HEADER MEMBRANE PROTEIN/PROTEIN TRANSPORT 14-FEB-11 3QQ2
TITLE CRYSTAL STRUCTURE OF THE BETA DOMAIN OF THE BORDETELLA AUTOTRANSPORTER
TITLE 2 BRKA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BRKA AUTOTRANSPORTER;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: BETA DOMAIN, UNP RESIDUES 727-1010;
COMPND 5 SYNONYM: SERUM RESISTANCE PROTEIN BRKA, BRKA TRANSLOCATOR;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BORDETELLA PERTUSSIS;
SOURCE 3 ORGANISM_TAXID: 520;
SOURCE 4 GENE: BP3494, BRKA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS BETA BARREL, TRANSMEMBRANE, MEMBRANE PROTEIN-PROTEIN TRANSPORT
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHAI,K.ZHANG,Y.HUO,F.SUN
REVDAT 3 01-NOV-23 3QQ2 1 SEQADV
REVDAT 2 27-APR-11 3QQ2 1 JRNL
REVDAT 1 13-APR-11 3QQ2 0
JRNL AUTH Y.ZHAI,K.ZHANG,Y.HUO,Y.ZHU,Q.ZHOU,J.LU,I.BLACK,X.PANG,
JRNL AUTH 2 A.W.ROSZAK,X.ZHANG,N.W.ISAACS,F.SUN
JRNL TITL AUTOTRANSPORTER PASSENGER DOMAIN SECRETION REQUIRES A
JRNL TITL 2 HYDROPHOBIC CAVITY AT THE EXTRACELLULAR ENTRANCE OF THE
JRNL TITL 3 BETA-DOMAIN PORE
JRNL REF BIOCHEM.J. V. 435 577 2011
JRNL REFN ISSN 0264-6021
JRNL PMID 21306302
JRNL DOI 10.1042/BJ20101548
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0088
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 28054
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) : 0.269
REMARK 3 R VALUE (WORKING SET) : 0.266
REMARK 3 FREE R VALUE : 0.324
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1507
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1474
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.29
REMARK 3 BIN R VALUE (WORKING SET) : 0.3830
REMARK 3 BIN FREE R VALUE SET COUNT : 94
REMARK 3 BIN FREE R VALUE : 0.4560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5772
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 97.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 92.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.26000
REMARK 3 B22 (A**2) : -2.22000
REMARK 3 B33 (A**2) : -0.03000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.454
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.343
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 41.812
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.895
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.848
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5927 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8012 ; 1.588 ; 1.929
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 738 ; 7.262 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 301 ;35.809 ;21.528
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 850 ;23.510 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 71 ;17.957 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 774 ; 0.109 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4768 ; 0.005 ; 0.020
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): 3619 ; 0.471 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5629 ; 0.922 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2308 ; 1.319 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2383 ; 2.314 ; 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 : 3
