HEADER HYDROLASE 27-JUL-07 2QR4
TITLE CRYSTAL STRUCTURE OF OLIGOENDOPEPTIDASE-F FROM ENTEROCOCCUS FAECIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDASE M3B, OLIGOENDOPEPTIDASE F;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 26-601;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS FAECIUM;
SOURCE 3 ORGANISM_TAXID: 333849;
SOURCE 4 STRAIN: DO;
SOURCE 5 GENE: EFAEDRAFT_1000;
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: BS-PSGX4(BC)
KEYWDS STRUCTURAL GENOMICS, OLIGOENDOPEPTIDASE F, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS,
KEYWDS 3 NYSGXRC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR U.A.RAMAGOPAL,R.TORO,A.J.MEYER,J.FREEMAN,K.BAIN,L.RODGERS,J.M.SAUDER,
AUTHOR 2 S.K.BURLEY,S.C.ALMO,NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL
AUTHOR 3 GENOMICS (NYSGXRC)
REVDAT 6 03-FEB-21 2QR4 1 AUTHOR JRNL SEQADV LINK
REVDAT 5 14-NOV-18 2QR4 1 AUTHOR
REVDAT 4 25-OCT-17 2QR4 1 REMARK
REVDAT 3 13-JUL-11 2QR4 1 VERSN
REVDAT 2 24-FEB-09 2QR4 1 VERSN
REVDAT 1 14-AUG-07 2QR4 0
JRNL AUTH U.A.RAMAGOPAL,R.TORO,A.J.MEYER,J.FREEMAN,K.BAIN,L.RODGERS,
JRNL AUTH 2 J.M.SAUDER,S.K.BURLEY,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF OLIGOENDOPEPTIDASE-F FROM ENTEROCOCCUS
JRNL TITL 2 FAECIUM.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 53751
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2726
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3697
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.2400
REMARK 3 BIN FREE R VALUE SET COUNT : 184
REMARK 3 BIN FREE R VALUE : 0.3140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8308
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 188
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.18000
REMARK 3 B22 (A**2) : 0.18000
REMARK 3 B33 (A**2) : -0.36000
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): 0.342
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.255
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.169
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.317
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8553 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11582 ; 1.142 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1030 ; 4.520 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 454 ;35.664 ;24.670
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1447 ;18.629 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;17.263 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1246 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6617 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4034 ; 0.235 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5972 ; 0.325 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 602 ; 0.184 ; 0.500
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): 42 ; 0.257 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.223 ; 0.500
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): 5255 ; 5.767 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8268 ; 7.055 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3707 ; 7.380 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3314 ; 9.177 ; 3.000
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 : 4
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 25 A 158 4
REMARK 3 1 B 25 B 158 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1094 ; 0.900 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1094 ; 3.920 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 159 A 312 4
REMARK 3 1 B 159 B 312 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 1209 ; 0.370 ; 0.500
