HEADER SPLICING 31-AUG-09 3IUG
TITLE CRYSTAL STRUCTURE OF THE RHOGAP DOMAIN OF RICS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RHO/CDC42/RAC GTPASE-ACTIVATING PROTEIN RICS;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RHO-GAP DOMAIN: UNP RESIDUES 367-577;
COMPND 5 SYNONYM: P200RHOGAP, P250GAP, RHOGAP INVOLVED IN THE BETA-CATENIN-N-
COMPND 6 CADHERIN AND NMDA RECEPTOR SIGNALING, BRAIN-SPECIFIC RHO GTPASE-
COMPND 7 ACTIVATING PROTEIN, GAB-ASSOCIATED CDC42/RAC GTPASE-ACTIVATING
COMPND 8 PROTEIN, GC-GAP, GTPASE REGULATOR INTERACTING WITH TRKA;
COMPND 9 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: GI:134105571, GRIT, KIAA0712, RICS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-V2R-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28-MHL
KEYWDS STRUCTURAL GENOMICS CONSORTIUM (SGC), GAP, ALTERNATIVE SPLICING, CELL
KEYWDS 2 JUNCTION, CELL MEMBRANE, CELL PROJECTION, CYTOPLASM, ENDOPLASMIC
KEYWDS 3 RETICULUM, ENDOSOME, GOLGI APPARATUS, GTPASE ACTIVATION, MEMBRANE,
KEYWDS 4 PHOSPHOPROTEIN, POSTSYNAPTIC CELL MEMBRANE, SH3 DOMAIN, SYNAPSE,
KEYWDS 5 SPLICING
EXPDTA X-RAY DIFFRACTION
AUTHOR L.NEDYALKOVA,W.TEMPEL,Y.TONG,Y.LI,C.H.ARROWSMITH,A.M.EDWARDS,
AUTHOR 2 C.BOUNTRA,J.WEIGELT,A.BOCHKAREV,H.PARK,STRUCTURAL GENOMICS
AUTHOR 3 CONSORTIUM (SGC)
REVDAT 3 06-SEP-23 3IUG 1 SEQADV
REVDAT 2 01-NOV-17 3IUG 1 REMARK
REVDAT 1 29-SEP-09 3IUG 0
JRNL AUTH L.NEDYALKOVA,W.TEMPEL,Y.TONG,Y.LI,C.H.ARROWSMITH,
JRNL AUTH 2 A.M.EDWARDS,C.BOUNTRA,J.WEIGELT,A.BOCHKAREV,H.PARK
JRNL TITL CRYSTAL STRUCTURE OF THE RHOGAP DOMAIN OF RICS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 45184
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : THIN SHELLS (SFTOOLS)
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.273
REMARK 3 FREE R VALUE TEST SET COUNT : 1027
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) : 1.77
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3183
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.3620
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2919
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 308
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.73400
REMARK 3 B22 (A**2) : -1.45700
REMARK 3 B33 (A**2) : 0.72300
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): 0.117
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.120
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.072
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.220
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3079 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2028 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4216 ; 1.563 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4972 ; 1.004 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 396 ; 5.187 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 144 ;33.357 ;23.819
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 504 ;12.667 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;16.179 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 490 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3443 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 633 ; 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): 1893 ; 1.048 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 751 ; 0.287 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3081 ; 1.838 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1186 ; 2.700 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1120 ; 4.300 ; 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 : MASK BULK SOLVENT
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. U VALUES: REFINED INDIVIDUALLY.
REMARK 4
REMARK 4 3IUG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-09.
REMARK 100 THE DEPOSITION ID IS D_1000054878.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-09
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
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45281
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.70200
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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2OSA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 5000 MME, 0.2M AMMONIUM
REMARK 280 SULFATE, 0.1M MES, 1:100 W/W SUBTILISIN, PH 6.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 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 -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 51.13200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.68450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 51.13200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.68450
REMARK 290 SMTRY3 4 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 300 REMARK: THE BIOLOGICAL UNIT WAS NOT DETERMINED.
