HEADER BIOSYNTHETIC PROTEIN,STRUCTURAL PROTEIN 17-APR-14 4PD0
TITLE 1.7 A RESOLUTION STRUCTURE OF GEPHYRIN'S E-DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GEPHYRIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: E-DOMAIN (UNP RESIDUES 350-768);
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: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: GPHN, GPH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS SCAFFOLDING PROTEIN, NEUROTRANSMITTER RECEPTOR ANCHORING PROTEIN,
KEYWDS 2 MOLYBDENUM COFACTOR BIOSYNTHESIS, BIOSYNTHETIC PROTEIN, STRUCTURAL
KEYWDS 3 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR V.B.KASARAGOD,H.M.MARIC,H.SCHINDELIN
REVDAT 7 27-SEP-23 4PD0 1 REMARK
REVDAT 6 08-JAN-20 4PD0 1 REMARK
REVDAT 5 27-SEP-17 4PD0 1 SOURCE REMARK
REVDAT 4 03-DEC-14 4PD0 1 JRNL
REVDAT 3 17-SEP-14 4PD0 1 JRNL
REVDAT 2 03-SEP-14 4PD0 1 JRNL
REVDAT 1 27-AUG-14 4PD0 0
JRNL AUTH H.M.MARIC,V.B.KASARAGOD,H.SCHINDELIN
JRNL TITL MODULATION OF GEPHYRIN-GLYCINE RECEPTOR AFFINITY BY
JRNL TITL 2 MULTIVALENCY.
JRNL REF ACS CHEM.BIOL. V. 9 2554 2014
JRNL REFN ESSN 1554-8937
JRNL PMID 25137389
JRNL DOI 10.1021/CB500303A
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 55170
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2800
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 43.8420 - 4.6129 1.00 2770 154 0.1702 0.1923
REMARK 3 2 4.6129 - 3.6620 1.00 2675 150 0.1337 0.1408
REMARK 3 3 3.6620 - 3.1993 1.00 2666 141 0.1485 0.1724
REMARK 3 4 3.1993 - 2.9068 1.00 2622 141 0.1571 0.1627
REMARK 3 5 2.9068 - 2.6985 1.00 2644 140 0.1593 0.2087
REMARK 3 6 2.6985 - 2.5394 1.00 2607 151 0.1625 0.1673
REMARK 3 7 2.5394 - 2.4123 1.00 2590 141 0.1489 0.1781
REMARK 3 8 2.4123 - 2.3073 1.00 2615 148 0.1431 0.1859
REMARK 3 9 2.3073 - 2.2184 1.00 2614 143 0.1538 0.1931
REMARK 3 10 2.2184 - 2.1419 1.00 2574 151 0.1596 0.2001
REMARK 3 11 2.1419 - 2.0749 1.00 2613 138 0.1563 0.1807
REMARK 3 12 2.0749 - 2.0156 1.00 2595 147 0.1648 0.1903
REMARK 3 13 2.0156 - 1.9625 1.00 2588 146 0.1783 0.2026
REMARK 3 14 1.9625 - 1.9147 1.00 2607 126 0.1789 0.1991
REMARK 3 15 1.9147 - 1.8711 1.00 2589 123 0.2003 0.2540
REMARK 3 16 1.8711 - 1.8313 1.00 2599 135 0.2067 0.2722
REMARK 3 17 1.8313 - 1.7947 1.00 2624 111 0.2177 0.2713
REMARK 3 18 1.7947 - 1.7608 1.00 2590 139 0.2258 0.2452
REMARK 3 19 1.7608 - 1.7294 1.00 2577 143 0.2308 0.2723
REMARK 3 20 1.7294 - 1.7000 1.00 2611 132 0.2341 0.2599
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.890
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 : 0.011 3264
REMARK 3 ANGLE : 1.322 4448
REMARK 3 CHIRALITY : 0.080 520
REMARK 3 PLANARITY : 0.007 588
REMARK 3 DIHEDRAL : 12.626 1249
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 319 THROUGH 349 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1271 30.7893 107.6308
REMARK 3 T TENSOR
REMARK 3 T11: 0.1879 T22: 0.1860
REMARK 3 T33: 0.1968 T12: 0.0602
REMARK 3 T13: -0.0197 T23: 0.0319
REMARK 3 L TENSOR
REMARK 3 L11: 1.8268 L22: 3.3355
REMARK 3 L33: 5.3516 L12: -0.7019
REMARK 3 L13: -1.2758 L23: 3.1679
REMARK 3 S TENSOR
REMARK 3 S11: 0.0692 S12: 0.0510 S13: -0.1482
REMARK 3 S21: -0.2599 S22: 0.1980 S23: -0.3127
REMARK 3 S31: 0.0378 S32: 0.4257 S33: -0.2394
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 350 THROUGH 472 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.6491 30.4972 153.9796
REMARK 3 T TENSOR
REMARK 3 T11: 0.2463 T22: 0.2915
REMARK 3 T33: 0.2553 T12: -0.0407
REMARK 3 T13: 0.0093 T23: 0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 3.2089 L22: 0.5367
REMARK 3 L33: 4.1249 L12: 1.2742
REMARK 3 L13: -3.6185 L23: -1.2443
REMARK 3 S TENSOR
REMARK 3 S11: 0.2052 S12: -0.2970 S13: -0.0697
REMARK 3 S21: 0.1401 S22: -0.1952 S23: 0.0465
REMARK 3 S31: -0.1773 S32: 0.1638 S33: 0.0043
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 473 THROUGH 550 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6889 39.6064 105.5499
REMARK 3 T TENSOR
REMARK 3 T11: 0.1680 T22: 0.1880
REMARK 3 T33: 0.2294 T12: 0.0201
REMARK 3 T13: 0.0105 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.6068 L22: 0.4915
REMARK 3 L33: 7.3204 L12: -0.0009
REMARK 3 L13: 1.1719 L23: -0.8026
REMARK 3 S TENSOR
REMARK 3 S11: -0.0098 S12: 0.1056 S13: -0.0133
REMARK 3 S21: -0.0625 S22: -0.0165 S23: -0.0121
REMARK 3 S31: -0.0963 S32: 0.0234 S33: 0.0532
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 551 THROUGH 627 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0838 36.9477 94.2530
REMARK 3 T TENSOR
REMARK 3 T11: 0.2241 T22: 0.3458
REMARK 3 T33: 0.2275 T12: 0.0234
REMARK 3 T13: 0.0291 T23: 0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 3.4453 L22: 4.7959
REMARK 3 L33: 1.5075 L12: -0.0547
REMARK 3 L13: -0.3244 L23: -0.6618
REMARK 3 S TENSOR
REMARK 3 S11: -0.0341 S12: 0.5790 S13: 0.1686
REMARK 3 S21: -0.6100 S22: 0.0188 S23: -0.2811
REMARK 3 S31: -0.0108 S32: 0.3163 S33: -0.0040
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 628 THROUGH 686 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.5057 19.6739 104.0162