REMARK 3 MEDIUM THERMAL 2 A (A**2): 1209 ; 2.910 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 324 A 416 4
REMARK 3 1 B 324 B 416 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 A (A): 253 ; 0.540 ; 0.500
REMARK 3 MEDIUM THERMAL 3 A (A**2): 253 ; 2.830 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 417 A 600 4
REMARK 3 1 B 417 B 600 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 4 A (A): 1461 ; 0.390 ; 0.500
REMARK 3 MEDIUM THERMAL 4 A (A**2): 1461 ; 3.110 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
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 25 A 158
REMARK 3 ORIGIN FOR THE GROUP (A): 35.8420 46.7690 78.1580
REMARK 3 T TENSOR
REMARK 3 T11: 0.0440 T22: 0.0547
REMARK 3 T33: -0.2236 T12: -0.0275
REMARK 3 T13: 0.0037 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 3.9940 L22: 1.2211
REMARK 3 L33: 3.0020 L12: -0.3539
REMARK 3 L13: -0.9626 L23: -0.3997
REMARK 3 S TENSOR
REMARK 3 S11: -0.0878 S12: -0.6142 S13: 0.0055
REMARK 3 S21: 0.1713 S22: 0.1009 S23: 0.0365
REMARK 3 S31: 0.0006 S32: -0.0279 S33: -0.0131
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 : A 159 A 316
REMARK 3 ORIGIN FOR THE GROUP (A): 54.9240 70.7650 61.6390
REMARK 3 T TENSOR
REMARK 3 T11: -0.0861 T22: -0.0633
REMARK 3 T33: -0.2997 T12: -0.0307
REMARK 3 T13: -0.0009 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.7053 L22: 1.6645
REMARK 3 L33: 0.8588 L12: 0.4206
REMARK 3 L13: -0.0849 L23: 0.3117
REMARK 3 S TENSOR
REMARK 3 S11: -0.0035 S12: -0.1654 S13: 0.0515
REMARK 3 S21: 0.0310 S22: 0.0566 S23: -0.1263
REMARK 3 S31: -0.0618 S32: 0.1123 S33: -0.0531
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 : A 322 A 419
REMARK 3 ORIGIN FOR THE GROUP (A): 54.4670 75.7960 90.5380
REMARK 3 T TENSOR
REMARK 3 T11: 0.6381 T22: 0.4101
REMARK 3 T33: 0.1945 T12: 0.1184
REMARK 3 T13: -0.0228 T23: 0.1677
REMARK 3 L TENSOR
REMARK 3 L11: 11.1059 L22: 5.1264
REMARK 3 L33: 2.7956 L12: 2.9597
REMARK 3 L13: 2.3131 L23: 1.8576
REMARK 3 S TENSOR
REMARK 3 S11: 0.4089 S12: -0.9810 S13: -1.0051
REMARK 3 S21: 0.9934 S22: -0.7016 S23: -0.4537
REMARK 3 S31: 0.8751 S32: -0.0130 S33: 0.2926
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 420 A 602
REMARK 3 ORIGIN FOR THE GROUP (A): 48.9880 79.8700 71.6890
REMARK 3 T TENSOR
REMARK 3 T11: -0.0656 T22: -0.0322
REMARK 3 T33: -0.2281 T12: 0.0182
REMARK 3 T13: 0.0150 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 1.0210 L22: 2.5360
REMARK 3 L33: 2.3083 L12: 0.3186
REMARK 3 L13: 0.7008 L23: 1.6182
REMARK 3 S TENSOR
REMARK 3 S11: -0.0527 S12: -0.2465 S13: 0.1571
REMARK 3 S21: 0.3328 S22: 0.0295 S23: 0.1033
REMARK 3 S31: 0.0833 S32: -0.2073 S33: 0.0232
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 25 B 160
REMARK 3 ORIGIN FOR THE GROUP (A): 26.1270 47.2260 41.2150
REMARK 3 T TENSOR
REMARK 3 T11: 0.0011 T22: 0.0098
REMARK 3 T33: -0.1866 T12: -0.0811
REMARK 3 T13: -0.0618 T23: 0.0615
REMARK 3 L TENSOR
REMARK 3 L11: 2.5773 L22: 2.1477
REMARK 3 L33: 0.4763 L12: 2.2468
REMARK 3 L13: -0.9469 L23: -0.6697
REMARK 3 S TENSOR
REMARK 3 S11: -0.2174 S12: 0.3249 S13: 0.1430
REMARK 3 S21: -0.2656 S22: 0.2585 S23: 0.2705
REMARK 3 S31: -0.0094 S32: -0.2097 S33: -0.0411
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 161 B 312
REMARK 3 ORIGIN FOR THE GROUP (A): 59.2260 39.3950 43.7110
REMARK 3 T TENSOR
REMARK 3 T11: -0.0066 T22: -0.0479
REMARK 3 T33: -0.1435 T12: -0.0103
REMARK 3 T13: 0.0709 T23: -0.0532
REMARK 3 L TENSOR
REMARK 3 L11: 1.6380 L22: 1.3212
REMARK 3 L33: 1.3398 L12: 0.2989
REMARK 3 L13: -0.5100 L23: -0.1628