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: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 349
REMARK 465 HIS A 350
REMARK 465 HIS A 351
REMARK 465 HIS A 352
REMARK 465 HIS A 353
REMARK 465 HIS A 354
REMARK 465 HIS A 355
REMARK 465 SER A 356
REMARK 465 SER A 357
REMARK 465 GLY A 358
REMARK 465 ARG A 359
REMARK 465 GLU A 360
REMARK 465 ASN A 361
REMARK 465 LEU A 362
REMARK 465 TYR A 363
REMARK 465 PHE A 364
REMARK 465 GLN A 365
REMARK 465 LYS A 533
REMARK 465 GLN A 534
REMARK 465 ILE A 535
REMARK 465 GLU A 536
REMARK 465 SER A 537
REMARK 465 ALA A 538
REMARK 465 CYS A 539
REMARK 465 PHE A 540
REMARK 465 SER A 541
REMARK 465 GLY A 542
REMARK 465 THR A 543
REMARK 465 ALA A 544
REMARK 465 ALA A 545
REMARK 465 PHE A 546
REMARK 465 MET A 547
REMARK 465 GLU A 548
REMARK 465 VAL A 549
REMARK 465 ARG A 550
REMARK 465 ILE A 551
REMARK 465 GLY A 569
REMARK 465 ARG A 570
REMARK 465 ILE A 571
REMARK 465 SER A 572
REMARK 465 MET A 573
REMARK 465 ALA A 574
REMARK 465 MET A 575
REMARK 465 GLN A 576
REMARK 465 GLU A 577
REMARK 465 MET B 349
REMARK 465 HIS B 350
REMARK 465 HIS B 351
REMARK 465 HIS B 352
REMARK 465 HIS B 353
REMARK 465 HIS B 354
REMARK 465 HIS B 355
REMARK 465 SER B 356
REMARK 465 SER B 357
REMARK 465 GLY B 358
REMARK 465 ARG B 359
REMARK 465 GLU B 360
REMARK 465 ASN B 361
REMARK 465 LEU B 362
REMARK 465 TYR B 363
REMARK 465 PHE B 364
REMARK 465 GLN B 365
REMARK 465 GLY B 366
REMARK 465 GLU B 367
REMARK 465 LYS B 533
REMARK 465 GLN B 534
REMARK 465 ILE B 535
REMARK 465 GLU B 536
REMARK 465 SER B 537
REMARK 465 ALA B 538
REMARK 465 CYS B 539
REMARK 465 PHE B 540
REMARK 465 SER B 541
REMARK 465 GLY B 542
REMARK 465 THR B 543
REMARK 465 ALA B 544
REMARK 465 ALA B 545
REMARK 465 PHE B 546
REMARK 465 MET B 547
REMARK 465 GLU B 548
REMARK 465 ARG B 570
REMARK 465 ILE B 571
REMARK 465 SER B 572
REMARK 465 MET B 573
REMARK 465 ALA B 574
REMARK 465 MET B 575
REMARK 465 GLN B 576
REMARK 465 GLU B 577
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 ARG A 417 NE CZ NH1 NH2
REMARK 470 LYS A 432 CG CD CE NZ
REMARK 470 GLU A 433 CG CD OE1 OE2
REMARK 470 GLN A 437 CG CD OE1 NE2
REMARK 470 ARG A 451 NE CZ NH1 NH2
REMARK 470 GLN A 552 CD OE1 NE2
REMARK 470 ARG B 368 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 417 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 425 CG CD OE1 OE2
REMARK 470 HIS B 426 CG ND1 CD2 CE1 NE2
REMARK 470 VAL B 427 CG1 CG2
REMARK 470 LYS B 432 CG CD CE NZ
REMARK 470 GLN B 461 CG CD OE1 NE2
REMARK 470 VAL B 549 CG1 CG2
REMARK 470 ARG B 550 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 551 CG1 CG2 CD1
REMARK 470 GLN B 552 CD OE1 NE2
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 407 NE - CZ - NH1 ANGL. DEV. = 3.4 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 TYR A 406 -13.51 69.14
REMARK 500 THR A 459 146.18 80.89
REMARK 500 TYR B 406 -9.69 67.65
REMARK 500 ASP B 438 75.06 -113.84
REMARK 500 THR B 459 145.30 77.72
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3IUG A 367 577 UNP A7KAX9 RICS_HUMAN 367 577
