HEADER PROTEIN TRANSPORT 11-MAY-06 2GZH
TITLE CRYSTAL STRUCTURE OF RAB11 IN COMPLEX WITH RAB11-FAMILY
TITLE 2 INTERACTING PROTEIN 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAS-RELATED PROTEIN RAB-11A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: G PROTEIN DOMAIN;
COMPND 5 SYNONYM: RAB-11, YL8;
COMPND 6 EC: 3.6.5.2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: RAB11-FIP2 LONG ISOFORM;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: RAB11-FIP2 RAB-BINDING DOMAIN;
COMPND 13 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: RAB11A;
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_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
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_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PMAL-C2X
KEYWDS RAS-LIKE G PROTEIN FOLD, A-HELICAL COILED COIL, PROTEIN
KEYWDS 2 TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR A.R.KHAN
REVDAT 3 24-FEB-09 2GZH 1 VERSN
REVDAT 2 29-AUG-06 2GZH 1 JRNL
REVDAT 1 15-AUG-06 2GZH 0
JRNL AUTH W.N.JAGOE,A.J.LINDSAY,R.J.READ,A.J.MCCOY,
JRNL AUTH 2 M.W.MCCAFFREY,A.R.KHAN
JRNL TITL CRYSTAL STRUCTURE OF RAB11 IN COMPLEX WITH RAB11
JRNL TITL 2 FAMILY INTERACTING PROTEIN 2.
JRNL REF STRUCTURE V. 14 1273 2006
JRNL REFN ISSN 0969-2126
JRNL PMID 16905101
JRNL DOI 10.1016/J.STR.2006.06.010
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.47 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.47
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 9719
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 492
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) : 2.47
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 684
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2220
REMARK 3 BIN FREE R VALUE SET COUNT : 43
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1809
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 125
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.15000
REMARK 3 B22 (A**2) : 0.15000
REMARK 3 B33 (A**2) : -0.22000
REMARK 3 B12 (A**2) : 0.07000
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): 0.541
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.290
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.204
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.799
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1889 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2555 ; 1.977 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 224 ; 7.096 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 91 ;31.526 ;23.297
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 332 ;18.903 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;21.656 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 290 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1393 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 921 ; 0.256 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1273 ; 0.317 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 160 ; 0.181 ; 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): 92 ; 0.224 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 17 ; 0.192 ; 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): 1152 ; 1.213 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1806 ; 2.146 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 843 ; 2.830 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 749 ; 4.631 ; 4.500
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
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2GZH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-06.
REMARK 100 THE RCSB ID CODE IS RCSB037739.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-DEC-05
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98175
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADSC
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10234
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.470
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 16.000
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.47
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 10.00