REMARK 3 S TENSOR
REMARK 3 S11: -0.1501 S12: 0.1832 S13: -0.3249
REMARK 3 S21: -0.2750 S22: 0.1069 S23: -0.3602
REMARK 3 S31: 0.2232 S32: 0.2161 S33: 0.0433
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 324 B 416
REMARK 3 ORIGIN FOR THE GROUP (A): 48.0620 29.7050 17.3460
REMARK 3 T TENSOR
REMARK 3 T11: 0.5863 T22: 0.4942
REMARK 3 T33: 0.5615 T12: 0.0157
REMARK 3 T13: 0.0237 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 16.4299 L22: 0.5694
REMARK 3 L33: 26.9377 L12: 2.5973
REMARK 3 L13: -3.8348 L23: -2.6400
REMARK 3 S TENSOR
REMARK 3 S11: 0.3238 S12: 1.8757 S13: 0.6761
REMARK 3 S21: -0.0075 S22: 0.4375 S23: 0.4965
REMARK 3 S31: -0.5847 S32: -0.6096 S33: -0.7614
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 417 B 600
REMARK 3 ORIGIN FOR THE GROUP (A): 54.7770 27.0300 36.6860
REMARK 3 T TENSOR
REMARK 3 T11: 0.2246 T22: 0.0979
REMARK 3 T33: 0.0241 T12: -0.0550
REMARK 3 T13: 0.1304 T23: -0.1369
REMARK 3 L TENSOR
REMARK 3 L11: 2.5427 L22: 1.7264
REMARK 3 L33: 2.0611 L12: 0.1779
REMARK 3 L13: -1.3221 L23: 0.5137
REMARK 3 S TENSOR
REMARK 3 S11: -0.2567 S12: 0.7100 S13: -0.6354
REMARK 3 S21: -0.4203 S22: 0.1075 S23: -0.1718
REMARK 3 S31: 0.5214 S32: -0.2367 S33: 0.1491
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 2QR4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000043949.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97930
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53824
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 15.80
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 15.70
REMARK 200 R MERGE FOR SHELL (I) : 0.76400
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: NULL
REMARK 200 SOFTWARE USED: SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE PH 4.6, 1.0M
REMARK 280 SODIUM FORMATE, VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.80950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 66.57100
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 66.57100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 128.71425
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 66.57100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 66.57100
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 42.90475
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 66.57100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 66.57100
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 128.71425
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 66.57100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 66.57100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 42.90475
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 85.80950
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: 3560 ANGSTROM**2
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 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 MSE A 23
REMARK 465 SER A 24
REMARK 465 THR A 317
REMARK 465 PHE A 318
REMARK 465 THR A 319
REMARK 465 TYR A 320
REMARK 465 GLU A 321
REMARK 465 VAL A 342
REMARK 465 GLU A 343
REMARK 465 LYS A 344
REMARK 465 ALA A 345
REMARK 465 PHE A 346
REMARK 465 SER A 347
REMARK 465 GLU A 348
REMARK 465 ARG A 349
REMARK 465 TRP A 350
REMARK 465 ILE A 351
REMARK 465 ASP A 352
REMARK 465 VAL A 353
REMARK 465 VAL A 354
REMARK 465 GLU A 355
REMARK 465 ASN A 356
REMARK 465 LYS A 357
REMARK 465 GLY A 358
REMARK 465 LYS A 359
REMARK 465 ARG A 360
REMARK 465 SER A 361
REMARK 465 GLY A 362
REMARK 465 ALA A 363
REMARK 465 TYR A 364
REMARK 465 SER A 365
REMARK 465 SER A 366
REMARK 465 GLY A 367
REMARK 465 SER A 368
REMARK 465 TYR A 369
REMARK 465 ASP A 370
