HEADER TRANSFER PROTEIN / STRUCTURAL PROTEIN 05-AUG-14 4U90
TITLE GEPHE IN COMPLEX WITH PEG CROSSLINKED GABA RECEPTOR ALPHA3 SUBUNIT
TITLE 2 DERIVED DIMERIC PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GEPHYRIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GEPHYRIN E DOMAIN, UNP RESIDUES 344-762;
COMPND 5 SYNONYM: PUTATIVE GLYCINE RECEPTOR-TUBULIN LINKER PROTEIN;
COMPND 6 EC: 2.7.7.75,2.10.1.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT ALPHA-3;
COMPND 10 CHAIN: D, E;
COMPND 11 SYNONYM: GABA(A) RECEPTOR SUBUNIT ALPHA-3;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: 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: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 11 ORGANISM_COMMON: RAT;
SOURCE 12 ORGANISM_TAXID: 10116
KEYWDS INHIBITORY SYNAPSE, SCAFFOLDING PROTEIN, GABA TYPE A RECEPTOR,
KEYWDS 2 TRANSFERASE, TRANSFER PROTEIN - STRUCTURAL PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR V.B.KASARAGOD,H.M.MARIC,H.SCHINDELIN
REVDAT 3 20-DEC-23 4U90 1 REMARK ATOM
REVDAT 2 11-FEB-15 4U90 1 JRNL
REVDAT 1 10-DEC-14 4U90 0
JRNL AUTH H.M.MARIC,V.B.KASARAGOD,L.HAUGAARD-KEDSTROM,T.J.HAUSRAT,
JRNL AUTH 2 M.KNEUSSEL,H.SCHINDELIN,K.STRMGAARD
JRNL TITL DESIGN AND SYNTHESIS OF HIGH-AFFINITY DIMERIC INHIBITORS
JRNL TITL 2 TARGETING THE INTERACTIONS BETWEEN GEPHYRIN AND INHIBITORY
JRNL TITL 3 NEUROTRANSMITTER RECEPTORS.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 54 490 2015
JRNL REFN ESSN 1521-3773
JRNL PMID 25413248
JRNL DOI 10.1002/ANIE.201409043
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 32616
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1694
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2392
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.2670
REMARK 3 BIN FREE R VALUE SET COUNT : 107
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3293
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 255
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.13000
REMARK 3 B22 (A**2) : -1.50000
REMARK 3 B33 (A**2) : 1.63000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.151
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.143
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.115
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.411
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3433 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3345 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4676 ; 1.907 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7716 ; 0.933 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 440 ; 6.630 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 143 ;39.854 ;24.406
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 569 ;16.241 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;21.521 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 544 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3861 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 713 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1739 ; 3.173 ; 3.370
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1738 ; 3.172 ; 3.368
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2171 ; 4.440 ; 5.024
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2172 ; 4.440 ; 5.027
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1693 ; 4.296 ; 3.918
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1693 ; 4.286 ; 3.918
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2501 ; 6.199 ; 5.677
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 13691 ; 8.999 ;32.735
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 13692 ; 8.999 ;32.736
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 319 A 736
REMARK 3 ORIGIN FOR THE GROUP (A): 5.5557 128.7595 117.6979
REMARK 3 T TENSOR
REMARK 3 T11: 0.2009 T22: 0.1103
REMARK 3 T33: 0.2257 T12: 0.0111
REMARK 3 T13: -0.0033 T23: 0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 0.1424 L22: 0.0643
REMARK 3 L33: 0.4607 L12: 0.0340
REMARK 3 L13: -0.0508 L23: -0.0793
REMARK 3 S TENSOR
REMARK 3 S11: -0.0173 S12: -0.0125 S13: -0.0107
REMARK 3 S21: -0.0139 S22: -0.0664 S23: 0.0350
REMARK 3 S31: 0.0330 S32: 0.1318 S33: 0.0838
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 368 D 377
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0804 109.3488 106.3605
REMARK 3 T TENSOR
REMARK 3 T11: 0.2704 T22: 0.0783
REMARK 3 T33: 0.2175 T12: 0.0701
REMARK 3 T13: 0.0324 T23: 0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 2.5021 L22: 4.0018
REMARK 3 L33: 2.5746 L12: 2.4633
REMARK 3 L13: -0.0625 L23: -2.0750
REMARK 3 S TENSOR
REMARK 3 S11: 0.1200 S12: 0.0299 S13: 0.0303
REMARK 3 S21: -0.0582 S22: -0.2556 S23: -0.0757
REMARK 3 S31: 0.2453 S32: 0.3474 S33: 0.1356