REMARK 200 R MERGE FOR SHELL (I) : 0.29700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 15.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM PHOSPHATE BUFFER,
REMARK 280 APPROXIMATELY 0.3M CONCENTRATION, PH 5, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.46667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 74.93333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 74.93333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 37.46667
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 300 REMARK: THE SECOND PART OF THE BIOLOGICAL UNIT IS GENERATED BY
REMARK 300 THE CRYSTALLOGRAPHIC 2-FOLD AXIS, TRANSFORMATION (1,-1,-1).
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 74.93333
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 1
REMARK 465 GLY A 2
REMARK 465 THR A 3
REMARK 465 ARG A 4
REMARK 465 ASP A 5
REMARK 465 GLY B 406
REMARK 465 ALA B 407
REMARK 465 MET B 408
REMARK 465 ALA B 409
REMARK 465 ALA B 410
REMARK 465 LYS B 411
REMARK 465 PHE B 412
REMARK 465 ARG B 413
REMARK 465 ALA B 414
REMARK 465 SER B 415
REMARK 465 ASN B 416
REMARK 465 ILE B 417
REMARK 465 MET B 418
REMARK 465 PRO B 419
REMARK 465 SER B 420
REMARK 465 SER B 421
REMARK 465 SER B 422
REMARK 465 PHE B 423
REMARK 465 HIS B 424
REMARK 465 MET B 425
REMARK 465 SER B 426
REMARK 465 PRO B 427
REMARK 465 THR B 428
REMARK 465 SER B 429
REMARK 465 ASN B 430
REMARK 465 GLU B 431
REMARK 465 ASP B 432
REMARK 465 LEU B 433
REMARK 465 ARG B 434
REMARK 465 LYS B 435
REMARK 465 ILE B 436
REMARK 465 PRO B 437
REMARK 465 ASP B 438
REMARK 465 SER B 439
REMARK 465 ASN B 440
REMARK 465 PRO B 441
REMARK 465 PHE B 442
REMARK 465 ASP B 443
REMARK 465 ALA B 444
REMARK 465 THR B 445
REMARK 465 ALA B 446
REMARK 465 ARG B 504
REMARK 465 LYS B 505
REMARK 465 ALA B 506
REMARK 465 GLY B 507
REMARK 465 LYS B 508
REMARK 465 PHE B 509
REMARK 465 SER B 510
REMARK 465 ASN B 511
REMARK 465 SER B 512
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 TYR A 173 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER B 450 CB OG
REMARK 470 LEU B 451 CB CG CD1 CD2
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 CA GLU A 7 O HOH A 659 0.00
REMARK 500 NH1 ARG A 140 OE1 GLU A 144 1.43
REMARK 500 N GLU A 7 O HOH A 659 1.49
REMARK 500 C GLU A 7 O HOH A 659 1.53
REMARK 500 CB GLU A 7 O HOH A 659 1.55
REMARK 500 CE LYS A 41 O HOH A 548 2.17
REMARK 500 O HOH A 576 O HOH A 629 2.19
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 475 NE - CZ - NH1 ANGL. DEV. = -3.1 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 7 171.15 71.55
REMARK 500 TYR A 8 161.57 164.39
REMARK 500 ASP A 56 -135.21 56.90
REMARK 500 ARG A 72 -77.87 -81.59
REMARK 500 ASP A 114 143.54 -39.29
REMARK 500 LYS A 125 39.91 70.70
REMARK 500 LEU A 128 55.15 -90.85
REMARK 500 SER A 158 -9.38 92.37
REMARK 500 ASN A 160 -0.50 67.60
REMARK 500 ARG B 449 -115.56 -65.86
REMARK 500 SER B 450 -56.13 64.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 950 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 25 OG
REMARK 620 2 THR A 43 OG1 68.8
REMARK 620 3 GTP A 900 O2B 89.4 153.0
REMARK 620 4 GTP A 900 O2G 153.7 93.9 100.1
REMARK 620 5 HOH A 658 O 98.7 98.4 100.5 103.5
REMARK 620 6 HOH A 655 O 80.2 80.4 80.4 77.3 178.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 951 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 648 O
REMARK 620 2 HOH A 657 O 164.5
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 901
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 950
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 951
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP A 900
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GZD RELATED DB: PDB
REMARK 900 SAME COMPLEX IN ORTHORHOMBIC SPACE GROUP
DBREF 2GZH A 2 173 UNP P62491 RB11A_HUMAN 1 172
DBREF 2GZH B 410 512 UNP Q7L804 RFIP2_HUMAN 410 512
SEQADV 2GZH MET A 1 UNP P62491 CLONING ARTIFACT
SEQADV 2GZH LEU A 70 UNP P62491 GLN 69 ENGINEERED
SEQADV 2GZH MSE A 120 UNP P62491 MET 119 MODIFIED RESIDUE
SEQADV 2GZH GLY B 406 UNP Q7L804 CLONING ARTIFACT
SEQADV 2GZH ALA B 407 UNP Q7L804 CLONING ARTIFACT
