HEADER TRANSFERASE 07-MAY-12 4F2G
TITLE THE CRYSTAL STRUCTURE OF ORNITHINE CARBAMOYLTRANSFERASE FROM
TITLE 2 BURKHOLDERIA THAILANDENSIS E264
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ORNITHINE CARBAMOYLTRANSFERASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OTCASE 1;
COMPND 5 EC: 2.1.3.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA THAILANDENSIS;
SOURCE 3 ORGANISM_TAXID: 271848;
SOURCE 4 STRAIN: E264 / ATCC 700388 / DSM 13276 / CIP 106301;
SOURCE 5 GENE: ARGF-1, ARGF1, BTH_I0732;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: AVA0421
KEYWDS STRUCTURAL GENOMICS, NIAID, NATIONAL INSTITUTE OF ALLERGY AND
KEYWDS 2 INFECTIOUS DISEASES, SEATTLE STRUCTURAL GENOMICS CENTER FOR
KEYWDS 3 INFECTIOUS DISEASE, SSGCID, CARBAMOYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.K.CRAIG,D.FOX,B.STAKER,L.STEWART,SEATTLE STRUCTURAL GENOMICS CENTER
AUTHOR 2 FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 3 13-SEP-23 4F2G 1 REMARK
REVDAT 2 30-OCT-13 4F2G 1 JRNL
REVDAT 1 30-MAY-12 4F2G 0
JRNL AUTH L.BAUGH,L.A.GALLAGHER,R.PATRAPUVICH,M.C.CLIFTON,
JRNL AUTH 2 A.S.GARDBERG,T.E.EDWARDS,B.ARMOUR,D.W.BEGLEY,S.H.DIETERICH,
JRNL AUTH 3 D.M.DRANOW,J.ABENDROTH,J.W.FAIRMAN,D.FOX,B.L.STAKER,I.PHAN,
JRNL AUTH 4 A.GILLESPIE,R.CHOI,S.NAKAZAWA-HEWITT,M.T.NGUYEN,A.NAPULI,
JRNL AUTH 5 L.BARRETT,G.W.BUCHKO,R.STACY,P.J.MYLER,L.J.STEWART,C.MANOIL,
JRNL AUTH 6 W.C.VAN VOORHIS
JRNL TITL COMBINING FUNCTIONAL AND STRUCTURAL GENOMICS TO SAMPLE THE
JRNL TITL 2 ESSENTIAL BURKHOLDERIA STRUCTOME.
JRNL REF PLOS ONE V. 8 53851 2013
JRNL REFN ESSN 1932-6203
JRNL PMID 23382856
JRNL DOI 10.1371/JOURNAL.PONE.0053851
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.3_928
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : LS_WUNIT_K1
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 27457
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1392
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 40.7830 - 4.5230 0.99 2933 156 0.1641 0.1846
REMARK 3 2 4.5230 - 3.5908 0.99 2753 147 0.1321 0.1715
REMARK 3 3 3.5908 - 3.1371 0.99 2702 142 0.1548 0.1944
REMARK 3 4 3.1371 - 2.8503 0.97 2630 140 0.1758 0.1891
REMARK 3 5 2.8503 - 2.6461 0.97 2625 137 0.1815 0.2075
REMARK 3 6 2.6461 - 2.4901 0.96 2559 135 0.1815 0.2429
REMARK 3 7 2.4901 - 2.3654 0.94 2534 138 0.1879 0.2039
REMARK 3 8 2.3654 - 2.2624 0.92 2469 132 0.1930 0.2416
REMARK 3 9 2.2624 - 2.1753 0.92 2447 134 0.1956 0.1964
REMARK 3 10 2.1753 - 2.1003 0.90 2413 131 0.2136 0.2113
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 34.88
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.07
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 2403
REMARK 3 ANGLE : 0.950 3273
REMARK 3 CHIRALITY : 0.066 355
REMARK 3 PLANARITY : 0.003 423
REMARK 3 DIHEDRAL : 13.000 852
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 6:16)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.4322 15.8495 -18.2687
REMARK 3 T TENSOR
REMARK 3 T11: 0.1421 T22: 0.1616
REMARK 3 T33: 0.1127 T12: 0.0490
REMARK 3 T13: 0.0080 T23: 0.0382
REMARK 3 L TENSOR
REMARK 3 L11: 6.4148 L22: 5.3711
REMARK 3 L33: 1.3096 L12: -0.7731
REMARK 3 L13: 0.4553 L23: -2.6485
REMARK 3 S TENSOR
REMARK 3 S11: 0.2632 S12: 0.6863 S13: 0.1856
REMARK 3 S21: -0.1709 S22: -0.1278 S23: 0.1249
REMARK 3 S31: -0.1502 S32: -0.1179 S33: -0.0816
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 17:35)
REMARK 3 ORIGIN FOR THE GROUP (A): -28.0629 5.4844 -14.2808
REMARK 3 T TENSOR
REMARK 3 T11: 0.0820 T22: 0.2219
REMARK 3 T33: 0.1844 T12: 0.0208
REMARK 3 T13: -0.0372 T23: -0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 4.0275 L22: 6.1461
REMARK 3 L33: 2.0330 L12: 2.5154
REMARK 3 L13: -2.5580 L23: -0.2363
REMARK 3 S TENSOR
REMARK 3 S11: 0.0195 S12: 0.1699 S13: -0.1649
REMARK 3 S21: -0.3371 S22: -0.2483 S23: 0.3979
REMARK 3 S31: 0.0715 S32: -0.0654 S33: 0.1497
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 36:56)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.0569 -1.4615 -11.9720
REMARK 3 T TENSOR
REMARK 3 T11: 0.1097 T22: 0.0375
REMARK 3 T33: 0.1154 T12: 0.0426
REMARK 3 T13: -0.0127 T23: 0.0422
REMARK 3 L TENSOR
REMARK 3 L11: 5.5071 L22: 3.8739
REMARK 3 L33: 2.6506 L12: 2.8592
REMARK 3 L13: 1.8168 L23: 1.3633
REMARK 3 S TENSOR
REMARK 3 S11: 0.0186 S12: 0.1204 S13: -0.1303
REMARK 3 S21: -0.0886 S22: 0.0688 S23: 0.2449
REMARK 3 S31: 0.0713 S32: 0.0269 S33: -0.0541
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 57:91)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.0823 4.5124 -8.0754
REMARK 3 T TENSOR
REMARK 3 T11: 0.0895 T22: 0.1127
REMARK 3 T33: 0.0622 T12: 0.0110
REMARK 3 T13: 0.0110 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 2.7738 L22: 3.7215