REMARK 465 THR A 371
REMARK 465 ASN A 372
REMARK 465 PRO A 373
REMARK 465 TYR A 374
REMARK 465 ILE A 375
REMARK 465 LEU A 376
REMARK 465 LEU A 377
REMARK 465 ASN A 378
REMARK 465 TRP A 379
REMARK 465 HIS A 380
REMARK 465 ASP A 381
REMARK 465 ARG A 403
REMARK 465 SER A 404
REMARK 465 ASN A 405
REMARK 465 GLN A 406
REMARK 465 PRO A 407
REMARK 465 TYR A 408
REMARK 465 VAL A 409
REMARK 465 TYR A 410
REMARK 465 GLY A 411
REMARK 465 ASP A 412
REMARK 465 TYR A 413
REMARK 465 SER A 414
REMARK 465 GLY A 603
REMARK 465 HIS A 604
REMARK 465 HIS A 605
REMARK 465 HIS A 606
REMARK 465 HIS A 607
REMARK 465 HIS A 608
REMARK 465 HIS A 609
REMARK 465 MSE B 23
REMARK 465 SER B 24
REMARK 465 GLU B 313
REMARK 465 ALA B 314
REMARK 465 PRO B 315
REMARK 465 ILE B 316
REMARK 465 THR B 317
REMARK 465 PHE B 318
REMARK 465 THR B 319
REMARK 465 TYR B 320
REMARK 465 GLU B 321
REMARK 465 GLU B 322
REMARK 465 ALA B 323
REMARK 465 ILE B 341
REMARK 465 VAL B 342
REMARK 465 GLU B 343
REMARK 465 LYS B 344
REMARK 465 ALA B 345
REMARK 465 PHE B 346
REMARK 465 SER B 347
REMARK 465 GLU B 348
REMARK 465 ARG B 349
REMARK 465 TRP B 350
REMARK 465 ILE B 351
REMARK 465 ASP B 352
REMARK 465 VAL B 353
REMARK 465 VAL B 354
REMARK 465 GLU B 355
REMARK 465 ASN B 356
REMARK 465 LYS B 357
REMARK 465 GLY B 358
REMARK 465 LYS B 359
REMARK 465 ARG B 360
REMARK 465 SER B 361
REMARK 465 GLY B 362
REMARK 465 ALA B 363
REMARK 465 TYR B 364
REMARK 465 SER B 365
REMARK 465 SER B 366
REMARK 465 GLY B 367
REMARK 465 SER B 368
REMARK 465 TYR B 369
REMARK 465 ASP B 370
REMARK 465 THR B 371
REMARK 465 ASN B 372
REMARK 465 PRO B 373
REMARK 465 TYR B 374
REMARK 465 ILE B 375
REMARK 465 LEU B 376
REMARK 465 LEU B 377
REMARK 465 ASN B 378
REMARK 465 TRP B 379
REMARK 465 HIS B 380
REMARK 465 ASP B 381
REMARK 465 THR B 382
REMARK 465 PHE B 401
REMARK 465 THR B 402
REMARK 465 ARG B 403
REMARK 465 SER B 404
REMARK 465 ASN B 405
REMARK 465 GLN B 406
REMARK 465 PRO B 407
REMARK 465 TYR B 408
REMARK 465 VAL B 409
REMARK 465 TYR B 410
REMARK 465 GLY B 411
REMARK 465 ASP B 412
REMARK 465 TYR B 413
REMARK 465 SER B 414
REMARK 465 ALA B 558
REMARK 465 GLY B 559
REMARK 465 ASN B 560
REMARK 465 ARG B 601
REMARK 465 GLU B 602
REMARK 465 GLY B 603
REMARK 465 HIS B 604
REMARK 465 HIS B 605
REMARK 465 HIS B 606
REMARK 465 HIS B 607
REMARK 465 HIS B 608
REMARK 465 HIS B 609
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 GLU A 313 OE1 OE2
REMARK 470 LYS A 324 CG CD CE NZ
REMARK 470 GLU A 325 CD OE1 OE2
REMARK 470 GLU A 336 CD OE1 OE2
REMARK 470 ILE A 341 CG1 CG2 CD1
REMARK 470 GLU A 547 CG CD OE1 OE2
REMARK 470 LYS B 324 CG CD CE NZ
REMARK 470 GLU B 325 CG CD OE1 OE2
REMARK 470 LEU B 328 CG CD1 CD2
REMARK 470 LEU B 331 CD1 CD2
REMARK 470 LYS B 332 CE NZ
REMARK 470 GLU B 336 CD OE1 OE2
REMARK 470 TYR B 338 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 383 CG CD1 CD2
REMARK 470 LEU B 389 CG CD1 CD2
REMARK 470 GLU B 392 OE2
REMARK 470 MSE B 393 CG SE CE
REMARK 470 TYR B 400 CD2 CE1 CE2 CZ OH
REMARK 470 ILE B 415 CG2 CD1
REMARK 470 TYR B 432 CE1 CE2 CZ OH
REMARK 470 GLN B 544 CD OE1 NE2
REMARK 470 GLU B 547 OE1 OE2
REMARK 470 LEU B 549 CD1 CD2
REMARK 470 LEU B 553 CD1
REMARK 470 LYS B 557 CD CE NZ
REMARK 470 LYS B 570 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU B 435 CD GLU B 435 OE1 0.101
REMARK 500 GLU B 435 CD GLU B 435 OE2 0.076
REMARK 500 THR B 436 CB THR B 436 OG1 -0.149
REMARK 500 GLU B 437 CG GLU B 437 CD 0.099
REMARK 500 GLU B 437 CD GLU B 437 OE1 0.151
REMARK 500 GLU B 437 CD GLU B 437 OE2 0.143
REMARK 500 LYS B 438 C LYS B 438 O 0.126