SEQADV 2GZH MET B 408 UNP Q7L804 CLONING ARTIFACT
SEQADV 2GZH ALA B 409 UNP Q7L804 CLONING ARTIFACT
SEQADV 2GZH MSE B 489 UNP Q7L804 MET 489 MODIFIED RESIDUE
SEQRES 1 A 173 MET GLY THR ARG ASP ASP GLU TYR ASP TYR LEU PHE LYS
SEQRES 2 A 173 VAL VAL LEU ILE GLY ASP SER GLY VAL GLY LYS SER ASN
SEQRES 3 A 173 LEU LEU SER ARG PHE THR ARG ASN GLU PHE ASN LEU GLU
SEQRES 4 A 173 SER LYS SER THR ILE GLY VAL GLU PHE ALA THR ARG SER
SEQRES 5 A 173 ILE GLN VAL ASP GLY LYS THR ILE LYS ALA GLN ILE TRP
SEQRES 6 A 173 ASP THR ALA GLY LEU GLU ARG TYR ARG ALA ILE THR SER
SEQRES 7 A 173 ALA TYR TYR ARG GLY ALA VAL GLY ALA LEU LEU VAL TYR
SEQRES 8 A 173 ASP ILE ALA LYS HIS LEU THR TYR GLU ASN VAL GLU ARG
SEQRES 9 A 173 TRP LEU LYS GLU LEU ARG ASP HIS ALA ASP SER ASN ILE
SEQRES 10 A 173 VAL ILE MSE LEU VAL GLY ASN LYS SER ASP LEU ARG HIS
SEQRES 11 A 173 LEU ARG ALA VAL PRO THR ASP GLU ALA ARG ALA PHE ALA
SEQRES 12 A 173 GLU LYS ASN GLY LEU SER PHE ILE GLU THR SER ALA LEU
SEQRES 13 A 173 ASP SER THR ASN VAL GLU ALA ALA PHE GLN THR ILE LEU
SEQRES 14 A 173 THR GLU ILE TYR
SEQRES 1 B 107 GLY ALA MET ALA ALA LYS PHE ARG ALA SER ASN ILE MET
SEQRES 2 B 107 PRO SER SER SER PHE HIS MET SER PRO THR SER ASN GLU
SEQRES 3 B 107 ASP LEU ARG LYS ILE PRO ASP SER ASN PRO PHE ASP ALA
SEQRES 4 B 107 THR ALA GLY TYR ARG SER LEU THR TYR GLU GLU VAL LEU
SEQRES 5 B 107 GLN GLU LEU VAL LYS HIS LYS GLU LEU LEU ARG ARG LYS
SEQRES 6 B 107 ASP THR HIS ILE ARG GLU LEU GLU ASP TYR ILE ASP ASN
SEQRES 7 B 107 LEU LEU VAL ARG VAL MSE GLU GLU THR PRO SER ILE LEU
SEQRES 8 B 107 ARG VAL PRO TYR GLU PRO SER ARG LYS ALA GLY LYS PHE
SEQRES 9 B 107 SER ASN SER
MODRES 2GZH MSE A 120 MET SELENOMETHIONINE
MODRES 2GZH MSE B 489 MET SELENOMETHIONINE
HET MSE A 120 8
HET MSE B 489 8
HET PO4 A 901 5
HET MG A 950 1
HET MG A 951 1
HET GTP A 900 32
HETNAM MSE SELENOMETHIONINE
HETNAM PO4 PHOSPHATE ION
HETNAM MG MAGNESIUM ION
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
FORMUL 1 MSE 2(C5 H11 N O2 SE)
FORMUL 3 PO4 O4 P 3-
FORMUL 4 MG 2(MG 2+)
FORMUL 6 GTP C10 H16 N5 O14 P3
FORMUL 7 HOH *125(H2 O)
HELIX 1 1 GLY A 23 ASN A 34 1 12
HELIX 2 2 ILE A 76 ARG A 82 1 7
HELIX 3 3 LYS A 95 ASN A 101 1 7
HELIX 4 4 ASN A 101 ALA A 113 1 13
HELIX 5 5 LEU A 128 ARG A 132 5 5
HELIX 6 6 PRO A 135 ASN A 146 1 12
HELIX 7 7 ASN A 160 GLU A 171 1 12
HELIX 8 8 THR B 452 THR B 492 1 41
HELIX 9 9 PRO B 493 ARG B 497 5 5
SHEET 1 A 6 VAL A 46 VAL A 55 0
SHEET 2 A 6 LYS A 58 THR A 67 -1 O ALA A 62 N ARG A 51
SHEET 3 A 6 TYR A 10 ILE A 17 1 N PHE A 12 O GLN A 63
SHEET 4 A 6 GLY A 86 ASP A 92 1 O VAL A 90 N ILE A 17
SHEET 5 A 6 VAL A 118 ASN A 124 1 O MSE A 120 N LEU A 89
SHEET 6 A 6 SER A 149 GLU A 152 1 O SER A 149 N LEU A 121
LINK MG MG A 950 OG SER A 25 1555 1555 2.18
LINK MG MG A 950 OG1 THR A 43 1555 1555 2.18
LINK MG MG A 950 O2B GTP A 900 1555 1555 2.16
LINK MG MG A 950 O2G GTP A 900 1555 1555 2.18
LINK C ILE A 119 N MSE A 120 1555 1555 1.32
LINK C MSE A 120 N LEU A 121 1555 1555 1.33
LINK MG MG A 950 O HOH A 658 1555 1555 2.10
LINK MG MG A 950 O HOH A 655 1555 1555 2.23
LINK MG MG A 951 O HOH A 648 1555 1555 2.90
LINK MG MG A 951 O HOH A 657 1555 1555 2.10
LINK C VAL B 488 N MSE B 489 1555 1555 1.32
LINK C MSE B 489 N GLU B 490 1555 1555 1.32
CISPEP 1 VAL B 498 PRO B 499 0 16.72
SITE 1 AC1 7 THR A 167 THR A 170 HOH A 604 LYS B 470
SITE 2 AC1 7 ASP B 471 ILE B 474 ARG B 475
SITE 1 AC2 5 SER A 25 THR A 43 HOH A 655 HOH A 658
SITE 2 AC2 5 GTP A 900
SITE 1 AC3 3 GLU A 108 HOH A 648 HOH A 657
SITE 1 AC4 27 SER A 20 GLY A 21 VAL A 22 GLY A 23
SITE 2 AC4 27 LYS A 24 SER A 25 ASN A 26 PHE A 36
SITE 3 AC4 27 ASN A 37 LEU A 38 SER A 40 SER A 42
SITE 4 AC4 27 THR A 43 GLY A 69 ASN A 124 LYS A 125
SITE 5 AC4 27 ASP A 127 LEU A 128 SER A 154 ALA A 155
SITE 6 AC4 27 LEU A 156 HOH A 565 HOH A 606 HOH A 611
SITE 7 AC4 27 HOH A 655 HOH A 658 MG A 950
CRYST1 64.740 64.740 112.400 90.00 90.00 120.00 P 31 2 1 6
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 0.015446 0.008918 0.000000 0.00000
SCALE2 0.000000 0.017836 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008897 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