DBREF 3IUG B 367 577 UNP A7KAX9 RICS_HUMAN 367 577
SEQADV 3IUG MET A 349 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG HIS A 350 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG HIS A 351 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG HIS A 352 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG HIS A 353 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG HIS A 354 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG HIS A 355 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG SER A 356 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG SER A 357 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG GLY A 358 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG ARG A 359 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG GLU A 360 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG ASN A 361 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG LEU A 362 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG TYR A 363 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG PHE A 364 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG GLN A 365 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG GLY A 366 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG MET B 349 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG HIS B 350 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG HIS B 351 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG HIS B 352 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG HIS B 353 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG HIS B 354 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG HIS B 355 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG SER B 356 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG SER B 357 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG GLY B 358 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG ARG B 359 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG GLU B 360 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG ASN B 361 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG LEU B 362 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG TYR B 363 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG PHE B 364 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG GLN B 365 UNP A7KAX9 EXPRESSION TAG
SEQADV 3IUG GLY B 366 UNP A7KAX9 EXPRESSION TAG
SEQRES 1 A 229 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 A 229 LEU TYR PHE GLN GLY GLU ARG VAL PHE GLY CYS ASP LEU
SEQRES 3 A 229 GLY GLU HIS LEU LEU ASN SER GLY PHE GLU VAL PRO GLN
SEQRES 4 A 229 VAL LEU GLN SER CYS THR ALA PHE ILE GLU ARG TYR GLY
SEQRES 5 A 229 ILE VAL ASP GLY ILE TYR ARG LEU SER GLY VAL ALA SER
SEQRES 6 A 229 ASN ILE GLN ARG LEU ARG HIS GLU PHE ASP SER GLU HIS
SEQRES 7 A 229 VAL PRO ASP LEU THR LYS GLU PRO TYR VAL GLN ASP ILE
SEQRES 8 A 229 HIS SER VAL GLY SER LEU CYS LYS LEU TYR PHE ARG GLU
SEQRES 9 A 229 LEU PRO ASN PRO LEU LEU THR TYR GLN LEU TYR GLU LYS
SEQRES 10 A 229 PHE SER ASP ALA VAL SER ALA ALA THR ASP GLU GLU ARG
SEQRES 11 A 229 LEU ILE LYS ILE HIS ASP VAL ILE GLN GLN LEU PRO PRO
