HEADER PROTEIN BINDING 10-APR-18 6G8W
TITLE CRYSTAL STRUCTURES OF THE SINGLE PDZ DOMAINS FROM GRASP65 AND THEIR
TITLE 2 INTERACTION WITH THE GOLGIN GM130
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GOLGI REASSEMBLY-STACKING PROTEIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GOLGI PERIPHERAL MEMBRANE PROTEIN P65,GOLGI PHOSPHOPROTEIN
COMPND 5 5,GOLPH5,GOLGI REASSEMBLY-STACKING PROTEIN OF 65 KDA,GRASP65;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GORASP1, GOLPH5, GRASP65;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PDZ2 DOMAIN STRUCTURE, GOLGI STACKING, GRASP FAMILY, GOLGINS, GOLGI
KEYWDS 2 APPARATUS, YEAST HOMOLOG OF GRASP65, VESICLE TRANSPORT, PROTEIN
KEYWDS 3 BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR C.M.JURK,Y.ROSKE,U.HEINEMANN
REVDAT 3 17-JAN-24 6G8W 1 LINK
REVDAT 2 06-MAY-20 6G8W 1 JRNL
REVDAT 1 24-APR-19 6G8W 0
JRNL AUTH C.M.JURK,Y.ROSKE,U.HEINEMANN
JRNL TITL CRYSTAL STRUCTURES OF THE SINGLE PDZ DOMAINS FROM GRASP65
JRNL TITL 2 AND THEIR INTERACTION WITH THE GOLGIN GM130
JRNL REF CROATICA CHEMICA ACTA 2018
JRNL REFN ISSN 0011-1643
JRNL DOI 10.5562/CCA3341
REMARK 2
REMARK 2 RESOLUTION. 2.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 10222
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 538
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) : 2.12
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 744
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2930
REMARK 3 BIN FREE R VALUE SET COUNT : 39
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1370
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 94
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.41000
REMARK 3 B22 (A**2) : -1.34000
REMARK 3 B33 (A**2) : -0.45000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.97000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.238
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.195
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.177
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.298
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1433 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1282 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1941 ; 1.979 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2984 ; 1.143 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 179 ; 6.663 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 59 ;34.690 ;23.898
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 211 ;15.222 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;11.986 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 209 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1589 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 285 ; 0.002 ; 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): 716 ; 3.355 ; 3.082
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 715 ; 3.356 ; 3.080
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 889 ; 5.090 ; 4.576
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 890 ; 5.088 ; 4.579
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 716 ; 4.063 ; 3.562
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 716 ; 4.061 ; 3.562
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1051 ; 6.299 ; 5.126
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1567 ; 8.959 ;37.231
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1568 ; 8.957 ;37.249
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 6G8W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009593.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAY-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10762
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.120
REMARK 200 RESOLUTION RANGE LOW (A) : 26.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.7800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.970
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: 3RLE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M NA/K PHOSPHATE PH 8.2, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