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 GLU B 437 OE1 - CD - OE2 ANGL. DEV. = -10.3 DEGREES
REMARK 500 GLU B 437 CG - CD - OE2 ANGL. DEV. = 14.0 DEGREES
REMARK 500 PRO B 500 C - N - CA ANGL. DEV. = 11.0 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 LEU A 153 -166.24 -105.78
REMARK 500 ASN A 263 7.02 -68.36
REMARK 500 GLU A 313 123.91 60.23
REMARK 500 TYR A 520 -139.12 -93.12
REMARK 500 ASN A 521 78.65 -151.79
REMARK 500 GLN A 544 57.45 38.80
REMARK 500 LYS B 42 -5.36 -56.33
REMARK 500 ASP B 86 58.40 -153.86
REMARK 500 GLU B 191 33.11 -77.01
REMARK 500 ASN B 192 -155.24 -141.00
REMARK 500 LEU B 311 -165.92 -115.75
REMARK 500 MSE B 339 -75.54 -44.27
REMARK 500 TYR B 520 -143.26 -83.25
REMARK 500 ASN B 521 78.27 -150.17
REMARK 500 GLN B 544 70.22 51.68
REMARK 500 PRO B 546 -71.35 -19.64
REMARK 500 LEU B 553 23.26 -76.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-10379L RELATED DB: TARGETDB
DBREF 2QR4 A 26 601 UNP Q3XYC8 Q3XYC8_ENTFC 26 601
DBREF 2QR4 B 26 601 UNP Q3XYC8 Q3XYC8_ENTFC 26 601
SEQADV 2QR4 MSE A 23 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 SER A 24 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 LEU A 25 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 GLU A 602 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 GLY A 603 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 HIS A 604 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 HIS A 605 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 HIS A 606 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 HIS A 607 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 HIS A 608 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 HIS A 609 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 MSE B 23 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 SER B 24 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 LEU B 25 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 GLU B 602 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 GLY B 603 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 HIS B 604 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 HIS B 605 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 HIS B 606 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 HIS B 607 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 HIS B 608 UNP Q3XYC8 EXPRESSION TAG
SEQADV 2QR4 HIS B 609 UNP Q3XYC8 EXPRESSION TAG
SEQRES 1 A 587 MSE SER LEU SER ASP GLN GLU PHE ASP GLU LYS TYR LEU
SEQRES 2 A 587 GLU LEU SER GLU GLU LEU LYS GLN SER GLU LYS HIS LYS
SEQRES 3 A 587 GLY THR LEU ASP GLN GLY ALA SER GLN PHE LEU ASN ALA
SEQRES 4 A 587 ILE GLU PHE VAL LEU ARG VAL TYR ARG GLN THR GLU VAL
SEQRES 5 A 587 ILE TYR VAL TYR ALA HIS LEU LYS ASN ASP GLN ASP THR
SEQRES 6 A 587 GLY ASN THR ASP TYR GLN ALA LEU TYR ALA ARG ALA SER
SEQRES 7 A 587 SER LEU PHE SER LYS VAL SER GLU ALA VAL SER TRP PHE
SEQRES 8 A 587 GLU PRO GLU ILE LEU GLN LEU SER ASP ASP GLN ILE TRP
SEQRES 9 A 587 GLN TYR PHE LYS GLU GLU PRO LYS LEU GLU VAL TYR ARG
SEQRES 10 A 587 HIS TYR ILE GLN GLN ILE VAL ASP ASN ARG ALA HIS VAL
SEQRES 11 A 587 LEU SER ALA GLU GLN GLU SER LEU LEU ALA GLY ALA GLY
SEQRES 12 A 587 GLU ILE PHE ASP ALA SER SER ASP THR PHE ALA VAL LEU
SEQRES 13 A 587 ASN ASN ALA ASP LEU VAL PHE PRO THR ILE GLU GLY GLU
SEQRES 14 A 587 ASN GLY GLU ILE VAL GLN LEU SER HIS GLY VAL TYR GLY
SEQRES 15 A 587 GLN LEU LEU GLU SER THR ASP ARG ARG VAL ARG GLU ALA
SEQRES 16 A 587 ALA PHE LYS GLY LEU TYR SER VAL TYR GLU GLN PHE ARG
SEQRES 17 A 587 ASN THR PHE ALA SER THR LEU GLY THR HIS ILE LYS GLY
