HEADER RNA BINDING PROTEIN/RNA 18-SEP-16 5GXI
TITLE STRUCTURE OF THE GEMIN5 WD40 DOMAIN IN COMPLEX WITH AAUUUUUGAG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GEM-ASSOCIATED PROTEIN 5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-739;
COMPND 5 SYNONYM: GEMIN5;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: RNA (5'-R(*A*AP*UP*UP*UP*UP*UP*GP*AP*G)-3');
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: U4 (118-127);
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: GEMIN5;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606
KEYWDS SNRNP ASSEMBLY, SNRNA, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS
KEYWDS 2 CONSORTIUM, SGC, RNA BINDING PROTEIN-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.XU,H.HE,Y.LI,A.DONG,C.BOUNTRA,C.H.ARROWSMITH,A.M.EDWARDS,J.MIN,
AUTHOR 2 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 6 29-NOV-23 5GXI 1 REMARK
REVDAT 5 14-DEC-22 5GXI 1 SEQADV
REVDAT 4 09-SEP-20 5GXI 1 TITLE
REVDAT 3 17-OCT-18 5GXI 1 SOURCE
REVDAT 2 04-JAN-17 5GXI 1 JRNL
REVDAT 1 26-OCT-16 5GXI 0
JRNL AUTH C.XU,H.ISHIKAWA,K.IZUMIKAWA,L.LI,H.HE,Y.NOBE,Y.YAMAUCHI,
JRNL AUTH 2 H.M.SHAHJEE,X.-H.WU,Y.-T.YU,T.ISOBE,N.TAKAHASHI,J.MIN
JRNL TITL STRUCTURAL INSIGHTS INTO GEMIN5-GUIDED SELECTION OF
JRNL TITL 2 PRE-SNRNAS FOR SNRNP ASSEMBLY
JRNL REF GENES DEV. V. 30 2376 2016
JRNL REFN ISSN 1549-5477
JRNL PMID 27881600
JRNL DOI 10.1101/GAD.288340.116
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 61867
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3294
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4531
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE SET COUNT : 255
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5150
REMARK 3 NUCLEIC ACID ATOMS : 82
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 381
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : 0.00000
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): 0.119
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.119
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.088
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.017
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5509 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5005 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7556 ; 1.894 ; 1.923
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11552 ; 1.062 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 690 ; 7.187 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 228 ;31.108 ;23.728
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 840 ;12.916 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;16.608 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 845 ; 0.119 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6164 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1275 ; 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): 2695 ; 2.407 ; 2.294
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2694 ; 2.402 ; 2.293
