HEADER TRANSFERASE 27-MAR-06 2GHR
TITLE CRYSTAL STRUCTURE OF HOMOSERINE O-SUCCINYLTRANSFERASE (NP_981826.1)
TITLE 2 FROM BACILLUS CEREUS ATCC 10987 AT 2.40 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMOSERINE O-SUCCINYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HOMOSERINE O- TRANSSUCCINYLASE, HTS;
COMPND 5 EC: 2.3.1.46;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS CEREUS;
SOURCE 3 ORGANISM_TAXID: 1396;
SOURCE 4 ATCC: 10987;
SOURCE 5 GENE: META;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS NP_981826.1, HOMOSERINE O-SUCCINYLTRANSFERASE, STRUCTURAL GENOMICS,
KEYWDS 2 JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE, PSI, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 6 25-JAN-23 2GHR 1 REMARK SEQADV LINK
REVDAT 5 13-JUL-11 2GHR 1 VERSN
REVDAT 4 24-FEB-09 2GHR 1 VERSN
REVDAT 3 28-AUG-07 2GHR 1 JRNL
REVDAT 2 31-OCT-06 2GHR 1 JRNL KEYWDS MASTER REMARK
REVDAT 2 2 1 DBREF SEQADV TITLE
REVDAT 1 11-APR-06 2GHR 0
JRNL AUTH C.ZUBIETA,S.S.KRISHNA,D.MCMULLAN,M.D.MILLER,P.ABDUBEK,
JRNL AUTH 2 S.AGARWALLA,E.AMBING,T.ASTAKHOVA,H.L.AXELROD,D.CARLTON,
JRNL AUTH 3 H.J.CHIU,T.CLAYTON,M.DELLER,M.DIDONATO,L.DUAN,M.A.ELSLIGER,
JRNL AUTH 4 S.K.GRZECHNIK,J.HALE,E.HAMPTON,G.W.HAN,J.HAUGEN,
JRNL AUTH 5 L.JAROSZEWSKI,K.K.JIN,H.E.KLOCK,M.W.KNUTH,E.KOESEMA,A.KUMAR,
JRNL AUTH 6 D.MARCIANO,A.T.MORSE,E.NIGOGHOSSIAN,S.OOMMACHEN,R.REYES,
JRNL AUTH 7 C.L.RIFE,H.V.BEDEM,D.WEEKES,A.WHITE,Q.XU,K.O.HODGSON,
JRNL AUTH 8 J.WOOLEY,A.M.DEACON,A.GODZIK,S.A.LESLEY,I.A.WILSON
JRNL TITL CRYSTAL STRUCTURE OF HOMOSERINE O-SUCCINYLTRANSFERASE FROM
JRNL TITL 2 BACILLUS CEREUS AT 2.4 A RESOLUTION
JRNL REF PROTEINS V. 68 999 2007
JRNL REFN ISSN 0887-3585
JRNL PMID 17546672
JRNL DOI 10.1002/PROT.21208
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 13291
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 : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 699
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 985
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE SET COUNT : 47
REMARK 3 BIN FREE R VALUE : 0.3660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2210
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 78
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 38.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : -0.02000
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): 0.346
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.255
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.186
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.028
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2265 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1990 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3060 ; 0.742 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4631 ; 0.513 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 267 ; 5.377 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 122 ;29.140 ;24.426
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 400 ;13.183 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;14.566 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 326 ; 0.049 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2511 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 470 ; 0.000 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 415 ; 0.204 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1959 ; 0.195 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1079 ; 0.187 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1251 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 78 ; 0.151 ; 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): 17 ; 0.136 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 63 ; 0.252 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.193 ; 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): 1368 ; 1.632 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 546 ; 0.358 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2148 ; 2.593 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1013 ; 4.574 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 912 ; 6.421 ;11.000