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 745 A 1010
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6630 -7.2937 29.0123
REMARK 3 T TENSOR
REMARK 3 T11: 0.2399 T22: 0.1186
REMARK 3 T33: 0.1563 T12: -0.1290
REMARK 3 T13: -0.1043 T23: 0.0398
REMARK 3 L TENSOR
REMARK 3 L11: 1.8190 L22: 2.3669
REMARK 3 L33: 2.1766 L12: 0.1475
REMARK 3 L13: -0.1289 L23: -1.0365
REMARK 3 S TENSOR
REMARK 3 S11: 0.1576 S12: 0.0726 S13: -0.0626
REMARK 3 S21: -0.2016 S22: -0.0958 S23: 0.0960
REMARK 3 S31: 0.4335 S32: -0.2959 S33: -0.0618
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 745 B 1010
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2690 -40.9964 41.6166
REMARK 3 T TENSOR
REMARK 3 T11: 0.2517 T22: 0.2787
REMARK 3 T33: 0.1760 T12: -0.1674
REMARK 3 T13: -0.0954 T23: 0.0552
REMARK 3 L TENSOR
REMARK 3 L11: 1.4092 L22: 3.7527
REMARK 3 L33: 2.0759 L12: -0.0694
REMARK 3 L13: -0.0486 L23: -0.7670
REMARK 3 S TENSOR
REMARK 3 S11: -0.2155 S12: -0.2744 S13: 0.2063
REMARK 3 S21: 0.2250 S22: 0.0294 S23: -0.0774
REMARK 3 S31: -0.2966 S32: 0.2321 S33: 0.1861
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 745 C 1010
REMARK 3 ORIGIN FOR THE GROUP (A): 36.9500 -68.4109 84.1491
REMARK 3 T TENSOR
REMARK 3 T11: 0.4779 T22: 0.8908
REMARK 3 T33: 0.4800 T12: 0.0657
REMARK 3 T13: -0.1029 T23: 0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 2.2183 L22: 0.7964
REMARK 3 L33: 4.4784 L12: 0.0738
REMARK 3 L13: 1.4967 L23: -0.4678
REMARK 3 S TENSOR
REMARK 3 S11: 0.0112 S12: -0.4042 S13: 0.0783
REMARK 3 S21: 0.0081 S22: 0.0630 S23: -0.0286
REMARK 3 S31: 0.2329 S32: 0.0536 S33: -0.0742
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3QQ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000063959.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.07176
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29563
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 8.400
REMARK 200 R MERGE (I) : 0.14500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 35.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.31500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.268
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2QOM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TIS-HCL, 10MM SPERMIDINE, 200MM
REMARK 280 LICL, 25% PEG 2000, PH8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 202.77450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 202.77450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 30.25500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 61.18600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 30.25500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 61.18600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 202.77450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 30.25500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 61.18600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 202.77450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 30.25500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 61.18600