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3366 ; 3.504 ; 3.423
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3367 ; 3.504 ; 3.423
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2814 ; 2.943 ; 2.552
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2815 ; 2.942 ; 2.553
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4174 ; 4.308 ; 3.724
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6333 ; 6.239 ;19.377
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6165 ; 6.163 ;19.106
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 5GXI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1300001646.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-APR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65191
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 28.920
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
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: 3OW8,2HES,3DM0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE, 0.2 M AMMONIUM
REMARK 280 ACETATE, 15% PEG 4000, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 62.26000
REMARK 290 SMTRY3 2 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 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 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 -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 ARG A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 HIS A 199
REMARK 465 GLY A 208
REMARK 465 GLU A 209
REMARK 465 ASP A 210
REMARK 465 CYS A 211
REMARK 465 LEU A 212
REMARK 465 SER A 213
REMARK 465 ILE A 214
REMARK 465 ASN A 215
REMARK 465 GLN A 216
REMARK 465 GLU A 217
REMARK 465 GLU A 218
REMARK 465 THR A 219
REMARK 465 SER A 220
REMARK 465 GLU A 221
REMARK 465 GLU A 222
REMARK 465 ALA A 223
REMARK 465 GLU A 224
REMARK 465 ILE A 225
REMARK 465 THR A 226
REMARK 465 ASN A 227
REMARK 465 GLY A 228
REMARK 465 ASN A 229
REMARK 465 ALA A 230
REMARK 465 VAL A 231
REMARK 465 ALA A 232
REMARK 465 GLN A 233
REMARK 465 ALA A 234
REMARK 465 PRO A 235
REMARK 465 VAL A 236
REMARK 465 THR A 237
REMARK 465 LYS A 238
REMARK 465 GLY A 239
REMARK 465 SER A 257
REMARK 465 ARG A 258
REMARK 465 GLY A 259
REMARK 465 GLY A 274
REMARK 465 GLY A 275
REMARK 465 GLY A 276
REMARK 465 ILE A 277
REMARK 465 ASP A 278
REMARK 465 PRO A 279
REMARK 465 THR A 280
REMARK 465 VAL A 281
REMARK 465 LYS A 282
REMARK 465 LEU A 487
REMARK 465 GLY A 488
REMARK 465 GLY A 489
REMARK 465 GLU A 490
REMARK 465 GLY A 491
REMARK 465 ASP A 492
REMARK 465 ARG A 493
REMARK 465 PRO A 494
REMARK 465 GLY A 723
REMARK 465 LYS A 724
REMARK 465 LYS A 725
REMARK 465 SER A 726
REMARK 465 ILE A 727
REMARK 465 GLU A 728
REMARK 465 LEU A 729
REMARK 465 GLU A 730
REMARK 465 LYS A 731
REMARK 465 LYS A 732
REMARK 465 ARG A 733
REMARK 465 LEU A 734
REMARK 465 SER A 735
REMARK 465 GLN A 736
REMARK 465 PRO A 737
REMARK 465 LYS A 738
REMARK 465 ALA A 739
REMARK 465 A B 118
REMARK 465 U B 124
REMARK 465 G B 125
REMARK 465 A B 126
REMARK 465 G B 127