REMARK 3 L33: 1.5625 L12: 1.5244
REMARK 3 L13: -0.6818 L23: -1.2602
REMARK 3 S TENSOR
REMARK 3 S11: 0.1065 S12: -0.0496 S13: -0.0616
REMARK 3 S21: 0.0096 S22: -0.1099 S23: -0.1923
REMARK 3 S31: -0.1865 S32: 0.1458 S33: -0.0153
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 92:149)
REMARK 3 ORIGIN FOR THE GROUP (A): -11.2181 12.2902 -12.5174
REMARK 3 T TENSOR
REMARK 3 T11: 0.0993 T22: 0.0995
REMARK 3 T33: 0.0913 T12: 0.0125
REMARK 3 T13: 0.0058 T23: 0.0339
REMARK 3 L TENSOR
REMARK 3 L11: 2.0544 L22: 1.4812
REMARK 3 L33: 1.7641 L12: -0.7970
REMARK 3 L13: -0.8596 L23: 0.5676
REMARK 3 S TENSOR
REMARK 3 S11: 0.0977 S12: 0.2478 S13: 0.1965
REMARK 3 S21: -0.1259 S22: -0.0485 S23: -0.0537
REMARK 3 S31: -0.1381 S32: 0.0281 S33: -0.0580
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 150:194)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8246 25.6814 -4.5823
REMARK 3 T TENSOR
REMARK 3 T11: 0.1635 T22: 0.1062
REMARK 3 T33: 0.2199 T12: 0.0495
REMARK 3 T13: 0.0754 T23: 0.0366
REMARK 3 L TENSOR
REMARK 3 L11: 3.1194 L22: 2.9033
REMARK 3 L33: 4.2269 L12: -0.7384
REMARK 3 L13: -0.0424 L23: 0.3119
REMARK 3 S TENSOR
REMARK 3 S11: 0.2030 S12: 0.0477 S13: 0.3205
REMARK 3 S21: -0.1621 S22: -0.0429 S23: 0.0105
REMARK 3 S31: -0.5006 S32: 0.0170 S33: -0.1047
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 195:222)
REMARK 3 ORIGIN FOR THE GROUP (A): -26.4135 29.7792 -2.3154
REMARK 3 T TENSOR
REMARK 3 T11: 0.3025 T22: 0.1674
REMARK 3 T33: 0.3247 T12: 0.1263
REMARK 3 T13: 0.1046 T23: 0.0442
REMARK 3 L TENSOR
REMARK 3 L11: 1.7875 L22: 2.0753
REMARK 3 L33: 1.5819 L12: -0.2429
REMARK 3 L13: 1.1433 L23: -1.3746
REMARK 3 S TENSOR
REMARK 3 S11: 0.2464 S12: 0.1872 S13: 0.5785
REMARK 3 S21: -0.1274 S22: -0.1538 S23: 0.0574
REMARK 3 S31: -0.5671 S32: -0.0419 S33: -0.0098
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 223:244)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.9916 26.3450 10.2978
REMARK 3 T TENSOR
REMARK 3 T11: 0.5001 T22: 0.2627
REMARK 3 T33: 0.4247 T12: -0.0035
REMARK 3 T13: 0.0323 T23: -0.1054
REMARK 3 L TENSOR
REMARK 3 L11: 7.4146 L22: 6.9628
REMARK 3 L33: 2.0049 L12: -5.9415
REMARK 3 L13: -2.4368 L23: 1.7159
REMARK 3 S TENSOR
REMARK 3 S11: -0.0840 S12: -0.6683 S13: 1.0320
REMARK 3 S21: 1.1330 S22: 0.5895 S23: -0.9137
REMARK 3 S31: -0.9107 S32: 0.4776 S33: -0.4877
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 245:283)
REMARK 3 ORIGIN FOR THE GROUP (A): -26.4248 19.2642 9.5109
REMARK 3 T TENSOR
REMARK 3 T11: 0.1534 T22: 0.1644
REMARK 3 T33: 0.1676 T12: 0.0438
REMARK 3 T13: 0.0692 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 2.0665 L22: 3.1380
REMARK 3 L33: 3.0247 L12: -1.3118
REMARK 3 L13: -1.0309 L23: 1.2256
REMARK 3 S TENSOR
REMARK 3 S11: 0.0372 S12: -0.1859 S13: 0.1685
REMARK 3 S21: 0.2754 S22: 0.0245 S23: 0.1468
REMARK 3 S31: -0.0929 S32: -0.0269 S33: -0.0435
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 284:307)
REMARK 3 ORIGIN FOR THE GROUP (A): -21.6788 5.6996 -9.4203
REMARK 3 T TENSOR
REMARK 3 T11: 0.0679 T22: 0.1259
REMARK 3 T33: 0.1430 T12: 0.0044
REMARK 3 T13: -0.0190 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 1.2611 L22: 2.2103
REMARK 3 L33: 3.4732 L12: -0.7331
REMARK 3 L13: -1.2783 L23: 1.4789
REMARK 3 S TENSOR
REMARK 3 S11: -0.0002 S12: 0.1585 S13: -0.0492
REMARK 3 S21: -0.0657 S22: -0.0453 S23: 0.1885
REMARK 3 S31: -0.0043 S32: -0.3047 S33: 0.0227
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4F2G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-12.
REMARK 100 THE DEPOSITION ID IS D_1000072370.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28707
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 40.775
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 10.96
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.4100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.49600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.020
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1PVV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: JCSG3 WELL F12 0.1M NA CITRATE PH5.6,
REMARK 280 1M AMMONIUM DIHYDROGEN PHOSPHATE WITH 15% EG ADDED TO WELL
REMARK 280 SOLUTION, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 Y+3/4,X+1/4,-Z+1/4
REMARK 290 14555 -Y+3/4,-X+3/4,-Z+3/4
REMARK 290 15555 Y+1/4,-X+1/4,Z+3/4
REMARK 290 16555 -Y+1/4,X+3/4,Z+1/4
REMARK 290 17555 X+3/4,Z+1/4,-Y+1/4
REMARK 290 18555 -X+1/4,Z+3/4,Y+1/4
REMARK 290 19555 -X+3/4,-Z+3/4,-Y+3/4
REMARK 290 20555 X+1/4,-Z+1/4,Y+3/4
REMARK 290 21555 Z+3/4,Y+1/4,-X+1/4
REMARK 290 22555 Z+1/4,-Y+1/4,X+3/4
REMARK 290 23555 -Z+1/4,Y+3/4,X+1/4
REMARK 290 24555 -Z+3/4,-Y+3/4,-X+3/4