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 368 E 377
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1954 89.1361 122.4718
REMARK 3 T TENSOR
REMARK 3 T11: 0.3686 T22: 0.1743
REMARK 3 T33: 0.2823 T12: -0.1418
REMARK 3 T13: 0.0424 T23: 0.1349
REMARK 3 L TENSOR
REMARK 3 L11: 10.5619 L22: 16.8073
REMARK 3 L33: 2.8547 L12: -12.2525
REMARK 3 L13: 1.4026 L23: 0.0592
REMARK 3 S TENSOR
REMARK 3 S11: 0.1614 S12: -0.2403 S13: 0.6064
REMARK 3 S21: -0.6986 S22: 0.0589 S23: -1.4144
REMARK 3 S31: -0.4103 S32: 0.1000 S33: -0.2202
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4U90 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000203006.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-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 : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9100
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34354
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 44.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.62300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: 2FU3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE PH 4.5, 20-30 % 2
REMARK 280 -METHYL-2,4-PENTANEDIOL., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
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 44.26900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.62000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 57.20300
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 44.26900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.62000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 57.20300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 44.26900
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.62000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 57.20300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 44.26900
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 49.62000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 57.20300
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, E
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 APPLY THE FOLLOWING TO CHAINS: A, D, E
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 198.48000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 228.81200
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 A1100 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1103 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1104 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 SER A 575
REMARK 465 MET A 576
REMARK 465 GLY A 577
REMARK 465 GLU A 578
REMARK 465 LYS A 579
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 NH2 ARG A 735 O HOH A 901 2.03
REMARK 500 O HOH A 1046 O HOH A 1078 2.10
REMARK 500 OG SER A 563 O HOH A 902 2.15
REMARK 500 N ALA A 451 O6 BU1 A 801 2.17
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 HIS A 591 41.12 71.61
REMARK 500 ASP A 615 13.86 82.47
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 A1146 DISTANCE = 7.27 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4U91 RELATED DB: PDB
REMARK 900 RELATED ID: 4PD0 RELATED DB: PDB
REMARK 900 RELATED ID: 4PD1 RELATED DB: PDB
REMARK 900 RELATED ID: 4TK1 RELATED DB: PDB
REMARK 900 RELATED ID: 4TK2 RELATED DB: PDB
REMARK 900 RELATED ID: 4TK3 RELATED DB: PDB
REMARK 900 RELATED ID: 4TK4 RELATED DB: PDB
DBREF 4U90 A 318 736 UNP Q03555 GEPH_RAT 344 762
DBREF 4U90 D 368 376 UNP P20236 GBRA3_RAT 396 404
DBREF 4U90 E 368 376 UNP P20236 GBRA3_RAT 396 404
SEQADV 4U90 CYS D 377 UNP P20236 EXPRESSION TAG
SEQADV 4U90 CYS E 377 UNP P20236 EXPRESSION TAG
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
SEQRES 1 D 10 PHE ASN ILE VAL GLY THR THR TYR PRO CYS
SEQRES 1 E 10 PHE ASN ILE VAL GLY THR THR TYR PRO CYS
HET BU1 A 801 6
HET 3F8 E 401 22
HETNAM BU1 1,4-BUTANEDIOL
HETNAM 3F8 1,1'-[ETHANE-1,2-DIYLBIS(OXYETHANE-2,1-DIYL)]BIS(1H-
HETNAM 2 3F8 PYRROLE-2,5-DIONE)
FORMUL 4 BU1 C4 H10 O2
FORMUL 5 3F8 C14 H16 N2 O6
FORMUL 6 HOH *255(H2 O)
HELIX 1 AA1 MET A 326 THR A 337 1 12
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 ILE A 588 1 8
HELIX 8 AA8 ASN A 627 GLN A 647 1 21
HELIX 9 AA9 ARG A 699 MET A 703 1 5
SHEET 1 AA1 2 LEU A 323 SER A 325 0
SHEET 2 AA1 2 ARG A 598 PHE A 600 1 O PHE A 600 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 493 N ILE A 345
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 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 0.23
CISPEP 2 LEU A 365 PRO A 366 0 -9.49
CISPEP 3 LYS A 602 PRO A 603 0 -12.99
CRYST1 88.538 99.240 114.406 90.00 90.00 90.00 I 2 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 0.011295 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010077 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008741 0.00000
(ATOM LINES ARE NOT SHOWN.)
END