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 25.41250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.30650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 25.41250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.30650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 1690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 13.0 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 HOH A 339 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 342 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 407 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 450 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 451 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 ALA A 108
REMARK 465 ILE A 142
REMARK 465 LEU A 143
REMARK 465 GLN A 144
REMARK 465 GLU A 145
REMARK 465 ALA B 108
REMARK 465 SER B 109
REMARK 465 ASP B 140
REMARK 465 GLN B 141
REMARK 465 ILE B 142
REMARK 465 LEU B 143
REMARK 465 GLN B 144
REMARK 465 GLU B 145
REMARK 465 SER B 146
REMARK 465 GLU B 147
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 NE2 HIS A 156 O HOH A 301 2.08
REMARK 500 O HOH B 440 O HOH B 442 2.14
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 OH TYR A 132 OH TYR A 132 2455 1.39
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 ASP A 140 CB - CG - OD1 ANGL. DEV. = 6.2 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 GLU A 110 54.92 -97.01
REMARK 500 LEU A 116 -134.21 -107.20
REMARK 500 TYR A 132 -15.64 63.79
REMARK 500 LEU B 116 -126.68 -103.86
REMARK 500 TYR B 132 -15.69 64.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues EDO B 305 and EDO B
REMARK 800 306
DBREF 6G8W A 108 204 UNP Q9BQQ3 GORS1_HUMAN 108 204
DBREF 6G8W B 108 204 UNP Q9BQQ3 GORS1_HUMAN 108 204
SEQRES 1 A 97 ALA SER GLU GLN VAL TRP HIS VAL LEU ASP VAL GLU PRO
SEQRES 2 A 97 SER SER PRO ALA ALA LEU ALA GLY LEU ARG PRO TYR THR
SEQRES 3 A 97 ASP TYR VAL VAL GLY SER ASP GLN ILE LEU GLN GLU SER
SEQRES 4 A 97 GLU ASP PHE PHE THR LEU ILE GLU SER HIS GLU GLY LYS
SEQRES 5 A 97 PRO LEU LYS LEU MET VAL TYR ASN SER LYS SER ASP SER
SEQRES 6 A 97 CYS ARG GLU VAL THR VAL THR PRO ASN ALA ALA TRP GLY
SEQRES 7 A 97 GLY GLU GLY SER LEU GLY CYS GLY ILE GLY TYR GLY TYR
SEQRES 8 A 97 LEU HIS ARG ILE PRO THR
SEQRES 1 B 97 ALA SER GLU GLN VAL TRP HIS VAL LEU ASP VAL GLU PRO
SEQRES 2 B 97 SER SER PRO ALA ALA LEU ALA GLY LEU ARG PRO TYR THR
SEQRES 3 B 97 ASP TYR VAL VAL GLY SER ASP GLN ILE LEU GLN GLU SER
SEQRES 4 B 97 GLU ASP PHE PHE THR LEU ILE GLU SER HIS GLU GLY LYS
SEQRES 5 B 97 PRO LEU LYS LEU MET VAL TYR ASN SER LYS SER ASP SER
SEQRES 6 B 97 CYS ARG GLU VAL THR VAL THR PRO ASN ALA ALA TRP GLY
SEQRES 7 B 97 GLY GLU GLY SER LEU GLY CYS GLY ILE GLY TYR GLY TYR
SEQRES 8 B 97 LEU HIS ARG ILE PRO THR
HET EDO B 301 4
HET EDO B 302 4
HET EDO B 303 4
HET EDO B 304 4
HET EDO B 305 4
HET EDO B 306 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 6(C2 H6 O2)
FORMUL 9 HOH *94(H2 O)
HELIX 1 AA1 SER A 122 ALA A 127 1 6
HELIX 2 AA2 ASP A 148 HIS A 156 1 9
HELIX 3 AA3 SER B 122 GLY B 128 1 7
HELIX 4 AA4 PHE B 149 HIS B 156 1 8
SHEET 1 AA1 5 SER A 172 VAL A 178 0
SHEET 2 AA1 5 LEU A 161 ASN A 167 -1 N VAL A 165 O ARG A 174
SHEET 3 AA1 5 ASP A 134 SER A 139 -1 N GLY A 138 O MET A 164
SHEET 4 AA1 5 TRP A 113 VAL A 118 -1 N TRP A 113 O VAL A 136
SHEET 5 AA1 5 CYS A 192 TYR A 196 -1 O GLY A 195 N HIS A 114
SHEET 1 AA2 5 SER B 172 VAL B 178 0
SHEET 2 AA2 5 LEU B 161 ASN B 167 -1 N LEU B 163 O VAL B 176
SHEET 3 AA2 5 ASP B 134 GLY B 138 -1 N VAL B 137 O MET B 164
SHEET 4 AA2 5 TRP B 113 VAL B 118 -1 N TRP B 113 O VAL B 136
SHEET 5 AA2 5 CYS B 192 TYR B 196 -1 O GLY B 195 N HIS B 114
LINK C2 EDO B 305 C1 EDO B 306 1555 1555 1.55
SITE 1 AC1 5 VAL A 112 HOH B 402 HOH B 414 HOH B 440
SITE 2 AC1 5 HOH B 442
SITE 1 AC2 6 SER A 121 LYS B 162 LYS B 169 SER B 170
SITE 2 AC2 6 HOH B 409 HOH B 411
SITE 1 AC3 2 EDO B 304 EDO B 305
SITE 1 AC4 4 TYR A 198 EDO B 303 EDO B 305 EDO B 306
SITE 1 AC5 6 TYR A 198 EDO B 303 EDO B 304 HOH B 406
SITE 2 AC5 6 HOH B 410 HOH B 420
CRYST1 50.825 82.613 49.220 90.00 110.82 90.00 C 1 2 1 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 0.019675 0.000000 0.007480 0.00000
SCALE2 0.000000 0.012105 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021736 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
