HEADER RNA BINDING PROTEIN 14-DEC-04 1Y96
TITLE CRYSTAL STRUCTURE OF THE GEMIN6/GEMIN7 HETERODIMER FROM THE HUMAN SMN
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GEM-ASSOCIATED PROTEIN 6;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: GEMIN6(1-86);
COMPND 5 SYNONYM: GEMIN6, SIP2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: GEM-ASSOCIATED PROTEIN 7;
COMPND 9 CHAIN: B, D;
COMPND 10 FRAGMENT: GEMIN7(47-131);
COMPND 11 SYNONYM: GEMIN7, SIP3;
COMPND 12 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: GEMIN6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGV67;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: GEMIN7;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET24D
KEYWDS SM FOLD, PROTEIN COMPLEX, RNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.MA,J.DOSTIE,G.DREYFUSS,G.D.VAN DUYNE
REVDAT 3 14-FEB-24 1Y96 1 REMARK
REVDAT 2 24-FEB-09 1Y96 1 VERSN
REVDAT 1 21-JUN-05 1Y96 0
JRNL AUTH Y.MA,J.DOSTIE,G.DREYFUSS,G.D.VAN DUYNE
JRNL TITL THE GEMIN6-GEMIN7 HETERODIMER FROM THE SURVIVAL OF MOTOR
JRNL TITL 2 NEURONS COMPLEX HAS AN SM PROTEIN-LIKE STRUCTURE.
JRNL REF STRUCTURE V. 13 883 2005
JRNL REFN ISSN 0969-2126
JRNL PMID 15939020
JRNL DOI 10.1016/J.STR.2005.03.014
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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)) : 5.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 49487
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2516
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) : 2113
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2790
REMARK 3 BIN FREE R VALUE SET COUNT : 116
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2710
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 108
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.09000
REMARK 3 B22 (A**2) : 1.09000
REMARK 3 B33 (A**2) : -2.18000
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): 0.126
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.128
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.090
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.262
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2762 ; 0.019 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2501 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3733 ; 1.283 ; 1.937
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5798 ; 0.790 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 336 ; 5.825 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 418 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3056 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 570 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 495 ; 0.189 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2727 ; 0.242 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1693 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 98 ; 0.160 ; 0.200
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): 12 ; 0.245 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 64 ; 0.280 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.134 ; 0.200
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): 1684 ; 0.804 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2711 ; 1.603 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1078 ; 2.493 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1022 ; 4.338 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 1Y96 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000031273.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUL-03; 24-JUL-03
REMARK 200 TEMPERATURE (KELVIN) : 100; NULL
REMARK 200 PH : 4.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : ALS; ALS
REMARK 200 BEAMLINE : 8.2.1; 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.07810; 1.07810
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111); NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49487
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.002
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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 (%) : 95.6
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: MAD; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, MPD, PH 4.7, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 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 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
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 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 68.00550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 68.00550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 40.75750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 68.00550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 68.00550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.75750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 68.00550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 68.00550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 40.75750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 68.00550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 68.00550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.75750