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
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 17 A 27
REMARK 3 ORIGIN FOR THE GROUP (A): 48.6630 25.0210 77.7560
REMARK 3 T TENSOR
REMARK 3 T11: 0.3171 T22: 0.4310
REMARK 3 T33: 0.2373 T12: 0.0101
REMARK 3 T13: 0.0175 T23: -0.0824
REMARK 3 L TENSOR
REMARK 3 L11: 28.0710 L22: 9.8223
REMARK 3 L33: 12.3047 L12: -10.1292
REMARK 3 L13: 1.7884 L23: -5.0271
REMARK 3 S TENSOR
REMARK 3 S11: -0.6366 S12: -0.5527 S13: 0.5124
REMARK 3 S21: 0.1546 S22: 0.1609 S23: -0.8333
REMARK 3 S31: 0.7473 S32: 1.2767 S33: 0.4757
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 28 A 37
REMARK 3 ORIGIN FOR THE GROUP (A): 37.5200 38.6500 57.6450
REMARK 3 T TENSOR
REMARK 3 T11: 0.0899 T22: 0.6033
REMARK 3 T33: 0.0702 T12: -0.1605
REMARK 3 T13: -0.1057 T23: -0.0517
REMARK 3 L TENSOR
REMARK 3 L11: 2.4284 L22: 12.9902
REMARK 3 L33: 0.3216 L12: -0.6969
REMARK 3 L13: -0.7187 L23: -0.9741
REMARK 3 S TENSOR
REMARK 3 S11: 0.1582 S12: -0.8649 S13: -0.0120
REMARK 3 S21: 1.0715 S22: -0.0059 S23: -0.8659
REMARK 3 S31: -1.0130 S32: 1.6445 S33: -0.1524
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 38 A 53
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1930 38.3030 51.0290
REMARK 3 T TENSOR
REMARK 3 T11: 0.2186 T22: 0.1641
REMARK 3 T33: 0.2526 T12: 0.0933
REMARK 3 T13: -0.0540 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 3.8145 L22: 3.2634
REMARK 3 L33: 17.1759 L12: 2.9284
REMARK 3 L13: -4.9613 L23: -0.5093
REMARK 3 S TENSOR
REMARK 3 S11: -0.1851 S12: 0.2549 S13: 0.9573
REMARK 3 S21: 0.3499 S22: 0.1547 S23: 0.6561
REMARK 3 S31: -0.8250 S32: -1.6354 S33: 0.0304
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 54 A 87
REMARK 3 ORIGIN FOR THE GROUP (A): 21.6930 39.7560 52.8490
REMARK 3 T TENSOR
REMARK 3 T11: 0.2443 T22: 0.0850
REMARK 3 T33: 0.2111 T12: 0.0128
REMARK 3 T13: -0.0168 T23: -0.0406
REMARK 3 L TENSOR
REMARK 3 L11: 2.2800 L22: 3.8280
REMARK 3 L33: 7.4583 L12: 1.8544
REMARK 3 L13: -0.1669 L23: 0.7865
REMARK 3 S TENSOR
REMARK 3 S11: -0.0397 S12: -0.1636 S13: 0.1017
REMARK 3 S21: 0.0110 S22: 0.1756 S23: 0.0731
REMARK 3 S31: -0.7372 S32: -0.2484 S33: -0.1359
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 : A 88 A 160
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5450 32.3020 39.3370
REMARK 3 T TENSOR
REMARK 3 T11: 0.1684 T22: 0.0853
REMARK 3 T33: 0.0384 T12: 0.0097
REMARK 3 T13: -0.0714 T23: 0.0482
REMARK 3 L TENSOR
REMARK 3 L11: 3.7287 L22: 2.1508
REMARK 3 L33: 2.9539 L12: 1.8002
REMARK 3 L13: 0.4659 L23: 0.5161
REMARK 3 S TENSOR
REMARK 3 S11: -0.1900 S12: 0.2986 S13: 0.2735
REMARK 3 S21: -0.2808 S22: 0.1821 S23: 0.0267
REMARK 3 S31: -0.3691 S32: 0.1150 S33: 0.0079
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 : A 161 A 225
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9040 16.1540 50.4410
REMARK 3 T TENSOR
REMARK 3 T11: 0.2011 T22: 0.0868
REMARK 3 T33: 0.0890 T12: 0.0456
REMARK 3 T13: -0.0618 T23: 0.0512
REMARK 3 L TENSOR
REMARK 3 L11: 2.6952 L22: 1.4863
REMARK 3 L33: 3.3515 L12: -0.1241
REMARK 3 L13: 0.1731 L23: 0.6488
REMARK 3 S TENSOR
REMARK 3 S11: 0.0177 S12: 0.0499 S13: -0.4063
REMARK 3 S21: 0.0449 S22: 0.0034 S23: -0.0969
REMARK 3 S31: 0.4499 S32: 0.1019 S33: -0.0211
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 : A 226 A 242
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7970 26.4350 51.4990
REMARK 3 T TENSOR
REMARK 3 T11: 0.1598 T22: 0.0624
REMARK 3 T33: 0.1701 T12: 0.0265
