG SER ALA ASN
SEQRES 31 A 419 GLY LEU LEU MET LEU PRO PRO LYS THR GLU GLN TYR VAL
SEQRES 32 A 419 GLU LEU HIS LYS GLY GLU VAL VAL ASP VAL MET VAL ILE
SEQRES 33 A 419 GLY ARG LEU
HET ACT A 801 7
HET ACT A 802 7
HET ACT A 803 7
HET ACT A 804 7
HET ACT A 805 7
HET ACT A 806 7
HET ACT A 807 7
HET ACT A 808 7
HET ACT A 809 7
HET ACT A 810 7
HET MPD A 811 22
HET MPD A 812 22
HETNAM ACT ACETATE ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 2 ACT 10(C2 H3 O2 1-)
FORMUL 12 MPD 2(C6 H14 O2)
FORMUL 14 HOH *519(H2 O)
HELIX 1 AA1 SER A 325 THR A 337 1 13
HELIX 2 AA2 ARG A 348 GLY A 350 5 3
HELIX 3 AA3 ARG A 379 GLY A 383 5 5
HELIX 4 AA4 GLY A 478 GLY A 489 1 12
HELIX 5 AA5 SER A 525 HIS A 537 1 13
HELIX 6 AA6 ASN A 550 ALA A 565 1 16
HELIX 7 AA7 TYR A 581 ASP A 589 1 9
HELIX 8 AA8 ASN A 627 PHE A 638 1 12
HELIX 9 AA9 PHE A 638 GLN A 647 1 10
HELIX 10 AB1 ARG A 699 MET A 703 1 5
SHEET 1 AA1 2 LEU A 323 THR A 324 0
SHEET 2 AA1 2 ARG A 598 VAL A 599 1 O ARG A 598 N THR A 324
SHEET 1 AA2 2 THR A 342 ASN A 346 0
SHEET 2 AA2 2 GLU A 492 ASN A 496 -1 O VAL A 495 N GLU A 343
SHEET 1 AA3 2 VAL A 359 TYR A 360 0
SHEET 2 AA3 2 CYS A 469 LEU A 471 -1 O LEU A 471 N VAL A 359
SHEET 1 AA4 2 ALA A 370 SER A 371 0
SHEET 2 AA4 2 ILE A 457 ARG A 458 -1 O ARG A 458 N ALA A 370
SHEET 1 AA5 6 ALA A 423 GLN A 426 0
SHEET 2 AA5 6 GLY A 375 VAL A 378 -1 N VAL A 378 O ALA A 423
SHEET 3 AA5 6 GLN A 407 VAL A 411 -1 O MET A 409 N ALA A 377
SHEET 4 AA5 6 GLY A 385 SER A 393 1 N SER A 393 O ARG A 410
SHEET 5 AA5 6 GLU A 442 ILE A 447 -1 O ILE A 447 N GLY A 385
SHEET 6 AA5 6 THR A 430 GLU A 435 -1 N GLU A 431 O ARG A 446
SHEET 1 AA6 6 THR A 541 VAL A 547 0
SHEET 2 AA6 6 VAL A 501 THR A 506 1 N SER A 505 O VAL A 547
SHEET 3 AA6 6 VAL A 567 SER A 571 1 O VAL A 567 N ALA A 502
SHEET 4 AA6 6 VAL A 617 LEU A 624 1 O LEU A 624 N THR A 570
SHEET 5 AA6 6 THR A 608 ILE A 614 -1 N LEU A 612 O LYS A 619
SHEET 6 AA6 6 GLN A 593 PHE A 596 -1 N GLN A 593 O THR A 611
SHEET 1 AA7 2 LEU A 510 LEU A 511 0
SHEET 2 AA7 2 ILE A 522 ARG A 523 1 O ILE A 522 N LEU A 511
SHEET 1 AA8 6 ILE A 656 LEU A 661 0
SHEET 2 AA8 6 TRP A 688 SER A 691 1 O ALA A 689 N ARG A 660
SHEET 3 AA8 6 GLU A 672 THR A 679 -1 N THR A 679 O TRP A 688
SHEET 4 AA8 6 GLY A 708 LEU A 712 -1 O LEU A 712 N GLU A 672
SHEET 5 AA8 6 VAL A 727 VAL A 732 -1 O MET A 731 N LEU A 709
SHEET 6 AA8 6 ILE A 656 LEU A 661 -1 N ALA A 659 O VAL A 728
SHEET 1 AA9 2 VAL A 665 LYS A 666 0
SHEET 2 AA9 2 GLU A 721 LEU A 722 -1 O LEU A 722 N VAL A 665
CISPEP 1 SER A 319 PRO A 320 0 -1.65
CISPEP 2 LEU A 365 PRO A 366 0 -9.11
CISPEP 3 LYS A 602 PRO A 603 0 -9.67
SITE 1 AC1 1 PHE A 600
SITE 1 AC2 3 CYS A 469 VAL A 470 SER A 702
SITE 1 AC3 1 HOH A 950
SITE 1 AC4 4 ARG A 564 ASP A 566 LYS A 619 HOH A1019
SITE 1 AC5 4 MET A 336 HOH A1100 HOH A1123 HOH A1232
SITE 1 AC6 1 HOH A1192
SITE 1 AC7 2 ASP A 613 GLY A 616
SITE 1 AC8 3 MPD A 811 HOH A 906 HOH A 974
SITE 1 AC9 4 GLU A 672 HIS A 674 HOH A 913 HOH A1208
SITE 1 AD1 6 SER A 480 PRO A 628 ARG A 675 ACT A 808
SITE 2 AD1 6 HOH A1040 HOH A1070
SITE 1 AD2 4 ILE A 417 PRO A 418 ALA A 421 HOH A1065
CRYST1 87.669 99.287 113.725 90.00 90.00 90.00 I 2 2 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 0.011407 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010072 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008793 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