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 70.62500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.62500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.62500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.62500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 70.62500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.62500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 70.62500
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 70.62500
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 70.62500
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 70.62500
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 70.62500
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 70.62500
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 70.62500
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 70.62500
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 70.62500
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 70.62500
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 70.62500
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 70.62500
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 105.93750
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 35.31250
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 35.31250
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 105.93750
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 105.93750
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 105.93750
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 35.31250
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 35.31250
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 105.93750
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 35.31250
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 105.93750
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 35.31250
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 105.93750
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 35.31250
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 35.31250
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 35.31250
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 105.93750
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 35.31250
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 105.93750
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 105.93750
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 105.93750
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 35.31250
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 35.31250
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 105.93750
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 105.93750
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 35.31250
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 35.31250
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 35.31250
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 35.31250
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 105.93750
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 35.31250
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 105.93750
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 35.31250
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 105.93750
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 105.93750
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 105.93750
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 3040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 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 -35.31250
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 -35.31250
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -35.31250
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 22270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 62180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -308.0 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 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 -1.000000 0.000000 -35.31250
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 -35.31250
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 -35.31250
REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 -35.31250
REMARK 350 BIOMT2 5 0.000000 0.000000 -1.000000 -35.31250
REMARK 350 BIOMT3 5 0.000000 -1.000000 0.000000 -35.31250
REMARK 350 BIOMT1 6 0.000000 0.000000 -1.000000 -35.31250
REMARK 350 BIOMT2 6 0.000000 -1.000000 0.000000 -35.31250
REMARK 350 BIOMT3 6 -1.000000 0.000000 0.000000 -35.31250
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -140.0 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 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 P PO4 A 403 LIES ON A SPECIAL POSITION.