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 3 CG CD OE1 NE2
REMARK 470 ARG A 120 NH1 NH2
REMARK 470 LYS A 184 CD CE NZ
REMARK 470 ARG A 260 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 271 CG CD CE NZ
REMARK 470 ARG A 272 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 315 CG CD OE1 NE2
REMARK 470 SER A 316 OG
REMARK 470 TRP A 317 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 317 CZ3 CH2
REMARK 470 ARG A 318 CG CD NE CZ NH1 NH2
REMARK 470 SER A 328 OG
REMARK 470 GLU A 329 CG CD OE1 OE2
REMARK 470 LYS A 349 CD CE NZ
REMARK 470 LYS A 413 CD CE NZ
REMARK 470 LYS A 419 CD CE NZ
REMARK 470 LYS A 426 CD CE NZ
REMARK 470 LYS A 438 CE NZ
REMARK 470 LYS A 460 CE NZ
REMARK 470 LYS A 470 CD CE NZ
REMARK 470 TRP A 513 CD2 CE2 CE3 CZ2 CZ3 CH2
REMARK 470 LYS A 514 CG CD CE NZ
REMARK 470 LYS A 569 CE NZ
REMARK 470 GLN A 593 CG CD OE1 NE2
REMARK 470 GLU A 595 CG CD OE1 OE2
REMARK 470 GLU A 623 CG CD OE1 OE2
REMARK 470 GLU A 630 CG CD OE1 OE2
REMARK 470 ARG A 671 NE CZ NH1 NH2
REMARK 470 ARG A 719 NE CZ NH1 NH2
REMARK 470 GLN A 722 CD OE1 NE2
REMARK 470 A B 119 P OP1 OP2 O5'
REMARK 470 U B 123 C5' C4' O4' C3' O3' C2' O2'
REMARK 470 U B 123 C1' N1 C2 O2 N3 C4 O4
REMARK 470 U B 123 C5 C6
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 A 6 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 66 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP A 129 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 252 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 319 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP A 528 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 557 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 652 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 ARG A 33 -117.33 53.46
REMARK 500 ARG A 33 -116.90 53.51
REMARK 500 ARG A 66 128.65 -35.22
REMARK 500 PRO A 76 131.95 -39.29
REMARK 500 ILE A 149 -68.72 -108.12
REMARK 500 GLN A 249 18.55 80.66
REMARK 500 MET A 263 124.42 -176.25
REMARK 500 ARG A 318 3.92 -64.48
REMARK 500 VAL A 425 -74.87 -101.33
REMARK 500 GLN A 576 -51.04 -138.30
REMARK 500 SER A 621 63.23 29.30
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 BME A 823
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5GXH RELATED DB: PDB
REMARK 900 RELATED ID: GEMIN5 RELATED DB: TARGETTRACK
DBREF 5GXI A 1 739 UNP Q8TEQ6 GEMI5_HUMAN 1 739
DBREF 5GXI B 118 127 PDB 5GXI 5GXI 118 127
SEQADV 5GXI MET A -17 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI HIS A -16 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI HIS A -15 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI HIS A -14 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI HIS A -13 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI HIS A -12 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI HIS A -11 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI SER A -10 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI SER A -9 