HEADER REPLICATION/RECOMBINATION 06-DEC-06 2O5V
TITLE RECOMBINATION MEDIATOR RECF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA REPLICATION AND REPAIR PROTEIN RECF;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 3 ORGANISM_TAXID: 1299;
SOURCE 4 GENE: RECF;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS ABC ATPASE, WALKER A MOTIF, P-LOOP, SIGNATURE MOTIF, REPLICATION-
KEYWDS 2 RECOMBINATION COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KOROLEV,O.KOROLEVA
REVDAT 4 27-DEC-23 2O5V 1 REMARK
REVDAT 3 24-FEB-09 2O5V 1 VERSN
REVDAT 2 29-MAY-07 2O5V 1 JRNL
REVDAT 1 06-FEB-07 2O5V 0
JRNL AUTH O.KOROLEVA,N.MAKHARASHVILI,C.T.COURCELLE,J.COURCELLE,
JRNL AUTH 2 S.KOROLEV
JRNL TITL STRUCTURAL CONSERVATION OF RECF AND RAD50: IMPLICATIONS FOR
JRNL TITL 2 DNA RECOGNITION AND RECF FUNCTION.
JRNL REF EMBO J. V. 26 867 2007
JRNL REFN ISSN 0261-4189
JRNL PMID 17255941
JRNL DOI 10.1038/SJ.EMBOJ.7601537
REMARK 2
REMARK 2 RESOLUTION. 1.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 80.9
REMARK 3 NUMBER OF REFLECTIONS : 39056
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2084
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) : 1.61
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.65
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1205
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 34.11
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE SET COUNT : 76
REMARK 3 BIN FREE R VALUE : 0.2600
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2737
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 500
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.33000
REMARK 3 B22 (A**2) : -0.17000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.61000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.103
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.109
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.063
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.788
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2781 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1932 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3768 ; 1.579 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4651 ; 0.924 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 357 ; 6.055 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 132 ;31.376 ;22.500
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 463 ;13.893 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;20.824 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 425 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3165 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 590 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 628 ; 0.234 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2215 ; 0.231 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1377 ; 0.177 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1545 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 339 ; 0.185 ; 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): 15 ; 0.140 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 73 ; 0.273 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 38 ; 0.191 ; 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): 2305 ; 1.638 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 737 ; 0.293 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2801 ; 1.733 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1124 ; 2.987 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 967 ; 4.496 ; 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 : BABINET MODEL WITH MASK
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2O5V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-DEC-06.
REMARK 100 THE DEPOSITION ID IS D_1000040725.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUL-04; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 19-ID; 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97959; 0.97934
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL
REMARK 200 DETECTOR MANUFACTURER : SBC-2; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41165
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.610
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 49.20
REMARK 200 R MERGE FOR SHELL (I) : 0.43600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: ARP/WARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5M (NH4)2SO4 20% SUCROSE, PH 8,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 43.70950
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: MONOMERIC
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 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 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 110 CB CG CD NE CZ NH1 NH2