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: 2700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 0.00000
REMARK 350 BIOMT3 2 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: 2820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 727
REMARK 465 ALA A 728
REMARK 465 GLU A 729
REMARK 465 SER A 730
REMARK 465 ASN A 731
REMARK 465 ALA A 732
REMARK 465 LEU A 733
REMARK 465 ASP A 734
REMARK 465 LYS A 735
REMARK 465 ARG A 736
REMARK 465 LEU A 737
REMARK 465 GLY A 738
REMARK 465 GLU A 739
REMARK 465 LEU A 740
REMARK 465 ARG A 741
REMARK 465 LEU A 742
REMARK 465 ARG A 743
REMARK 465 ALA A 744
REMARK 465 ARG A 763
REMARK 465 HIS A 764
REMARK 465 ALA A 765
REMARK 465 ARG A 766
REMARK 465 THR A 949
REMARK 465 GLY A 950
REMARK 465 ASP A 951
REMARK 465 VAL A 952
REMARK 465 ARG A 953
REMARK 465 THR A 954
REMARK 465 ASN A 955
REMARK 465 GLY A 956
REMARK 465 ILE A 957
REMARK 465 GLY A 958
REMARK 465 HIS A 959
REMARK 465 ALA A 960
REMARK 465 GLY A 961
REMARK 465 ALA A 962
REMARK 465 GLY A 963
REMARK 465 ARG A 964
REMARK 465 HIS A 965
REMARK 465 MET B 727
REMARK 465 ALA B 728
REMARK 465 GLU B 729
REMARK 465 SER B 730
REMARK 465 ASN B 731
REMARK 465 ALA B 732
REMARK 465 LEU B 733
REMARK 465 ASP B 734
REMARK 465 LYS B 735
REMARK 465 ARG B 736
REMARK 465 LEU B 737
REMARK 465 GLY B 738
REMARK 465 GLU B 739
REMARK 465 LEU B 740
REMARK 465 ARG B 741
REMARK 465 LEU B 742
REMARK 465 ARG B 743
REMARK 465 ALA B 744
REMARK 465 HIS B 764
REMARK 465 ALA B 765
REMARK 465 ARG B 766
REMARK 465 GLY B 950
REMARK 465 ASP B 951
REMARK 465 VAL B 952
REMARK 465 ARG B 953
REMARK 465 THR B 954
REMARK 465 ASN B 955
REMARK 465 GLY B 956
REMARK 465 ILE B 957
REMARK 465 GLY B 958
REMARK 465 HIS B 959
REMARK 465 ALA B 960
REMARK 465 GLY B 961
REMARK 465 ALA B 962
REMARK 465 MET C 727
REMARK 465 ALA C 728
REMARK 465 GLU C 729
REMARK 465 SER C 730
REMARK 465 ASN C 731
REMARK 465 ALA C 732
REMARK 465 LEU C 733
REMARK 465 ASP C 734
REMARK 465 LYS C 735
REMARK 465 ARG C 736
REMARK 465 LEU C 737
REMARK 465 GLY C 738
REMARK 465 GLU C 739
REMARK 465 LEU C 740
REMARK 465 ARG C 741
REMARK 465 LEU C 742
REMARK 465 ARG C 743
REMARK 465 ALA C 744
REMARK 465 ARG C 763
REMARK 465 HIS C 764
REMARK 465 ALA C 765
REMARK 465 ARG C 766
REMARK 465 GLY C 950
REMARK 465 ASP C 951
REMARK 465 VAL C 952
REMARK 465 ARG C 953
REMARK 465 THR C 954
REMARK 465 ASN C 955
REMARK 465 GLY C 956
REMARK 465 ILE C 957
REMARK 465 GLY C 958
REMARK 465 HIS C 959
REMARK 465 ALA C 960
REMARK 465 GLY C 961
REMARK 465 ALA C 962
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 LEU A 816 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 LEU B 816 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 LEU C 832 CA - CB - CG ANGL. DEV. = 14.8 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 PRO A 806 -91.47 -53.71
REMARK 500 ASP A 808 -110.60 -46.51
REMARK 500 THR A 850 -16.19 56.60
REMARK 500 TYR A 898 -163.97 -126.14
REMARK 500 ARG A 899 112.02 -177.32