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI GLY A -8 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI ARG A -7 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI GLU A -6 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI ASN A -5 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI LEU A -4 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI TYR A -3 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI PHE A -2 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI GLN A -1 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI GLY A 0 UNP Q8TEQ6 EXPRESSION TAG
SEQADV 5GXI GLN A 682 UNP Q8TEQ6 ARG 682 VARIANT
SEQRES 1 A 757 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 A 757 LEU TYR PHE GLN GLY MET GLY GLN GLU PRO ARG THR LEU
SEQRES 3 A 757 PRO PRO SER PRO ASN TRP TYR CYS ALA ARG CYS SER ASP
SEQRES 4 A 757 ALA VAL PRO GLY GLY LEU PHE GLY PHE ALA ALA ARG THR
SEQRES 5 A 757 SER VAL PHE LEU VAL ARG VAL GLY PRO GLY ALA GLY GLU
SEQRES 6 A 757 SER PRO GLY THR PRO PRO PHE ARG VAL ILE GLY GLU LEU
SEQRES 7 A 757 VAL GLY HIS THR GLU ARG VAL SER GLY PHE THR PHE SER
SEQRES 8 A 757 HIS HIS PRO GLY GLN TYR ASN LEU CYS ALA THR SER SER
SEQRES 9 A 757 ASP ASP GLY THR VAL LYS ILE TRP ASP VAL GLU THR LYS
SEQRES 10 A 757 THR VAL VAL THR GLU HIS ALA LEU HIS GLN HIS THR ILE
SEQRES 11 A 757 SER THR LEU HIS TRP SER PRO ARG VAL LYS ASP LEU ILE
SEQRES 12 A 757 VAL SER GLY ASP GLU LYS GLY VAL VAL PHE CYS TYR TRP
SEQRES 13 A 757 PHE ASN ARG ASN ASP SER GLN HIS LEU PHE ILE GLU PRO
SEQRES 14 A 757 ARG THR ILE PHE CYS LEU THR CYS SER PRO HIS HIS GLU
SEQRES 15 A 757 ASP LEU VAL ALA ILE GLY TYR LYS ASP GLY ILE VAL VAL
SEQRES 16 A 757 ILE ILE ASP ILE SER LYS LYS GLY GLU VAL ILE HIS ARG
SEQRES 17 A 757 LEU ARG GLY HIS ASP ASP GLU ILE HIS SER ILE ALA TRP
SEQRES 18 A 757 CYS PRO LEU PRO GLY GLU ASP CYS LEU SER ILE ASN GLN
SEQRES 19 A 757 GLU GLU THR SER GLU GLU ALA GLU ILE THR ASN GLY ASN
SEQRES 20 A 757 ALA VAL ALA GLN ALA PRO VAL THR LYS GLY CYS TYR LEU
SEQRES 21 A 757 ALA THR GLY SER LYS ASP GLN THR ILE ARG ILE TRP SER
SEQRES 22 A 757 CYS SER ARG GLY ARG GLY VAL MET ILE LEU LYS LEU PRO
SEQRES 23 A 757 PHE LEU LYS ARG ARG GLY GLY GLY ILE ASP PRO THR VAL
SEQRES 24 A 757 LYS GLU ARG LEU TRP LEU THR LEU HIS TRP PRO SER ASN
SEQRES 25 A 757 GLN PRO THR GLN LEU VAL SER SER CYS PHE GLY GLY GLU
SEQRES 26 A 757 LEU LEU GLN TRP ASP LEU THR GLN SER TRP ARG ARG LYS
SEQRES 27 A 757 TYR THR LEU PHE SER ALA SER SER GLU GLY GLN ASN HIS
SEQRES 28 A 757 SER ARG ILE VAL PHE ASN LEU CYS PRO LEU GLN THR GLU
SEQRES 29 A 757 ASP ASP LYS GLN LEU LEU LEU SER THR SER MET ASP ARG
SEQRES 30 A 757 ASP VAL LYS CYS TRP ASP ILE ALA THR LEU GLU CYS SER
SEQRES 31 A 757 TRP THR LEU PRO SER LEU GLY GLY PHE ALA TYR SER LEU
SEQRES 32 A 757 ALA PHE SER SER VAL ASP ILE GLY SER LEU ALA ILE GLY
SEQRES 33 A 757 VAL GLY ASP GLY MET ILE ARG VAL TRP ASN THR LEU SER
SEQRES 34 A 757 ILE LYS ASN ASN TYR ASP VAL LYS ASN PHE TRP GLN GLY