SEQRES 18 A 587 HIS ASN PHE LYS ALA LYS VAL ARG ASN TYR SER SER ALA
SEQRES 19 A 587 ARG GLU ALA SER LEU SER ASN ASN HIS ILE PRO GLU SER
SEQRES 20 A 587 VAL TYR ASP THR LEU VAL ASP VAL VAL ASN LYS HIS LEU
SEQRES 21 A 587 PRO LEU LEU HIS ARG TYR MSE GLU LEU ARG LYS ARG LEU
SEQRES 22 A 587 LEU GLU VAL GLU LYS LEU HIS MSE TYR ASP LEU TYR THR
SEQRES 23 A 587 PRO VAL LEU GLY GLU ALA PRO ILE THR PHE THR TYR GLU
SEQRES 24 A 587 GLU ALA LYS GLU LYS ALA LEU GLU ALA LEU LYS PRO MSE
SEQRES 25 A 587 GLY GLU GLU TYR MSE ALA ILE VAL GLU LYS ALA PHE SER
SEQRES 26 A 587 GLU ARG TRP ILE ASP VAL VAL GLU ASN LYS GLY LYS ARG
SEQRES 27 A 587 SER GLY ALA TYR SER SER GLY SER TYR ASP THR ASN PRO
SEQRES 28 A 587 TYR ILE LEU LEU ASN TRP HIS ASP THR LEU ASP GLN LEU
SEQRES 29 A 587 PHE THR LEU VAL HIS GLU MSE GLY HIS SER VAL HIS SER
SEQRES 30 A 587 TYR PHE THR ARG SER ASN GLN PRO TYR VAL TYR GLY ASP
SEQRES 31 A 587 TYR SER ILE PHE LEU ALA GLU ILE ALA SER THR THR ASN
SEQRES 32 A 587 GLU ASN ILE LEU THR GLU TYR LEU LEU GLU THR GLU LYS
SEQRES 33 A 587 ASP PRO ARG VAL ARG ALA TYR VAL LEU ASN HIS TYR LEU
SEQRES 34 A 587 ASP GLY PHE LYS GLY THR VAL PHE ARG GLN THR GLN PHE
SEQRES 35 A 587 ALA GLU PHE GLU HIS PHE MSE HIS THR GLU ASP GLU LYS
SEQRES 36 A 587 GLY VAL PRO LEU THR SER GLU TYR LEU SER ASP SER TYR
SEQRES 37 A 587 GLY LYS LEU ASN ALA LYS TYR TYR GLY PRO ALA VAL GLU
SEQRES 38 A 587 GLU ASP PRO GLU ILE LYS PHE GLU TRP SER ARG ILE PRO
SEQRES 39 A 587 HIS PHE TYR TYR ASN TYR TYR VAL PHE GLN TYR SER THR
SEQRES 40 A 587 GLY PHE SER ALA ALA SER ALA LEU ALA LYS LYS ILE LEU
SEQRES 41 A 587 ASN GLN GLU PRO GLU ALA LEU GLU ASN TYR LEU ALA TYR
SEQRES 42 A 587 LEU LYS ALA GLY ASN SER ASP TYR PRO VAL GLU VAL MSE
SEQRES 43 A 587 LYS LYS ALA GLY VAL ASP MSE THR GLN ALA ALA TYR ILE
SEQRES 44 A 587 GLU ASP ALA MSE SER MSE PHE GLU GLN ARG LEU ASN GLU
SEQRES 45 A 587 LEU GLU GLU LEU ILE ASP ARG GLU GLY HIS HIS HIS HIS
SEQRES 46 A 587 HIS HIS
SEQRES 1 B 587 MSE SER LEU SER ASP GLN GLU PHE ASP GLU LYS TYR LEU
SEQRES 2 B 587 GLU LEU SER GLU GLU LEU LYS GLN SER GLU LYS HIS LYS
SEQRES 3 B 587 GLY THR LEU ASP GLN GLY ALA SER GLN PHE LEU ASN ALA
SEQRES 4 B 587 ILE GLU PHE VAL LEU ARG VAL TYR ARG GLN THR GLU VAL
SEQRES 5 B 587 ILE TYR VAL TYR ALA HIS LEU LYS ASN ASP GLN ASP THR
SEQRES 6 B 587 GLY ASN THR ASP TYR GLN ALA LEU TYR ALA ARG ALA SER
SEQRES 7 B 587 SER LEU PHE SER LYS VAL SER GLU ALA VAL SER TRP PHE
SEQRES 8 B 587 GLU PRO GLU ILE LEU GLN LEU SER ASP ASP GLN ILE TRP
SEQRES 9 B 587 GLN TYR PHE LYS GLU GLU PRO LYS LEU GLU VAL TYR ARG
SEQRES 10 B 587 HIS TYR ILE GLN GLN ILE VAL ASP ASN ARG ALA HIS VAL
SEQRES 11 B 587 LEU SER ALA GLU GLN GLU SER LEU LEU ALA GLY ALA GLY
SEQRES 12 B 587 GLU ILE PHE ASP ALA SER SER ASP THR PHE ALA VAL LEU
SEQRES 13 B 587 ASN ASN ALA ASP LEU VAL PHE PRO THR ILE GLU GLY GLU
SEQRES 14 B 587 ASN GLY GLU ILE VAL GLN LEU SER HIS GLY VAL TYR GLY
SEQRES 15 B 587 GLN LEU LEU GLU SER THR ASP ARG ARG VAL ARG GLU ALA
SEQRES 16 B 587 ALA PHE LYS GLY LEU TYR SER VAL TYR GLU GLN PHE ARG
SEQRES 17 B 587 ASN THR PHE ALA SER THR LEU GLY THR HIS ILE LYS GLY
SEQRES 18 B 587 HIS ASN PHE LYS ALA LYS VAL ARG ASN TYR SER SER ALA
SEQRES 19 B 587 ARG GLU ALA SER LEU SER ASN ASN HIS ILE PRO GLU SER
SEQRES 20 B 587 VAL TYR ASP THR LEU VAL ASP VAL VAL ASN LYS HIS LEU
SEQRES 21 B 587 PRO LEU LEU HIS ARG TYR MSE GLU LEU ARG LYS ARG LEU
SEQRES 22 B 587 LEU GLU VAL GLU LYS LEU HIS MSE TYR ASP LEU TYR THR
SEQRES 23 B 587 PRO VAL LEU GLY GLU ALA PRO ILE THR PHE THR TYR GLU
SEQRES 24 B 587 GLU ALA LYS GLU LYS ALA LEU GLU ALA LEU LYS PRO MSE
SEQRES 25 B 587 GLY GLU GLU TYR MSE ALA ILE VAL GLU LYS ALA PHE SER