REMARK 500 ASN A 902 43.52 38.19
REMARK 500 ARG A 967 161.18 179.06
REMARK 500 LYS A 980 46.66 83.36
REMARK 500 ASP A 994 -85.27 -55.67
REMARK 500 ASN A 997 107.12 -160.46
REMARK 500 THR B 850 -145.14 31.33
REMARK 500 PRO B 877 140.96 -34.29
REMARK 500 ASN B 902 61.77 14.68
REMARK 500 ALA B 910 84.75 -57.42
REMARK 500 THR B 912 117.35 -162.57
REMARK 500 HIS B 965 -153.58 -140.77
REMARK 500 LYS B 980 62.13 72.51
REMARK 500 ASP B 994 -73.65 -52.50
REMARK 500 ALA C 746 78.55 61.62
REMARK 500 SER C 755 101.28 -168.02
REMARK 500 SER C 784 76.46 -151.95
REMARK 500 PRO C 806 101.43 -42.90
REMARK 500 ASP C 851 156.37 106.59
REMARK 500 ARG C 854 78.13 -159.16
REMARK 500 ASP C 879 16.26 85.49
REMARK 500 GLU C 883 80.38 -159.44
REMARK 500 SER C 901 -99.05 -31.70
REMARK 500 ASN C 902 62.36 -66.04
REMARK 500 ALA C 929 91.85 -65.83
REMARK 500 ARG C 967 103.12 177.89
REMARK 500 TYR C 990 100.95 -178.40
REMARK 500 ARG C 995 24.50 173.12
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3QQ2 A 727 1010 UNP Q45340 BRKA_BORPE 727 1010
DBREF 3QQ2 B 727 1010 UNP Q45340 BRKA_BORPE 727 1010
DBREF 3QQ2 C 727 1010 UNP Q45340 BRKA_BORPE 727 1010
SEQADV 3QQ2 MET A 727 UNP Q45340 LEU 727 ENGINEERED MUTATION
SEQADV 3QQ2 MET B 727 UNP Q45340 LEU 727 ENGINEERED MUTATION
SEQADV 3QQ2 MET C 727 UNP Q45340 LEU 727 ENGINEERED MUTATION
SEQRES 1 A 284 MET ALA GLU SER ASN ALA LEU ASP LYS ARG LEU GLY GLU
SEQRES 2 A 284 LEU ARG LEU ARG ALA ASP ALA GLY GLY PRO TRP ALA ARG
SEQRES 3 A 284 THR PHE SER GLU ARG GLN GLN ILE SER ASN ARG HIS ALA
SEQRES 4 A 284 ARG ALA TYR ASP GLN THR VAL SER GLY LEU GLU ILE GLY
SEQRES 5 A 284 LEU ASP ARG GLY TRP SER ALA SER GLY GLY ARG TRP TYR
SEQRES 6 A 284 ALA GLY GLY LEU LEU GLY TYR THR TYR ALA ASP ARG THR
SEQRES 7 A 284 TYR PRO GLY ASP GLY GLY GLY LYS VAL LYS GLY LEU HIS
SEQRES 8 A 284 VAL GLY GLY TYR ALA ALA TYR VAL GLY ASP GLY GLY TYR
SEQRES 9 A 284 TYR LEU ASP THR VAL LEU ARG LEU GLY ARG TYR ASP GLN
SEQRES 10 A 284 GLN TYR ASN ILE ALA GLY THR ASP GLY GLY ARG VAL THR
SEQRES 11 A 284 ALA ASP TYR ARG THR SER GLY ALA ALA TRP SER LEU GLU
SEQRES 12 A 284 GLY GLY ARG ARG PHE GLU LEU PRO ASN ASP TRP PHE ALA
SEQRES 13 A 284 GLU PRO GLN ALA GLU VAL MET LEU TRP ARG THR SER GLY
SEQRES 14 A 284 LYS ARG TYR ARG ALA SER ASN GLY LEU ARG VAL LYS VAL
SEQRES 15 A 284 ASP ALA ASN THR ALA THR LEU GLY ARG LEU GLY LEU ARG
SEQRES 16 A 284 PHE GLY ARG ARG ILE ALA LEU ALA GLY GLY ASN ILE VAL
SEQRES 17 A 284 GLN PRO TYR ALA ARG LEU GLY TRP THR GLN GLU PHE LYS
SEQRES 18 A 284 SER THR GLY ASP VAL ARG THR ASN GLY ILE GLY HIS ALA
SEQRES 19 A 284 GLY ALA GLY ARG HIS GLY ARG VAL GLU LEU GLY ALA GLY
SEQRES 20 A 284 VAL ASP ALA ALA LEU GLY LYS GLY HIS ASN LEU TYR ALA
SEQRES 21 A 284 SER TYR GLU TYR ALA ALA GLY ASP ARG ILE ASN ILE PRO
SEQRES 22 A 284 TRP SER PHE HIS ALA GLY TYR ARG TYR SER PHE
SEQRES 1 B 284 MET ALA GLU SER ASN ALA LEU ASP LYS ARG LEU GLY GLU
SEQRES 2 B 284 LEU ARG LEU ARG ALA ASP ALA GLY GLY PRO TRP ALA ARG
SEQRES 3 B 284 THR PHE SER GLU ARG GLN GLN ILE SER ASN ARG HIS ALA
SEQRES 4 B 284 ARG ALA TYR ASP GLN THR VAL SER GLY LEU GLU ILE GLY