SEQRES 35 A 757 VAL LYS SER LYS VAL THR ALA LEU CYS TRP HIS PRO THR
SEQRES 36 A 757 LYS GLU GLY CYS LEU ALA PHE GLY THR ASP ASP GLY LYS
SEQRES 37 A 757 VAL GLY LEU TYR ASP THR TYR SER ASN LYS PRO PRO GLN
SEQRES 38 A 757 ILE SER SER THR TYR HIS LYS LYS THR VAL TYR THR LEU
SEQRES 39 A 757 ALA TRP GLY PRO PRO VAL PRO PRO MET SER LEU GLY GLY
SEQRES 40 A 757 GLU GLY ASP ARG PRO SER LEU ALA LEU TYR SER CYS GLY
SEQRES 41 A 757 GLY GLU GLY ILE VAL LEU GLN HIS ASN PRO TRP LYS LEU
SEQRES 42 A 757 SER GLY GLU ALA PHE ASP ILE ASN LYS LEU ILE ARG ASP
SEQRES 43 A 757 THR ASN SER ILE LYS TYR LYS LEU PRO VAL HIS THR GLU
SEQRES 44 A 757 ILE SER TRP LYS ALA ASP GLY LYS ILE MET ALA LEU GLY
SEQRES 45 A 757 ASN GLU ASP GLY SER ILE GLU ILE PHE GLN ILE PRO ASN
SEQRES 46 A 757 LEU LYS LEU ILE CYS THR ILE GLN GLN HIS HIS LYS LEU
SEQRES 47 A 757 VAL ASN THR ILE SER TRP HIS HIS GLU HIS GLY SER GLN
SEQRES 48 A 757 PRO GLU LEU SER TYR LEU MET ALA SER GLY SER ASN ASN
SEQRES 49 A 757 ALA VAL ILE TYR VAL HIS ASN LEU LYS THR VAL ILE GLU
SEQRES 50 A 757 SER SER PRO GLU SER PRO VAL THR ILE THR GLU PRO TYR
SEQRES 51 A 757 ARG THR LEU SER GLY HIS THR ALA LYS ILE THR SER VAL
SEQRES 52 A 757 ALA TRP SER PRO HIS HIS ASP GLY ARG LEU VAL SER ALA
SEQRES 53 A 757 SER TYR ASP GLY THR ALA GLN VAL TRP ASP ALA LEU ARG
SEQRES 54 A 757 GLU GLU PRO LEU CYS ASN PHE ARG GLY HIS GLN GLY ARG
SEQRES 55 A 757 LEU LEU CYS VAL ALA TRP SER PRO LEU ASP PRO ASP CYS
SEQRES 56 A 757 ILE TYR SER GLY ALA ASP ASP PHE CYS VAL HIS LYS TRP
SEQRES 57 A 757 LEU THR SER MET GLN ASP HIS SER ARG PRO PRO GLN GLY
SEQRES 58 A 757 LYS LYS SER ILE GLU LEU GLU LYS LYS ARG LEU SER GLN
SEQRES 59 A 757 PRO LYS ALA
SEQRES 1 B 10 A A U U U U U G A G
HET UNX A 801 1
HET UNX A 802 1
HET UNX A 803 1
HET UNX A 804 1
HET UNX A 805 1
HET UNX A 806 1
HET UNX A 807 1
HET UNX A 808 1
HET UNX A 809 1
HET UNX A 810 1
HET UNX A 811 1
HET UNX A 812 1
HET UNX A 813 1
HET UNX A 814 1
HET UNX A 815 1
HET UNX A 816 1
HET UNX A 817 1
HET UNX A 818 1
HET UNX A 819 1
HET UNX A 820 1
HET UNX A 821 1
HET UNX A 822 1
HETNAM UNX UNKNOWN ATOM OR ION
FORMUL 3 UNX 22(X)
FORMUL 25 HOH *381(H2 O)
HELIX 1 AA1 PRO A 43 GLY A 46 5 4
HELIX 2 AA2 PHE A 304 GLY A 306 5 3
HELIX 3 AA3 ILE A 522 SER A 531 1 10
HELIX 4 AA4 GLN A 593 SER A 597 5 5
HELIX 5 AA5 LEU A 614 SER A 621 1 8
HELIX 6 AA6 LEU A 670 GLU A 672 5 3
HELIX 7 AA7 SER A 713 GLN A 715 5 3
SHEET 1 AA1 4 ARG A 6 LEU A 8 0
SHEET 2 AA1 4 VAL A 707 LEU A 711 -1 O VAL A 707 N LEU A 8
SHEET 3 AA1 4 CYS A 697 ALA A 702 -1 N ILE A 698 O TRP A 710
SHEET 4 AA1 4 LEU A 685 TRP A 690 -1 N ALA A 689 O TYR A 699
SHEET 1 AA2 4 SER A 20 VAL A 23 0
SHEET 2 AA2 4 LEU A 27 ALA A 32 -1 O GLY A 29 N ASP A 21
SHEET 3 AA2 4 SER A 35 VAL A 41 -1 O VAL A 39 N PHE A 28
SHEET 4 AA2 4 PHE A 54 LEU A 60 -1 O LEU A 60 N VAL A 36
SHEET 1 AA3 4 VAL A 67 PHE A 72 0
SHEET 2 AA3 4 LEU A 81 SER A 86 -1 O ALA A 83 N THR A 71
SHEET 3 AA3 4 VAL A 91 ASP A 95 -1 O TRP A 94 N CYS A 82
SHEET 4 AA3 4 THR A 100 HIS A 105 -1 O VAL A 102 N ILE A 93