SEQRES 26 B 587 GLU ARG TRP ILE ASP VAL VAL GLU ASN LYS GLY LYS ARG
SEQRES 27 B 587 SER GLY ALA TYR SER SER GLY SER TYR ASP THR ASN PRO
SEQRES 28 B 587 TYR ILE LEU LEU ASN TRP HIS ASP THR LEU ASP GLN LEU
SEQRES 29 B 587 PHE THR LEU VAL HIS GLU MSE GLY HIS SER VAL HIS SER
SEQRES 30 B 587 TYR PHE THR ARG SER ASN GLN PRO TYR VAL TYR GLY ASP
SEQRES 31 B 587 TYR SER ILE PHE LEU ALA GLU ILE ALA SER THR THR ASN
SEQRES 32 B 587 GLU ASN ILE LEU THR GLU TYR LEU LEU GLU THR GLU LYS
SEQRES 33 B 587 ASP PRO ARG VAL ARG ALA TYR VAL LEU ASN HIS TYR LEU
SEQRES 34 B 587 ASP GLY PHE LYS GLY THR VAL PHE ARG GLN THR GLN PHE
SEQRES 35 B 587 ALA GLU PHE GLU HIS PHE MSE HIS THR GLU ASP GLU LYS
SEQRES 36 B 587 GLY VAL PRO LEU THR SER GLU TYR LEU SER ASP SER TYR
SEQRES 37 B 587 GLY LYS LEU ASN ALA LYS TYR TYR GLY PRO ALA VAL GLU
SEQRES 38 B 587 GLU ASP PRO GLU ILE LYS PHE GLU TRP SER ARG ILE PRO
SEQRES 39 B 587 HIS PHE TYR TYR ASN TYR TYR VAL PHE GLN TYR SER THR
SEQRES 40 B 587 GLY PHE SER ALA ALA SER ALA LEU ALA LYS LYS ILE LEU
SEQRES 41 B 587 ASN GLN GLU PRO GLU ALA LEU GLU ASN TYR LEU ALA TYR
SEQRES 42 B 587 LEU LYS ALA GLY ASN SER ASP TYR PRO VAL GLU VAL MSE
SEQRES 43 B 587 LYS LYS ALA GLY VAL ASP MSE THR GLN ALA ALA TYR ILE
SEQRES 44 B 587 GLU ASP ALA MSE SER MSE PHE GLU GLN ARG LEU ASN GLU
SEQRES 45 B 587 LEU GLU GLU LEU ILE ASP ARG GLU GLY HIS HIS HIS HIS
SEQRES 46 B 587 HIS HIS
MODRES 2QR4 MSE A 289 MET SELENOMETHIONINE
MODRES 2QR4 MSE A 303 MET SELENOMETHIONINE
MODRES 2QR4 MSE A 334 MET SELENOMETHIONINE
MODRES 2QR4 MSE A 339 MET SELENOMETHIONINE
MODRES 2QR4 MSE A 393 MET SELENOMETHIONINE
MODRES 2QR4 MSE A 471 MET SELENOMETHIONINE
MODRES 2QR4 MSE A 568 MET SELENOMETHIONINE
MODRES 2QR4 MSE A 575 MET SELENOMETHIONINE
MODRES 2QR4 MSE A 585 MET SELENOMETHIONINE
MODRES 2QR4 MSE A 587 MET SELENOMETHIONINE
MODRES 2QR4 MSE B 289 MET SELENOMETHIONINE
MODRES 2QR4 MSE B 303 MET SELENOMETHIONINE
MODRES 2QR4 MSE B 334 MET SELENOMETHIONINE
MODRES 2QR4 MSE B 339 MET SELENOMETHIONINE
MODRES 2QR4 MSE B 393 MET SELENOMETHIONINE
MODRES 2QR4 MSE B 471 MET SELENOMETHIONINE
MODRES 2QR4 MSE B 568 MET SELENOMETHIONINE
MODRES 2QR4 MSE B 575 MET SELENOMETHIONINE
MODRES 2QR4 MSE B 585 MET SELENOMETHIONINE
MODRES 2QR4 MSE B 587 MET SELENOMETHIONINE
HET MSE A 289 8
HET MSE A 303 8
HET MSE A 334 8
HET MSE A 339 8
HET MSE A 393 8
HET MSE A 471 8
HET MSE A 568 8
HET MSE A 575 8
HET MSE A 585 8
HET MSE A 587 8
HET MSE B 289 8
HET MSE B 303 8
HET MSE B 334 8
HET MSE B 339 8
HET MSE B 393 5
HET MSE B 471 8
HET MSE B 568 8
HET MSE B 575 8
HET MSE B 585 8
HET MSE B 587 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 3 HOH *188(H2 O)
HELIX 1 1 LEU A 25 LEU A 41 1 17
HELIX 2 2 GLN A 43 LYS A 48 1 6
HELIX 3 3 THR A 50 GLN A 53 5 4
HELIX 4 4 GLY A 54 ASP A 86 1 33
HELIX 5 5 ASN A 89 VAL A 110 1 22
HELIX 6 6 TRP A 112 LEU A 118 1 7
HELIX 7 7 SER A 121 GLU A 132 1 12
HELIX 8 8 PRO A 133 VAL A 137 5 5
HELIX 9 9 TYR A 138 ASP A 147 1 10
HELIX 10 10 ASN A 148 VAL A 152 5 5
HELIX 11 11 SER A 154 ALA A 164 1 11
HELIX 12 12 ALA A 164 ALA A 181 1 18
HELIX 13 13 SER A 199 GLU A 208 1 10
HELIX 14 14 ASP A 211 PHE A 229 1 19
HELIX 15 15 PHE A 229 ARG A 251 1 23
HELIX 16 16 SER A 255 ASN A 263 1 9
HELIX 17 17 PRO A 267 HIS A 281 1 15
HELIX 18 18 HIS A 281 GLU A 297 1 17
HELIX 19 19 HIS A 302 LEU A 306 5 5
HELIX 20 20 ALA A 323 LEU A 331 1 9
HELIX 21 21 MSE A 334 ILE A 341 1 8
HELIX 22 22 THR A 382 THR A 402 1 21
HELIX 23 23 ILE A 415 GLU A 437 1 23
HELIX 24 24 ASP A 439 VAL A 458 1 20
HELIX 25 25 VAL A 458 LYS A 477 1 20
HELIX 26 26 THR A 482 GLY A 499 1 18
