HEADER ANTIVIRAL PROTEIN/HYDROLASE 13-MAR-14 4P4T
TITLE GDP-BOUND STALKLESS-MXA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERFERON-INDUCED GTP-BINDING PROTEIN MX1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 37-366 AND 637-662 VIA LINKER GSGS;
COMPND 5 SYNONYM: INTERFERON-INDUCED PROTEIN P78,IFI-78K,INTERFERON-REGULATED
COMPND 6 RESISTANCE GTP-BINDING PROTEIN MXA,MYXOMA RESISTANCE PROTEIN 1,
COMPND 7 MYXOVIRUS RESISTANCE PROTEIN 1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MX1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GTPASE, DYNAMIN-RELATED PROTEIN, ANTIVIRAL, MECHANO-ENZYME,
KEYWDS 2 HYDROLASE, GTP-BINDING PROTEIN, ANTIVIRAL PROTEIN-HYDROLASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.L.RENNIE,S.A.MCKELVIE,E.M.BULLOCH,R.L.KINGSTON
REVDAT 4 27-SEP-23 4P4T 1 REMARK
REVDAT 3 20-JUL-16 4P4T 1 REMARK
REVDAT 2 05-NOV-14 4P4T 1 HEADER COMPND
REVDAT 1 22-OCT-14 4P4T 0
JRNL AUTH M.L.RENNIE,S.A.MCKELVIE,E.M.BULLOCH,R.L.KINGSTON
JRNL TITL TRANSIENT DIMERIZATION OF HUMAN MXA PROMOTES GTP HYDROLYSIS,
JRNL TITL 2 RESULTING IN A MECHANICAL POWER STROKE.
JRNL REF STRUCTURE V. 22 1433 2014
JRNL REFN ISSN 0969-2126
JRNL PMID 25295396
JRNL DOI 10.1016/J.STR.2014.08.015
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 16884
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) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 890
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 28
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 REFLECTION IN BIN (WORKING SET) : 877
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.25
REMARK 3 BIN R VALUE (WORKING SET) : 0.3040
REMARK 3 BIN FREE R VALUE SET COUNT : 45
REMARK 3 BIN FREE R VALUE : 0.3330
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2641
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 87
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.38000
REMARK 3 B22 (A**2) : -0.46000
REMARK 3 B33 (A**2) : -0.92000
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): 0.353
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.241
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.224
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.641
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2733 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3698 ; 1.128 ; 2.013
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 337 ; 4.901 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 120 ;36.058 ;24.833
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 529 ;15.681 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;15.187 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 437 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1971 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1342 ; 1.016 ; 2.818
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1672 ; 1.782 ; 4.214
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1389 ; 1.200 ; 3.067
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4146 ; 5.744 ;24.113
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 44 A 662
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0046 -0.3062 80.0314
REMARK 3 T TENSOR
REMARK 3 T11: 0.1418 T22: 0.1466
REMARK 3 T33: 0.0577 T12: -0.1079
REMARK 3 T13: -0.0007 T23: 0.0263
REMARK 3 L TENSOR
REMARK 3 L11: 1.4196 L22: 4.2695
REMARK 3 L33: 2.4280 L12: -0.5480
REMARK 3 L13: -0.4959 L23: 1.6372
REMARK 3 S TENSOR
REMARK 3 S11: 0.0065 S12: -0.0813 S13: -0.0790
REMARK 3 S21: -0.2993 S22: 0.1313 S23: -0.3941
REMARK 3 S31: 0.0659 S32: 0.2074 S33: -0.1379
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: NULL
REMARK 4
REMARK 4 4P4T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAR-14.