REMARK 470 GLU A 351 CG CD OE1 OE2
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 O HOH A 707 O HOH A 1021 2.06
REMARK 500 O HOH A 790 O HOH A 1051 2.07
REMARK 500 OD1 ASN A 23 O HOH A 933 2.13
REMARK 500 O HOH A 724 O HOH A 1058 2.17
REMARK 500 OD2 ASP A 300 O HOH A 972 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 A 94 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 202 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 280 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG A 280 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG A 309 NE - CZ - NH1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG A 309 NE - CZ - NH2 ANGL. DEV. = -6.8 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 109 -120.69 -81.09
REMARK 500 GLU A 168 45.14 -108.94
REMARK 500 ASP A 259 -1.64 71.53
REMARK 500 ASP A 300 68.80 60.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 109 ARG A 110 -149.53
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 SO4 A 600
DBREF 2O5V A 1 359 UNP Q9RVE0 RECF_DEIRA 1 359
SEQRES 1 A 359 MET GLY ASP VAL ARG LEU SER ALA LEU SER THR LEU ASN
SEQRES 2 A 359 TYR ARG ASN LEU ALA PRO GLY THR LEU ASN PHE PRO GLU
SEQRES 3 A 359 GLY VAL THR GLY ILE TYR GLY GLU ASN GLY ALA GLY LYS
SEQRES 4 A 359 THR ASN LEU LEU GLU ALA ALA TYR LEU ALA LEU THR GLY
SEQRES 5 A 359 GLN THR ASP ALA PRO ARG ILE GLU GLN LEU ILE GLN ALA
SEQRES 6 A 359 GLY GLU THR GLU ALA TYR VAL ARG ALA ASP LEU GLN GLN
SEQRES 7 A 359 GLY GLY SER LEU SER ILE GLN GLU VAL GLY LEU GLY ARG
SEQRES 8 A 359 GLY ARG ARG GLN LEU LYS VAL ASP GLY VAL ARG ALA ARG
SEQRES 9 A 359 THR GLY ASP LEU PRO ARG GLY GLY ALA VAL TRP ILE ARG
SEQRES 10 A 359 PRO GLU ASP SER GLU LEU VAL PHE GLY PRO PRO SER GLY
SEQRES 11 A 359 ARG ARG ALA TYR LEU ASP SER LEU LEU SER ARG LEU SER
SEQRES 12 A 359 ALA ARG TYR GLY GLU GLN LEU SER ARG TYR GLU ARG THR
SEQRES 13 A 359 VAL SER GLN ARG ASN ALA ALA LEU ARG GLY GLY GLU GLU
SEQRES 14 A 359 TRP ALA MET HIS VAL TRP ASP ASP VAL LEU LEU LYS LEU
SEQRES 15 A 359 GLY THR GLU ILE MET LEU PHE ARG ARG ARG ALA LEU THR
SEQRES 16 A 359 ARG LEU ASP GLU LEU ALA ARG GLU ALA ASN ALA GLN LEU
SEQRES 17 A 359 GLY SER ARG LYS THR LEU ALA LEU THR LEU THR GLU SER
SEQRES 18 A 359 THR SER PRO GLU THR TYR ALA ALA ASP LEU ARG GLY ARG
SEQRES 19 A 359 ARG ALA GLU GLU LEU ALA ARG GLY SER THR VAL THR GLY
SEQRES 20 A 359 PRO HIS ARG ASP ASP LEU LEU LEU THR LEU GLY ASP PHE
SEQRES 21 A 359 PRO ALA SER ASP TYR ALA SER ARG GLY GLU GLY ARG THR
SEQRES 22 A 359 VAL ALA LEU ALA LEU ARG ARG ALA GLU LEU GLU LEU LEU
SEQRES 23 A 359 ARG GLU LYS PHE GLY GLU ASP PRO VAL LEU LEU LEU ASP
SEQRES 24 A 359 ASP PHE THR ALA GLU LEU ASP PRO HIS ARG ARG GLN TYR
SEQRES 25 A 359 LEU LEU ASP LEU ALA ALA SER VAL PRO GLN ALA ILE VAL
SEQRES 26 A 359 THR GLY THR GLU LEU ALA PRO GLY ALA ALA LEU THR LEU
SEQRES 27 A 359 ARG ALA GLN ALA GLY ARG PHE THR PRO VAL ALA ASP GLU
SEQRES 28 A 359 GLU MET GLN ALA GLU GLY THR ALA
HET SO4 A 600 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *500(H2 O)
HELIX 1 1 GLY A 38 GLY A 52 1 15
HELIX 2 2 ARG A 58 ILE A 63 5 6
HELIX 3 3 ARG A 104 LEU A 108 5 5
HELIX 4 4 SER A 121 GLY A 126 1 6
HELIX 5 5 PRO A 127 SER A 143 1 17
HELIX 6 6 SER A 143 GLY A 166 1 24
HELIX 7 7 GLU A 168 MET A 172 5 5
HELIX 8 8 TRP A 175 LEU A 208 1 34
HELIX 9 9 THR A 226 ARG A 234 1 9
HELIX 10 10 ARG A 234 GLY A 242 1 9
HELIX 11 11 GLY A 247 ASP A 251 5 5
HELIX 12 12 ALA A 262 ALA A 266 1 5
HELIX 13 13 SER A 267 GLY A 291 1 25
HELIX 14 14 ASP A 300 GLU A 304 5 5
HELIX 15 15 ASP A 306 VAL A 320 1 15
SHEET 1 A 6 GLY A 20 ASN A 23 0
SHEET 2 A 6 LEU A 6 LEU A 12 -1 N LEU A 9 O LEU A 22
SHEET 3 A 6 ALA A 70 GLN A 78 -1 O ASP A 75 N ALA A 8
SHEET 4 A 6 SER A 81 GLY A 90 -1 O GLN A 85 N ALA A 74
SHEET 5 A 6 ARG A 93 VAL A 98 -1 O GLN A 95 N GLY A 88
SHEET 6 A 6 VAL A 101 ALA A 103 -1 O VAL A 101 N VAL A 98
SHEET 1 B 6 ALA A 113 ILE A 116 0
SHEET 2 B 6 VAL A 295 LEU A 298 1 O LEU A 297 N VAL A 114
SHEET 3 B 6 GLN A 322 GLY A 327 1 O ILE A 324 N LEU A 298
SHEET 4 B 6 GLY A 27 TYR A 32 1 N THR A 29 O ALA A 323
SHEET 5 B 6 LEU A 336 GLN A 341 1 O ALA A 340 N TYR A 32
SHEET 6 B 6 ARG A 344 PRO A 347 -1 O THR A 346 N ARG A 339
SHEET 1 C 3 LEU A 214 THR A 219 0
SHEET 2 C 3 ASP A 252 LEU A 257 -1 O ASP A 252 N THR A 219
SHEET 3 C 3 PHE A 260 PRO A 261 -1 O PHE A 260 N LEU A 257
SITE 1 AC1 10 GLU A 34 ASN A 35 GLY A 36 ALA A 37
SITE 2 AC1 10 GLY A 38 LYS A 39 THR A 40 HOH A 810
SITE 3 AC1 10 HOH A 817 HOH A1096
CRYST1 47.897 87.419 52.898 90.00 115.00 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 0.020878 0.000000 0.009736 0.00000
SCALE2 0.000000 0.011439 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020859 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