HELIX 27 27 ASP A 505 TYR A 520 5 16
HELIX 28 28 VAL A 524 ASN A 543 1 20
HELIX 29 29 GLU A 547 GLY A 559 1 13
HELIX 30 30 TYR A 563 ALA A 571 1 9
HELIX 31 31 ALA A 578 GLU A 602 1 25
HELIX 32 32 SER B 26 LEU B 41 1 16
HELIX 33 33 LYS B 42 SER B 44 5 3
HELIX 34 34 GLY B 54 ASP B 86 1 33
HELIX 35 35 ASN B 89 VAL B 110 1 22
HELIX 36 36 TRP B 112 LEU B 118 1 7
HELIX 37 37 SER B 121 GLU B 132 1 12
HELIX 38 38 PRO B 133 VAL B 137 5 5
HELIX 39 39 TYR B 138 ASP B 147 1 10
HELIX 40 40 ASN B 148 VAL B 152 5 5
HELIX 41 41 SER B 154 ALA B 164 1 11
HELIX 42 42 ALA B 164 ALA B 181 1 18
HELIX 43 43 SER B 199 SER B 209 1 11
HELIX 44 44 ASP B 211 PHE B 229 1 19
HELIX 45 45 PHE B 229 ARG B 251 1 23
HELIX 46 46 SER B 255 ASN B 263 1 9
HELIX 47 47 PRO B 267 HIS B 281 1 15
HELIX 48 48 HIS B 281 GLU B 297 1 17
HELIX 49 49 HIS B 302 LEU B 306 5 5
HELIX 50 50 GLU B 325 LEU B 331 1 7
HELIX 51 51 LYS B 332 MSE B 334 5 3
HELIX 52 52 GLY B 335 ALA B 340 1 6
HELIX 53 53 LEU B 383 HIS B 398 1 16
HELIX 54 54 ILE B 415 GLU B 437 1 23
HELIX 55 55 ASP B 439 VAL B 458 1 20
HELIX 56 56 VAL B 458 GLY B 478 1 21
HELIX 57 57 THR B 482 GLY B 499 1 18
HELIX 58 58 ASP B 505 TYR B 520 5 16
HELIX 59 59 VAL B 524 ASN B 543 1 20
HELIX 60 60 GLU B 547 LEU B 556 1 10
HELIX 61 61 TYR B 563 ALA B 571 1 9
HELIX 62 62 ALA B 578 ASP B 600 1 23
SHEET 1 A 2 THR A 187 GLU A 189 0
SHEET 2 A 2 ILE A 195 GLN A 197 -1 O VAL A 196 N ILE A 188
SHEET 1 B 2 THR B 187 GLU B 189 0
SHEET 2 B 2 ILE B 195 GLN B 197 -1 O VAL B 196 N ILE B 188
LINK C TYR A 288 N MSE A 289 1555 1555 1.33
LINK C MSE A 289 N GLU A 290 1555 1555 1.33
LINK C HIS A 302 N MSE A 303 1555 1555 1.33
LINK C MSE A 303 N TYR A 304 1555 1555 1.33
LINK C PRO A 333 N MSE A 334 1555 1555 1.33
LINK C MSE A 334 N GLY A 335 1555 1555 1.33
LINK C TYR A 338 N MSE A 339 1555 1555 1.33
LINK C MSE A 339 N ALA A 340 1555 1555 1.33
LINK C GLU A 392 N MSE A 393 1555 1555 1.33
LINK C MSE A 393 N GLY A 394 1555 1555 1.33
LINK C PHE A 470 N MSE A 471 1555 1555 1.33
LINK C MSE A 471 N HIS A 472 1555 1555 1.34
LINK C VAL A 567 N MSE A 568 1555 1555 1.33
LINK C MSE A 568 N LYS A 569 1555 1555 1.33
LINK C ASP A 574 N MSE A 575 1555 1555 1.33
LINK C MSE A 575 N THR A 576 1555 1555 1.33
LINK C ALA A 584 N MSE A 585 1555 1555 1.33
LINK C MSE A 585 N SER A 586 1555 1555 1.32
LINK C SER A 586 N MSE A 587 1555 1555 1.32
LINK C MSE A 587 N PHE A 588 1555 1555 1.33
LINK C TYR B 288 N MSE B 289 1555 1555 1.33
LINK C MSE B 289 N GLU B 290 1555 1555 1.33
LINK C HIS B 302 N MSE B 303 1555 1555 1.33
LINK C MSE B 303 N TYR B 304 1555 1555 1.33
LINK C PRO B 333 N MSE B 334 1555 1555 1.33
LINK C MSE B 334 N GLY B 335 1555 1555 1.33
LINK C TYR B 338 N MSE B 339 1555 1555 1.33
LINK C MSE B 339 N ALA B 340 1555 1555 1.33
LINK C GLU B 392 N MSE B 393 1555 1555 1.33
LINK C MSE B 393 N GLY B 394 1555 1555 1.33
LINK C PHE B 470 N MSE B 471 1555 1555 1.33
LINK C MSE B 471 N HIS B 472 1555 1555 1.33
LINK C VAL B 567 N MSE B 568 1555 1555 1.33
LINK C MSE B 568 N LYS B 569 1555 1555 1.33
LINK C ASP B 574 N MSE B 575 1555 1555 1.33
LINK C MSE B 575 N THR B 576 1555 1555 1.33
LINK C ALA B 584 N MSE B 585 1555 1555 1.33
LINK C MSE B 585 N SER B 586 1555 1555 1.33
LINK C SER B 586 N MSE B 587 1555 1555 1.33
LINK C MSE B 587 N PHE B 588 1555 1555 1.33
CRYST1 133.142 133.142 171.619 90.00 90.00 90.00 P 43 21 2 16
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 0.007511 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007511 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005827 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