REMARK 100 THE DEPOSITION ID IS D_1000200358.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.1
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17794
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 32.050
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 4P4U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0-2.5M AMMONIUM SULFATE, 0.2M
REMARK 280 AMPSO/KOH PH 9.1, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-Z+1/2
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 23.51000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 106.16500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.79500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 106.16500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.51000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.79500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 23.51000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 38.79500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 106.16500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 38.79500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 23.51000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 106.16500
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: 4970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 38.79500
REMARK 350 BIOMT3 2 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 819 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 821 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 37
REMARK 465 GLU A 38
REMARK 465 ASN A 39
REMARK 465 ASN A 40
REMARK 465 LEU A 41
REMARK 465 SER A 42
REMARK 465 SER A 43
REMARK 465 GLY A 98
REMARK 465 SER A 99
REMARK 465 GLY A 100
REMARK 465 ILE A 101
REMARK 465 VAL A 102
REMARK 465 THR A 103
REMARK 465 GLY A 154
REMARK 465 MET A 155
REMARK 465 ASP A 629
REMARK 465 ILE A 630
REMARK 465 PRO A 631
REMARK 465 GLU A 632
REMARK 465 GLY A 633
REMARK 465 SER A 634
REMARK 465 GLY A 635
REMARK 465 SER A 636
REMARK 465 SER A 637
REMARK 465 ASP A 638
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 LYS A 639 CG CD CE NZ
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 ASN A 116 -134.15 -81.57
REMARK 500 GLN A 127 -127.09 51.61
REMARK 500 ARG A 241 49.92 -141.06
REMARK 500 ASN A 266 33.98 70.44
REMARK 500 VAL A 268 -63.45 -106.06
REMARK 500 THR A 319 146.83 84.07
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 GDP A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 704
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4P4U RELATED DB: PDB
REMARK 900 RELATED ID: 4P4S RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CHIMERA PROTEIN IS STALKLESS-MXA MADE OF UNP RESIDUES 37-366 AND
REMARK 999 637-662 VIA LINKER GSGS
DBREF 4P4T A 37 632 UNP P20591 MX1_HUMAN 37 366
DBREF 4P4T A 637 662 UNP P20591 MX1_HUMAN 637 662
SEQADV 4P4T SER A 42 UNP P20591 CYS 42 ENGINEERED MUTATION
SEQADV 4P4T SER A 322 UNP P20591 CYS 322 ENGINEERED MUTATION
SEQADV 4P4T SER A 336 UNP P20591 CYS 336 ENGINEERED MUTATION
SEQADV 4P4T GLY A 633 UNP P20591 LINKER
SEQADV 4P4T SER A 634 UNP P20591 LINKER
SEQADV 4P4T GLY A 635 UNP P20591 LINKER
SEQADV 4P4T SER A 636 UNP P20591 LINKER
SEQRES 1 A 360 ALA GLU ASN ASN LEU SER SER GLN TYR GLU GLU LYS VAL
SEQRES 2 A 360 ARG PRO CYS ILE ASP LEU ILE ASP SER LEU ARG ALA LEU
SEQRES 3 A 360 GLY VAL GLU GLN ASP LEU ALA LEU PRO ALA ILE ALA VAL
SEQRES 4 A 360 ILE GLY ASP GLN SER SER GLY LYS SER SER VAL LEU GLU
SEQRES 5 A 360 ALA LEU SER GLY VAL ALA LEU PRO ARG GLY SER GLY ILE