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 0.00000
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 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 2580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 2610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 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 D 47
REMARK 465 GLN D 48
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET B 73 SD MET B 73 CE -0.682
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 B 57 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG B 57 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP B 98 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP C 14 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP C 52 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP D 98 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Y96 A 1 86 UNP Q8WXD5 GEMI6_HUMAN 1 86
DBREF 1Y96 C 1 86 UNP Q8WXD5 GEMI6_HUMAN 1 86
DBREF 1Y96 B 47 131 UNP Q9H840 GEMI7_HUMAN 47 131
DBREF 1Y96 D 47 131 UNP Q9H840 GEMI7_HUMAN 47 131
SEQRES 1 A 86 MET SER GLU TRP MET LYS LYS GLY PRO LEU GLU TRP GLN
SEQRES 2 A 86 ASP TYR ILE TYR LYS GLU VAL ARG VAL THR ALA SER GLU
SEQRES 3 A 86 LYS ASN GLU TYR LYS GLY TRP VAL LEU THR THR ASP PRO
SEQRES 4 A 86 VAL SER ALA ASN ILE VAL LEU VAL ASN PHE LEU GLU ASP
SEQRES 5 A 86 GLY SER MET SER VAL THR GLY ILE MET GLY HIS ALA VAL
SEQRES 6 A 86 GLN THR VAL GLU THR MET ASN GLU GLY ASP HIS ARG VAL
SEQRES 7 A 86 ARG GLU LYS LEU MET HIS LEU PHE
SEQRES 1 B 85 ALA GLN GLU SER LEU GLU SER GLN GLU GLN ARG ALA ARG
SEQRES 2 B 85 ALA ALA LEU ARG GLU ARG TYR LEU ARG SER LEU LEU ALA
SEQRES 3 B 85 MET VAL GLY HIS GLN VAL SER PHE THR LEU HIS GLU GLY
SEQRES 4 B 85 VAL ARG VAL ALA ALA HIS PHE GLY ALA THR ASP LEU ASP
SEQRES 5 B 85 VAL ALA ASN PHE TYR VAL SER GLN LEU GLN THR PRO ILE
SEQRES 6 B 85 GLY VAL GLN ALA GLU ALA LEU LEU ARG CYS SER ASP ILE
SEQRES 7 B 85 ILE SER TYR THR PHE LYS PRO
SEQRES 1 C 86 MET SER GLU TRP MET LYS LYS GLY PRO LEU GLU TRP GLN
SEQRES 2 C 86 ASP TYR ILE TYR LYS GLU VAL ARG VAL THR ALA SER GLU
SEQRES 3 C 86 LYS ASN GLU TYR LYS GLY TRP VAL LEU THR THR ASP PRO
SEQRES 4 C 86 VAL SER ALA ASN ILE VAL LEU VAL ASN PHE LEU GLU ASP
SEQRES 5 C 86 GLY SER MET SER VAL THR GLY ILE MET GLY HIS ALA VAL
SEQRES 6 C 86 GLN THR VAL GLU THR MET ASN GLU GLY ASP HIS ARG VAL
SEQRES 7 C 86 ARG GLU LYS LEU MET HIS LEU PHE
SEQRES 1 D 85 ALA GLN GLU SER LEU GLU SER GLN GLU GLN ARG ALA ARG
SEQRES 2 D 85 ALA ALA LEU ARG GLU ARG TYR LEU ARG SER LEU LEU ALA
SEQRES 3 D 85 MET VAL GLY HIS GLN VAL SER PHE THR LEU HIS GLU GLY
SEQRES 4 D 85 VAL ARG VAL ALA ALA HIS PHE GLY ALA THR ASP LEU ASP
SEQRES 5 D 85 VAL ALA ASN PHE TYR VAL SER GLN LEU GLN THR PRO ILE
SEQRES 6 D 85 GLY VAL GLN ALA GLU ALA LEU LEU ARG CYS SER ASP ILE
SEQRES 7 D 85 ILE SER TYR THR PHE LYS PRO
FORMUL 5 HOH *108(H2 O)
HELIX 1 1 SER A 2 LYS A 7 1 6
HELIX 2 2 GLY A 8 TYR A 15 1 8
HELIX 3 3 ASP A 75 HIS A 84 1 10
HELIX 4 4 SER B 50 VAL B 74 1 25
HELIX 5 5 GLU C 3 LYS C 7 5 5
HELIX 6 6 GLY C 8 ASP C 14 1 7
HELIX 7 7 ASP C 75 HIS C 84 1 10
HELIX 8 8 SER D 50 MET D 73 1 24
SHEET 1 A10 VAL A 65 ASN A 72 0
SHEET 2 A10 GLU A 19 ALA A 24 -1 N GLU A 19 O MET A 71
SHEET 3 A10 ASN A 28 THR A 37 -1 O GLY A 32 N VAL A 20
SHEET 4 A10 ILE A 44 PHE A 49 -1 O VAL A 47 N TRP A 33
SHEET 5 A10 MET A 55 ILE A 60 -1 O THR A 58 N LEU A 46
SHEET 6 A10 ILE B 124 PHE B 129 -1 O TYR B 127 N GLY A 59
SHEET 7 A10 GLN B 77 LEU B 82 -1 N THR B 81 O ILE B 125
SHEET 8 A10 ARG B 87 THR B 95 -1 O VAL B 88 N PHE B 80
SHEET 9 A10 ASN B 101 LEU B 107 -1 O TYR B 103 N ALA B 94
SHEET 10 A10 GLN B 114 ARG B 120 -1 O LEU B 119 N PHE B 102
SHEET 1 B10 VAL C 65 ASN C 72 0
SHEET 2 B10 GLU C 19 ALA C 24 -1 N THR C 23 O GLN C 66
SHEET 3 B10 ASN C 28 THR C 37 -1 O ASN C 28 N ALA C 24
SHEET 4 B10 ILE C 44 PHE C 49 -1 O VAL C 45 N LEU C 35
SHEET 5 B10 MET C 55 ILE C 60 -1 O THR C 58 N LEU C 46
SHEET 6 B10 ILE D 124 PHE D 129 -1 O TYR D 127 N GLY C 59
SHEET 7 B10 GLN D 77 LEU D 82 -1 N THR D 81 O SER D 126
SHEET 8 B10 ARG D 87 THR D 95 -1 O VAL D 88 N PHE D 80
SHEET 9 B10 ASN D 101 GLN D 108 -1 O TYR D 103 N ALA D 94
SHEET 10 B10 VAL D 113 ARG D 120 -1 O LEU D 119 N PHE D 102
CRYST1 136.011 136.011 81.515 90.00 90.00 90.00 P 42 21 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 0.007352 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007352 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012268 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