SEQRES 12 A 229 PRO HIS TYR ARG THR LEU GLU PHE LEU MET ARG HIS LEU
SEQRES 13 A 229 SER LEU LEU ALA ASP TYR CYS SER ILE THR ASN MET HIS
SEQRES 14 A 229 ALA LYS ASN LEU ALA ILE VAL TRP ALA PRO ASN LEU LEU
SEQRES 15 A 229 ARG SER LYS GLN ILE GLU SER ALA CYS PHE SER GLY THR
SEQRES 16 A 229 ALA ALA PHE MET GLU VAL ARG ILE GLN SER VAL VAL VAL
SEQRES 17 A 229 GLU PHE ILE LEU ASN HIS VAL ASP VAL LEU PHE SER GLY
SEQRES 18 A 229 ARG ILE SER MET ALA MET GLN GLU
SEQRES 1 B 229 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 B 229 LEU TYR PHE GLN GLY GLU ARG VAL PHE GLY CYS ASP LEU
SEQRES 3 B 229 GLY GLU HIS LEU LEU ASN SER GLY PHE GLU VAL PRO GLN
SEQRES 4 B 229 VAL LEU GLN SER CYS THR ALA PHE ILE GLU ARG TYR GLY
SEQRES 5 B 229 ILE VAL ASP GLY ILE TYR ARG LEU SER GLY VAL ALA SER
SEQRES 6 B 229 ASN ILE GLN ARG LEU ARG HIS GLU PHE ASP SER GLU HIS
SEQRES 7 B 229 VAL PRO ASP LEU THR LYS GLU PRO TYR VAL GLN ASP ILE
SEQRES 8 B 229 HIS SER VAL GLY SER LEU CYS LYS LEU TYR PHE ARG GLU
SEQRES 9 B 229 LEU PRO ASN PRO LEU LEU THR TYR GLN LEU TYR GLU LYS
SEQRES 10 B 229 PHE SER ASP ALA VAL SER ALA ALA THR ASP GLU GLU ARG
SEQRES 11 B 229 LEU ILE LYS ILE HIS ASP VAL ILE GLN GLN LEU PRO PRO
SEQRES 12 B 229 PRO HIS TYR ARG THR LEU GLU PHE LEU MET ARG HIS LEU
SEQRES 13 B 229 SER LEU LEU ALA ASP TYR CYS SER ILE THR ASN MET HIS
SEQRES 14 B 229 ALA LYS ASN LEU ALA ILE VAL TRP ALA PRO ASN LEU LEU
SEQRES 15 B 229 ARG SER LYS GLN ILE GLU SER ALA CYS PHE SER GLY THR
SEQRES 16 B 229 ALA ALA PHE MET GLU VAL ARG ILE GLN SER VAL VAL VAL
SEQRES 17 B 229 GLU PHE ILE LEU ASN HIS VAL ASP VAL LEU PHE SER GLY
SEQRES 18 B 229 ARG ILE SER MET ALA MET GLN GLU
HET UNX A 6 1
HET UNX A 8 1
HET UNX B 1 1
HET UNX B 2 1
HET UNX B 3 1
HET UNX B 4 1
HET UNX B 5 1
HET UNX B 7 1
HET UNX B 9 1
HET UNX B 10 1
HET UNX B 11 1
HETNAM UNX UNKNOWN ATOM OR ION
FORMUL 3 UNX 11(X)
FORMUL 14 HOH *308(H2 O)
HELIX 1 1 ASP A 373 GLY A 382 1 10
HELIX 2 2 PRO A 386 GLY A 400 1 15
HELIX 3 3 VAL A 411 SER A 424 1 14
HELIX 4 4 ASP A 438 LEU A 453 1 16
HELIX 5 5 LEU A 462 SER A 471 1 10
HELIX 6 6 THR A 474 GLN A 487 1 14
HELIX 7 7 PRO A 490 ASP A 509 1 20
HELIX 8 8 TYR A 510 ASN A 515 1 6
HELIX 9 9 HIS A 517 LEU A 530 1 14
HELIX 10 10 GLN A 552 HIS A 562 1 11
HELIX 11 11 HIS A 562 PHE A 567 1 6
HELIX 12 12 ASP B 373 GLY B 382 1 10
HELIX 13 13 PRO B 386 GLY B 400 1 15
HELIX 14 14 VAL B 411 SER B 424 1 14
HELIX 15 15 ASP B 438 LEU B 453 1 16
HELIX 16 16 LEU B 462 SER B 471 1 10
HELIX 17 17 THR B 474 GLN B 487 1 14
HELIX 18 18 PRO B 490 TYR B 510 1 21
HELIX 19 19 TYR B 510 ASN B 515 1 6
HELIX 20 20 HIS B 517 LEU B 530 1 14
HELIX 21 21 VAL B 549 HIS B 562 1 14
HELIX 22 22 HIS B 562 PHE B 567 1 6
CISPEP 1 GLU A 433 PRO A 434 0 -0.80
CISPEP 2 GLU B 433 PRO B 434 0 -1.86
CRYST1 102.264 117.369 37.717 90.00 90.00 90.00 P 21 21 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 0.009779 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008520 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026513 0.00000
(ATOM LINES ARE NOT SHOWN.)
END