REMARK 3 T13: -0.0343 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 5.5384 L22: 1.0178
REMARK 3 L33: 4.1737 L12: -1.3405
REMARK 3 L13: 0.3477 L23: 0.7011
REMARK 3 S TENSOR
REMARK 3 S11: -0.0308 S12: -0.1765 S13: 0.1927
REMARK 3 S21: 0.1430 S22: 0.0484 S23: -0.2098
REMARK 3 S31: 0.4585 S32: 0.0927 S33: -0.0176
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 : A 243 A 256
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2610 28.6250 55.1290
REMARK 3 T TENSOR
REMARK 3 T11: 0.0732 T22: 0.2463
REMARK 3 T33: -0.0003 T12: 0.0592
REMARK 3 T13: -0.0642 T23: -0.0452
REMARK 3 L TENSOR
REMARK 3 L11: 23.3415 L22: 1.9991
REMARK 3 L33: 16.1805 L12: -4.4326
REMARK 3 L13: 10.3675 L23: -5.3476
REMARK 3 S TENSOR
REMARK 3 S11: 0.0289 S12: -0.4335 S13: 0.0540
REMARK 3 S21: -0.0322 S22: 0.0055 S23: -0.0950
REMARK 3 S31: -0.4081 S32: -1.1725 S33: -0.0344
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 257 A 292
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4500 23.6780 61.2580
REMARK 3 T TENSOR
REMARK 3 T11: 0.1651 T22: 0.1357
REMARK 3 T33: 0.0153 T12: 0.0227
REMARK 3 T13: -0.0618 T23: 0.0454
REMARK 3 L TENSOR
REMARK 3 L11: 3.6374 L22: 0.9298
REMARK 3 L33: 2.8970 L12: -0.3393
REMARK 3 L13: 0.4096 L23: 0.2319
REMARK 3 S TENSOR
REMARK 3 S11: 0.0415 S12: -0.6905 S13: -0.1856
REMARK 3 S21: 0.2434 S22: -0.0914 S23: 0.0479
REMARK 3 S31: 0.1712 S32: -0.2674 S33: 0.0500
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 293 A 297
REMARK 3 ORIGIN FOR THE GROUP (A): 37.6540 31.1930 51.5290
REMARK 3 T TENSOR
REMARK 3 T11: -0.0119 T22: 0.1634
REMARK 3 T33: 0.3034 T12: 0.1317
REMARK 3 T13: -0.0455 T23: -0.0656
REMARK 3 L TENSOR
REMARK 3 L11: 23.5171 L22: 30.4796
REMARK 3 L33: 54.0625 L12: 14.9041
REMARK 3 L13: 10.9058 L23: -25.1940
REMARK 3 S TENSOR
REMARK 3 S11: -1.7710 S12: -1.1767 S13: -1.7869
REMARK 3 S21: -0.6399 S22: 0.8740 S23: -2.0869
REMARK 3 S31: 1.6202 S32: 3.4994 S33: 0.8969
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. THE MAIN CHAIN AT PRO45 MAY NOT BE
REMARK 3 RELIABLE. 3. DUE TO WEAK DENSITY DUE TO A STRONG ICE RING, 263
REMARK 3 REFLECTIONS BETWEEN 3.63-3.71 ANGSTROMS WERE OMITTED FROM THE
REMARK 3 FINAL REFINEMENT. 4. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY
REMARK 4
REMARK 4 2GHR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037133.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL1-5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918381, 0.979094,0.978532
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : 1M LONG RH COATED BENT
REMARK 200 CYLINDRICAL MIRROR FOR
REMARK 200 HORIZONTAL AND VERTICAL FOCUSSING
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14274
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 29.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : 0.12400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.59200
REMARK 200 R SYM FOR SHELL (I) : 0.59200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M (NH4)2SO4, 0.1M TRIS PH 8.0 ,
REMARK 280 VAPOR DIFFUSION,SITTING DROP,NANODROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 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,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+3/4
REMARK 290 8555 -Y,-X,-Z+1/4
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 37.70150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 18.85075
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 56.55225
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 37.70150
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 56.55225
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 18.85075
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300 SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT
REMARK 300 SCATTERING SUPPORTS THE ASSIGNMENT OF A DIMER AS
REMARK 300 A BIOLOGICALLY SIGNIFICANT OLIGIMERIZATION STATE.