SEQRES 5 B 284 LEU ASP ARG GLY TRP SER ALA SER GLY GLY ARG TRP TYR
SEQRES 6 B 284 ALA GLY GLY LEU LEU GLY TYR THR TYR ALA ASP ARG THR
SEQRES 7 B 284 TYR PRO GLY ASP GLY GLY GLY LYS VAL LYS GLY LEU HIS
SEQRES 8 B 284 VAL GLY GLY TYR ALA ALA TYR VAL GLY ASP GLY GLY TYR
SEQRES 9 B 284 TYR LEU ASP THR VAL LEU ARG LEU GLY ARG TYR ASP GLN
SEQRES 10 B 284 GLN TYR ASN ILE ALA GLY THR ASP GLY GLY ARG VAL THR
SEQRES 11 B 284 ALA ASP TYR ARG THR SER GLY ALA ALA TRP SER LEU GLU
SEQRES 12 B 284 GLY GLY ARG ARG PHE GLU LEU PRO ASN ASP TRP PHE ALA
SEQRES 13 B 284 GLU PRO GLN ALA GLU VAL MET LEU TRP ARG THR SER GLY
SEQRES 14 B 284 LYS ARG TYR ARG ALA SER ASN GLY LEU ARG VAL LYS VAL
SEQRES 15 B 284 ASP ALA ASN THR ALA THR LEU GLY ARG LEU GLY LEU ARG
SEQRES 16 B 284 PHE GLY ARG ARG ILE ALA LEU ALA GLY GLY ASN ILE VAL
SEQRES 17 B 284 GLN PRO TYR ALA ARG LEU GLY TRP THR GLN GLU PHE LYS
SEQRES 18 B 284 SER THR GLY ASP VAL ARG THR ASN GLY ILE GLY HIS ALA
SEQRES 19 B 284 GLY ALA GLY ARG HIS GLY ARG VAL GLU LEU GLY ALA GLY
SEQRES 20 B 284 VAL ASP ALA ALA LEU GLY LYS GLY HIS ASN LEU TYR ALA
SEQRES 21 B 284 SER TYR GLU TYR ALA ALA GLY ASP ARG ILE ASN ILE PRO
SEQRES 22 B 284 TRP SER PHE HIS ALA GLY TYR ARG TYR SER PHE
SEQRES 1 C 284 MET ALA GLU SER ASN ALA LEU ASP LYS ARG LEU GLY GLU
SEQRES 2 C 284 LEU ARG LEU ARG ALA ASP ALA GLY GLY PRO TRP ALA ARG
SEQRES 3 C 284 THR PHE SER GLU ARG GLN GLN ILE SER ASN ARG HIS ALA
SEQRES 4 C 284 ARG ALA TYR ASP GLN THR VAL SER GLY LEU GLU ILE GLY
SEQRES 5 C 284 LEU ASP ARG GLY TRP SER ALA SER GLY GLY ARG TRP TYR
SEQRES 6 C 284 ALA GLY GLY LEU LEU GLY TYR THR TYR ALA ASP ARG THR
SEQRES 7 C 284 TYR PRO GLY ASP GLY GLY GLY LYS VAL LYS GLY LEU HIS
SEQRES 8 C 284 VAL GLY GLY TYR ALA ALA TYR VAL GLY ASP GLY GLY TYR
SEQRES 9 C 284 TYR LEU ASP THR VAL LEU ARG LEU GLY ARG TYR ASP GLN
SEQRES 10 C 284 GLN TYR ASN ILE ALA GLY THR ASP GLY GLY ARG VAL THR
SEQRES 11 C 284 ALA ASP TYR ARG THR SER GLY ALA ALA TRP SER LEU GLU
SEQRES 12 C 284 GLY GLY ARG ARG PHE GLU LEU PRO ASN ASP TRP PHE ALA
SEQRES 13 C 284 GLU PRO GLN ALA GLU VAL MET LEU TRP ARG THR SER GLY
SEQRES 14 C 284 LYS ARG TYR ARG ALA SER ASN GLY LEU ARG VAL LYS VAL
SEQRES 15 C 284 ASP ALA ASN THR ALA THR LEU GLY ARG LEU GLY LEU ARG
SEQRES 16 C 284 PHE GLY ARG ARG ILE ALA LEU ALA GLY GLY ASN ILE VAL
SEQRES 17 C 284 GLN PRO TYR ALA ARG LEU GLY TRP THR GLN GLU PHE LYS
SEQRES 18 C 284 SER THR GLY ASP VAL ARG THR ASN GLY ILE GLY HIS ALA
SEQRES 19 C 284 GLY ALA GLY ARG HIS GLY ARG VAL GLU LEU GLY ALA GLY
SEQRES 20 C 284 VAL ASP ALA ALA LEU GLY LYS GLY HIS ASN LEU TYR ALA
SEQRES 21 C 284 SER TYR GLU TYR ALA ALA GLY ASP ARG ILE ASN ILE PRO
SEQRES 22 C 284 TRP SER PHE HIS ALA GLY TYR ARG TYR SER PHE
HELIX 1 1 LEU C 978 HIS C 982 5 5
CISPEP 1 PRO B 806 GLY B 807 0 -11.87
CRYST1 60.510 122.372 405.549 90.00 90.00 90.00 C 2 2 21 24
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 0.016526 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008172 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002466 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