REMARK 3 T TENSOR
REMARK 3 T11: 0.2610 T22: 0.1679
REMARK 3 T33: 0.2388 T12: 0.0400
REMARK 3 T13: -0.0135 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 2.0607 L22: 2.9210
REMARK 3 L33: 1.3131 L12: 1.8006
REMARK 3 L13: 0.0949 L23: -0.2384
REMARK 3 S TENSOR
REMARK 3 S11: -0.1030 S12: 0.1122 S13: -0.1454
REMARK 3 S21: -0.2443 S22: 0.1016 S23: 0.0808
REMARK 3 S31: 0.3266 S32: -0.0468 S33: -0.0083
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 687 THROUGH 712 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2029 18.8355 100.4723
REMARK 3 T TENSOR
REMARK 3 T11: 0.3829 T22: 0.3942
REMARK 3 T33: 0.4881 T12: -0.0281
REMARK 3 T13: -0.1137 T23: 0.0683
REMARK 3 L TENSOR
REMARK 3 L11: 5.9233 L22: 5.0263
REMARK 3 L33: 2.7493 L12: -3.0106
REMARK 3 L13: -2.0061 L23: 0.9318
REMARK 3 S TENSOR
REMARK 3 S11: 0.1901 S12: 1.2673 S13: 0.3651
REMARK 3 S21: -0.8957 S22: -0.0557 S23: 1.1699
REMARK 3 S31: 0.0296 S32: -0.6296 S33: -0.0674
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 713 THROUGH 736 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6946 9.6499 99.5824
REMARK 3 T TENSOR
REMARK 3 T11: 0.3822 T22: 0.1924
REMARK 3 T33: 0.3735 T12: 0.0357
REMARK 3 T13: 0.0579 T23: -0.0298
REMARK 3 L TENSOR
REMARK 3 L11: 3.9794 L22: 2.9751
REMARK 3 L33: 4.3878 L12: 1.7941
REMARK 3 L13: 2.0667 L23: -1.4127
REMARK 3 S TENSOR
REMARK 3 S11: 0.0714 S12: 0.3437 S13: -0.6642
REMARK 3 S21: -0.4022 S22: -0.0261 S23: -0.2494
REMARK 3 S31: 0.6482 S32: 0.1625 S33: -0.0010
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 4PD0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000201165.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
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) : 0.9198
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55179
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 43.830
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.00
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: NULL
REMARK 200 STARTING MODEL: 2FU3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM-CITRATE, PH 4.5, 28-34% 2
REMARK 280 -METHYL-2,4-PENTANEDIOL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 43.82750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.00400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 56.84750
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 43.82750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.00400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 56.84750
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 43.82750
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.00400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 56.84750
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 43.82750
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.00400
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 56.84750
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 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR
REMARK 300 CYCLIC POINT SYMMETRY (SCHOENFLIES SYMBOL = C2).
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: 6120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 227.39000
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 A 824 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 934 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 936 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1084 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 318
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 HE22 GLN A 398 O HOH A 1126 1.38
REMARK 500 HZ3 LYS A 362 O HOH A 1071 1.53
REMARK 500 O HOH A 1093 O HOH A 1125 2.11
REMARK 500 O HOH A 1024 O HOH A 1098 2.19
REMARK 500 O HOH A 866 O HOH A 1067 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 814 O HOH A 823 3557 2.04
REMARK 500 O HOH A 903 O HOH A 946 8557 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 GLU A 578 -20.48 -30.28
REMARK 500 LYS A 579 -147.22 -96.22
REMARK 500 HIS A 682 -109.42 36.22
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 A1084 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH A1108 DISTANCE = 6.15 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FU3 RELATED DB: PDB
REMARK 900 RELATED ID: 4PD1 RELATED DB: PDB
DBREF 4PD0 A 318 736 UNP Q03555 GEPH_RAT 350 768
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
FORMUL 2 HOH *329(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 ASP A 580 ASP A 589 1 10
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 ARG A 704 1 6
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 TYR A 376 O VAL A 425
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 ILE A 569 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 0.36
CISPEP 2 LEU A 365 PRO A 366 0 -7.28
CISPEP 3 LYS A 602 PRO A 603 0 -7.87
CRYST1 87.655 100.008 113.695 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 0.011408 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009999 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008795 0.00000
(ATOM LINES ARE NOT SHOWN.)
END