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 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 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 131.95525
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 GLY A 0
REMARK 465 MSE A 1
REMARK 465 PRO A 2
REMARK 465 ILE A 3
REMARK 465 ILE A 4
REMARK 465 ILE A 5
REMARK 465 ASP A 6
REMARK 465 LYS A 7
REMARK 465 ASP A 8
REMARK 465 LEU A 9
REMARK 465 PRO A 10
REMARK 465 ALA A 11
REMARK 465 ARG A 12
REMARK 465 LYS A 13
REMARK 465 VAL A 14
REMARK 465 LEU A 15
REMARK 465 GLN A 16
REMARK 465 HIS A 75
REMARK 465 LEU A 76
REMARK 465 SER A 77
REMARK 465 ARG A 78
REMARK 465 ASN A 79
REMARK 465 VAL A 80
REMARK 465 ALA A 81
REMARK 465 GLN A 82
REMARK 465 GLU A 83
REMARK 465 HIS A 84
REMARK 465 LEU A 85
REMARK 465 THR A 86
REMARK 465 PRO A 298
REMARK 465 TYR A 299
REMARK 465 VAL A 300
REMARK 465 LEU A 301
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 18 CB CG CD OE1 OE2
REMARK 470 THR A 46 CB OG1 CG2
REMARK 470 ARG A 93 NE CZ NH1 NH2
REMARK 470 GLU A 215 CD OE1 OE2
REMARK 470 LYS A 265 CG CD CE NZ
REMARK 470 LYS A 272 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 CYS A 240 CB CYS A 240 SG -0.116
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 CYS A 142 -116.88 44.80
REMARK 500 ARG A 193 145.55 -172.96
REMARK 500 HIS A 220 -68.07 -120.39
REMARK 500 HIS A 235 66.56 -118.98
REMARK 500 TYR A 263 -59.13 -128.46
REMARK 500 GLU A 296 -158.53 -90.96
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 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 360725 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV
REMARK 999 PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE
REMARK 999 TARGET SEQUENCE.
DBREF 2GHR A 1 301 UNP Q72X44 META_BACC1 1 301
SEQADV 2GHR GLY A 0 UNP Q72X44 EXPRESSION TAG
SEQADV 2GHR MSE A 1 UNP Q72X44 MET 1 MODIFIED RESIDUE
SEQADV 2GHR MSE A 23 UNP Q72X44 MET 23 MODIFIED RESIDUE
SEQADV 2GHR MSE A 44 UNP Q72X44 MET 44 MODIFIED RESIDUE
SEQADV 2GHR MSE A 72 UNP Q72X44 MET 72 MODIFIED RESIDUE
SEQADV 2GHR MSE A 128 UNP Q72X44 MET 128 MODIFIED RESIDUE
SEQADV 2GHR MSE A 164 UNP Q72X44 MET 164 MODIFIED RESIDUE
SEQRES 1 A 302 GLY MSE PRO ILE ILE ILE ASP LYS ASP LEU PRO ALA ARG
SEQRES 2 A 302 LYS VAL LEU GLN GLU GLU ASN ILE PHE VAL MSE THR LYS
SEQRES 3 A 302 GLU ARG ALA GLU THR GLN ASP ILE ARG ALA LEU LYS ILE
SEQRES 4 A 302 ALA ILE LEU ASN LEU MSE PRO THR LYS GLN GLU THR GLU
SEQRES 5 A 302 ALA GLN LEU LEU ARG LEU ILE GLY ASN THR PRO LEU GLN
SEQRES 6 A 302 LEU ASP VAL HIS LEU LEU HIS MSE GLU SER HIS LEU SER
SEQRES 7 A 302 ARG ASN VAL ALA GLN GLU HIS LEU THR SER PHE TYR LYS
SEQRES 8 A 302 THR PHE ARG ASP ILE GLU ASN GLU LYS PHE ASP GLY LEU
SEQRES 9 A 302 ILE ILE THR GLY ALA PRO VAL GLU THR LEU SER PHE GLU
SEQRES 10 A 302 GLU VAL ASP TYR TRP GLU GLU LEU LYS ARG ILE MSE GLU
SEQRES 11 A 302 TYR SER LYS THR ASN VAL THR SER THR LEU HIS ILE CYS
SEQRES 12 A 302 TRP GLY ALA GLN ALA GLY LEU TYR HIS HIS TYR GLY VAL