SEQRES 6 A 360 VAL THR ARG CYS PRO LEU VAL LEU LYS LEU LYS LYS LEU
SEQRES 7 A 360 VAL ASN GLU ASP LYS TRP ARG GLY LYS VAL SER TYR GLN
SEQRES 8 A 360 ASP TYR GLU ILE GLU ILE SER ASP ALA SER GLU VAL GLU
SEQRES 9 A 360 LYS GLU ILE ASN LYS ALA GLN ASN ALA ILE ALA GLY GLU
SEQRES 10 A 360 GLY MET GLY ILE SER HIS GLU LEU ILE THR LEU GLU ILE
SEQRES 11 A 360 SER SER ARG ASP VAL PRO ASP LEU THR LEU ILE ASP LEU
SEQRES 12 A 360 PRO GLY ILE THR ARG VAL ALA VAL GLY ASN GLN PRO ALA
SEQRES 13 A 360 ASP ILE GLY TYR LYS ILE LYS THR LEU ILE LYS LYS TYR
SEQRES 14 A 360 ILE GLN ARG GLN GLU THR ILE SER LEU VAL VAL VAL PRO
SEQRES 15 A 360 SER ASN VAL ASP ILE ALA THR THR GLU ALA LEU SER MET
SEQRES 16 A 360 ALA GLN GLU VAL ASP PRO GLU GLY ASP ARG THR ILE GLY
SEQRES 17 A 360 ILE LEU THR LYS PRO ASP LEU VAL ASP LYS GLY THR GLU
SEQRES 18 A 360 ASP LYS VAL VAL ASP VAL VAL ARG ASN LEU VAL PHE HIS
SEQRES 19 A 360 LEU LYS LYS GLY TYR MET ILE VAL LYS CYS ARG GLY GLN
SEQRES 20 A 360 GLN GLU ILE GLN ASP GLN LEU SER LEU SER GLU ALA LEU
SEQRES 21 A 360 GLN ARG GLU LYS ILE PHE PHE GLU ASN HIS PRO TYR PHE
SEQRES 22 A 360 ARG ASP LEU LEU GLU GLU GLY LYS ALA THR VAL PRO SER
SEQRES 23 A 360 LEU ALA GLU LYS LEU THR SER GLU LEU ILE THR HIS ILE
SEQRES 24 A 360 SER LYS SER LEU PRO LEU LEU GLU ASN GLN ILE LYS GLU
SEQRES 25 A 360 THR HIS GLN ARG ILE THR GLU GLU LEU GLN LYS TYR GLY
SEQRES 26 A 360 VAL ASP ILE PRO GLU GLY SER GLY SER SER ASP LYS ARG
SEQRES 27 A 360 LYS PHE LEU LYS GLU ARG LEU ALA ARG LEU THR GLN ALA
SEQRES 28 A 360 ARG ARG ARG LEU ALA GLN PHE PRO GLY
HET GDP A 701 28
HET SO4 A 702 5
HET SO4 A 703 5
HET SO4 A 704 5
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM SO4 SULFATE ION
FORMUL 2 GDP C10 H15 N5 O11 P2
FORMUL 3 SO4 3(O4 S 2-)
FORMUL 6 HOH *87(H2 O)
HELIX 1 AA1 VAL A 49 ALA A 61 1 13
HELIX 2 AA2 GLY A 82 GLY A 92 1 11
HELIX 3 AA3 ASP A 135 SER A 137 5 3
HELIX 4 AA4 GLU A 138 ALA A 151 1 14
HELIX 5 AA5 ASP A 193 GLN A 207 1 15
HELIX 6 AA6 ASP A 222 THR A 225 5 4
HELIX 7 AA7 THR A 226 ASP A 236 1 11
HELIX 8 AA8 LYS A 248 VAL A 252 5 5
HELIX 9 AA9 THR A 256 ARG A 265 1 10
HELIX 10 AB1 GLY A 282 ASP A 288 1 7
HELIX 11 AB2 SER A 291 HIS A 306 1 16
HELIX 12 AB3 PHE A 309 GLU A 315 1 7
HELIX 13 AB4 THR A 319 LEU A 339 1 21
HELIX 14 AB5 LEU A 341 TYR A 360 1 20
HELIX 15 AB6 ARG A 640 PHE A 660 1 21
SHEET 1 AA1 9 TYR A 129 ILE A 133 0
SHEET 2 AA1 9 ARG A 121 TYR A 126 -1 N VAL A 124 O ILE A 131
SHEET 3 AA1 9 ILE A 162 SER A 168 -1 O GLU A 165 N LYS A 123
SHEET 4 AA1 9 LEU A 107 LYS A 113 1 N LYS A 110 O LEU A 164
SHEET 5 AA1 9 LEU A 174 ASP A 178 -1 O LEU A 174 N LEU A 111
SHEET 6 AA1 9 ALA A 72 GLY A 77 1 N VAL A 75 O ILE A 177
SHEET 7 AA1 9 THR A 211 PRO A 218 1 O LEU A 214 N ALA A 74
SHEET 8 AA1 9 THR A 242 THR A 247 1 O ILE A 245 N VAL A 217
SHEET 9 AA1 9 TYR A 275 ILE A 277 1 O MET A 276 N LEU A 246
CISPEP 1 PHE A 660 PRO A 661 0 5.08
SITE 1 AC1 18 SER A 80 SER A 81 GLY A 82 LYS A 83
SITE 2 AC1 18 SER A 84 SER A 85 LYS A 248 ASP A 250
SITE 3 AC1 18 ASP A 253 LYS A 279 CYS A 280 ARG A 281
SITE 4 AC1 18 GLY A 282 GLN A 283 ILE A 286 HOH A 809
SITE 5 AC1 18 HOH A 845 HOH A 848
SITE 1 AC2 5 LYS A 141 LYS A 145 ASN A 266 LYS A 317
SITE 2 AC2 5 HOH A 808
SITE 1 AC3 1 ARG A 208
SITE 1 AC4 2 ARG A 654 ARG A 655
CRYST1 47.020 77.590 212.330 90.00 90.00 90.00 I 21 21 21 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 0.021268 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012888 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004710 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