SHEET 1 AA4 4 ILE A 112 TRP A 117 0
SHEET 2 AA4 4 LEU A 124 ASP A 129 -1 O GLY A 128 N SER A 113
SHEET 3 AA4 4 VAL A 133 TRP A 138 -1 O TYR A 137 N ILE A 125
SHEET 4 AA4 4 ASP A 143 PHE A 148 -1 O GLN A 145 N CYS A 136
SHEET 1 AA5 4 ILE A 154 CYS A 159 0
SHEET 2 AA5 4 LEU A 166 TYR A 171 -1 O GLY A 170 N CYS A 156
SHEET 3 AA5 4 VAL A 176 ASP A 180 -1 O ILE A 179 N VAL A 167
SHEET 4 AA5 4 VAL A 187 LEU A 191 -1 O LEU A 191 N VAL A 176
SHEET 1 AA6 4 ILE A 201 TRP A 203 0
SHEET 2 AA6 4 TYR A 241 GLY A 245 -1 O ALA A 243 N ALA A 202
SHEET 3 AA6 4 THR A 250 SER A 255 -1 O TRP A 254 N LEU A 242
SHEET 4 AA6 4 GLY A 261 LYS A 266 -1 O LEU A 265 N ILE A 251
SHEET 1 AA7 4 LEU A 289 HIS A 290 0
SHEET 2 AA7 4 GLN A 298 SER A 302 -1 O VAL A 300 N HIS A 290
SHEET 3 AA7 4 LEU A 308 ASP A 312 -1 O TRP A 311 N LEU A 299
SHEET 4 AA7 4 TYR A 321 LEU A 323 -1 O THR A 322 N GLN A 310
SHEET 1 AA8 4 VAL A 337 GLN A 344 0
SHEET 2 AA8 4 GLN A 350 SER A 356 -1 O LEU A 353 N CYS A 341
SHEET 3 AA8 4 ASP A 360 ASP A 365 -1 O TRP A 364 N LEU A 352
SHEET 4 AA8 4 CYS A 371 PRO A 376 -1 O LEU A 375 N VAL A 361
SHEET 1 AA9 4 ALA A 382 PHE A 387 0
SHEET 2 AA9 4 SER A 394 VAL A 399 -1 O ALA A 396 N ALA A 386
SHEET 3 AA9 4 ILE A 404 ASN A 408 -1 O TRP A 407 N LEU A 395
SHEET 4 AA9 4 VAL A 418 PHE A 421 -1 O PHE A 421 N ILE A 404
SHEET 1 AB1 4 VAL A 429 TRP A 434 0
SHEET 2 AB1 4 CYS A 441 THR A 446 -1 O GLY A 445 N ALA A 431
SHEET 3 AB1 4 VAL A 451 ASP A 455 -1 O TYR A 454 N LEU A 442
SHEET 4 AB1 4 GLN A 463 ILE A 464 -1 O GLN A 463 N LEU A 453
SHEET 1 AB2 4 VAL A 473 GLY A 479 0
SHEET 2 AB2 4 ALA A 497 GLY A 502 -1 O TYR A 499 N ALA A 477
SHEET 3 AB2 4 VAL A 507 HIS A 510 -1 O HIS A 510 N LEU A 498
SHEET 4 AB2 4 PHE A 520 ASP A 521 -1 O PHE A 520 N GLN A 509
SHEET 1 AB3 5 HIS A 539 TRP A 544 0
SHEET 2 AB3 5 ILE A 550 ASN A 555 -1 O GLY A 554 N THR A 540
SHEET 3 AB3 5 ILE A 560 GLN A 564 -1 O PHE A 563 N MET A 551
SHEET 4 AB3 5 LYS A 569 ILE A 574 -1 O ILE A 574 N ILE A 560
SHEET 5 AB3 5 VAL A 626 ILE A 628 1 O ILE A 628 N THR A 573
SHEET 1 AB4 4 VAL A 581 TRP A 586 0
SHEET 2 AB4 4 LEU A 599 SER A 604 -1 O ALA A 601 N SER A 585
SHEET 3 AB4 4 ILE A 609 ASN A 613 -1 O HIS A 612 N MET A 600
SHEET 4 AB4 4 ARG A 633 LEU A 635 -1 O LEU A 635 N ILE A 609
SHEET 1 AB5 4 ILE A 642 TRP A 647 0
SHEET 2 AB5 4 ARG A 654 SER A 659 -1 O ALA A 658 N SER A 644
SHEET 3 AB5 4 ALA A 664 ASP A 668 -1 O TRP A 667 N LEU A 655
SHEET 4 AB5 4 GLU A 673 PHE A 678 -1 O CYS A 676 N VAL A 666
SSBOND 1 CYS A 240 CYS A 256 1555 1555 2.05
CISPEP 1 GLY A 25 GLY A 26 0 -2.15
CISPEP 2 PRO A 483 PRO A 484 0 7.79
CISPEP 3 ILE A 565 PRO A 566 0 8.18
SITE 1 AC1 1 CYS A 441
CRYST1 57.850 124.520 60.600 90.00 116.77 90.00 P 1 21 1 2
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 0.017286 0.000000 0.008722 0.00000
SCALE2 0.000000 0.008031 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018483 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