SEQRES 13 A 302 GLN LYS TYR PRO LEU LYS GLU LYS MSE PHE GLY VAL PHE
SEQRES 14 A 302 GLU HIS GLU VAL ARG GLU GLN HIS VAL LYS LEU LEU GLN
SEQRES 15 A 302 GLY PHE ASP GLU LEU PHE PHE ALA PRO HIS SER ARG HIS
SEQRES 16 A 302 THR GLU VAL ARG GLU SER ASP ILE ARG GLU VAL LYS GLU
SEQRES 17 A 302 LEU THR LEU LEU ALA ASN SER GLU GLU ALA GLY VAL HIS
SEQRES 18 A 302 LEU VAL ILE GLY GLN GLU GLY ARG GLN VAL PHE ALA LEU
SEQRES 19 A 302 GLY HIS SER GLU TYR SER CYS ASP THR LEU LYS GLN GLU
SEQRES 20 A 302 TYR GLU ARG ASP ARG ASP LYS GLY LEU ASN ILE ASP VAL
SEQRES 21 A 302 PRO LYS ASN TYR PHE LYS HIS ASP ASN PRO ASN GLU LYS
SEQRES 22 A 302 PRO LEU VAL ARG TRP ARG SER HIS GLY ASN LEU LEU PHE
SEQRES 23 A 302 SER ASN TRP LEU ASN TYR TYR VAL TYR GLN GLU THR PRO
SEQRES 24 A 302 TYR VAL LEU
MODRES 2GHR MSE A 23 MET SELENOMETHIONINE
MODRES 2GHR MSE A 44 MET SELENOMETHIONINE
MODRES 2GHR MSE A 72 MET SELENOMETHIONINE
MODRES 2GHR MSE A 128 MET SELENOMETHIONINE
MODRES 2GHR MSE A 164 MET SELENOMETHIONINE
HET MSE A 23 8
HET MSE A 44 8
HET MSE A 72 8
HET MSE A 128 8
HET MSE A 164 8
HET SO4 A 302 5
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
FORMUL 1 MSE 5(C5 H11 N O2 SE)
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *78(H2 O)
HELIX 1 1 THR A 46 ILE A 58 1 13
HELIX 2 2 THR A 91 GLU A 96 1 6
HELIX 3 3 SER A 114 VAL A 118 5 5
HELIX 4 4 TYR A 120 ASN A 134 1 15
HELIX 5 5 CYS A 142 GLY A 154 1 13
HELIX 6 6 VAL A 177 GLN A 181 5 5
HELIX 7 7 ARG A 198 GLU A 204 1 7
HELIX 8 8 ASP A 241 LYS A 253 1 13
HELIX 9 9 PHE A 264 ASN A 268 5 5
HELIX 10 10 TRP A 277 TYR A 292 1 16
SHEET 1 A10 TYR A 89 LYS A 90 0
SHEET 2 A10 LEU A 65 LEU A 70 1 N LEU A 69 O LYS A 90
SHEET 3 A10 LEU A 36 LEU A 41 1 N ILE A 38 O HIS A 68
SHEET 4 A10 PHE A 100 ILE A 105 1 O ILE A 104 N LEU A 41
SHEET 5 A10 VAL A 135 ILE A 141 1 O LEU A 139 N LEU A 103
SHEET 6 A10 GLN A 229 ALA A 232 1 O VAL A 230 N HIS A 140
SHEET 7 A10 GLY A 218 GLY A 224 -1 N VAL A 222 O PHE A 231
SHEET 8 A10 LEU A 208 SER A 214 -1 N LEU A 211 O LEU A 221
SHEET 9 A10 TYR A 158 VAL A 172 -1 N GLU A 171 O ASN A 213
SHEET 10 A10 LEU A 186 GLU A 196 -1 O PHE A 187 N HIS A 170
LINK C VAL A 22 N MSE A 23 1555 1555 1.33
LINK C MSE A 23 N THR A 24 1555 1555 1.32
LINK C LEU A 43 N MSE A 44 1555 1555 1.33
LINK C MSE A 44 N PRO A 45 1555 1555 1.35
LINK C HIS A 71 N MSE A 72 1555 1555 1.33
LINK C MSE A 72 N GLU A 73 1555 1555 1.32
LINK C ILE A 127 N MSE A 128 1555 1555 1.32
LINK C MSE A 128 N GLU A 129 1555 1555 1.34
LINK C LYS A 163 N MSE A 164 1555 1555 1.34
LINK C MSE A 164 N PHE A 165 1555 1555 1.33
SITE 1 AC1 3 SER A 239 CYS A 240 ARG A 278
CRYST1 95.890 95.890 75.403 90.00 90.00 90.00 P 41 2 2 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 0.010430 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010430 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013260 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