REMARK 375 O3 PO4 A 403 LIES ON A SPECIAL POSITION.
REMARK 375 P PO4 A 404 LIES ON A SPECIAL POSITION.
REMARK 375 O3 PO4 A 404 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 563 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 638 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 657 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 ALA A 3
REMARK 465 LYS A 4
REMARK 465 THR A 5
REMARK 465 THR A 227
REMARK 465 SER A 228
REMARK 465 MET A 229
REMARK 465 GLY A 230
REMARK 465 PHE A 231
REMARK 465 GLU A 232
REMARK 465 ALA A 233
REMARK 465 GLU A 234
REMARK 465 ASN A 235
REMARK 465 GLU A 236
REMARK 465 ALA A 237
REMARK 465 ARG A 238
REMARK 465 ASN A 309
REMARK 465 HIS A 310
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 35 CG CD CE NZ
REMARK 470 TYR A 37 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 80 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 180 CG CD CE NZ
REMARK 470 LYS A 194 CG CD CE NZ
REMARK 470 LEU A 195 CG CD1 CD2
REMARK 470 GLU A 199 CG CD OE1 OE2
REMARK 470 LYS A 215 CG CD CE NZ
REMARK 470 LYS A 239 CG CD CE NZ
REMARK 470 ARG A 240 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 242 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 308 CG CD1 CD2
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 129 129.51 142.86
REMARK 500 GLU A 271 -89.76 -114.83
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 EDO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 408
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PVV RELATED DB: PDB
REMARK 900 MOLECULAR REPLACEMENT MODEL
REMARK 900 RELATED ID: SSGCID-BUTHA.00088.A RELATED DB: TARGETTRACK
DBREF 4F2G A 1 310 UNP Q2T0L1 Q2T0L1_BURTA 1 309
SEQRES 1 A 309 MET THR ALA LYS THR ILE ARG HIS TYR LEU GLN PHE LYS
SEQRES 2 A 309 ASP PHE SER LEU GLU ASP TYR GLU TYR VAL LEU GLU ARG
SEQRES 3 A 309 THR GLY ILE LEU LYS ARG LYS PHE LYS ASN TYR GLU THR
SEQRES 4 A 309 TYR HIS PRO LEU HIS ASP ARG THR LEU ALA MET ILE PHE
SEQRES 5 A 309 GLU LYS SER SER THR ARG THR ARG LEU SER PHE GLU ALA
SEQRES 6 A 309 GLY ILE PHE GLN LEU GLY GLY HIS ALA VAL PHE MET SER
SEQRES 7 A 309 THR ARG ASP THR GLN LEU GLY ARG GLY GLU PRO VAL GLU
SEQRES 8 A 309 ASP SER ALA GLN VAL ILE SER ARG MET VAL ASP ILE ILE
SEQRES 9 A 309 MET ILE ARG THR PHE GLU GLN ASP ILE ILE GLN ARG PHE
SEQRES 10 A 309 ALA GLU ASN SER ARG VAL PRO VAL ILE ASN GLY LEU THR
SEQRES 11 A 309 ASN GLU TYR HIS PRO CYS GLN VAL LEU ALA ASP ILE PHE
SEQRES 12 A 309 THR TYR TYR GLU HIS ARG GLY PRO ILE ARG GLY LYS THR
SEQRES 13 A 309 VAL ALA TRP VAL GLY ASP ALA ASN ASN MET LEU TYR THR
SEQRES 14 A 309 TRP ILE GLN ALA ALA ARG ILE LEU ASP PHE LYS LEU GLN
SEQRES 15 A 309 LEU SER THR PRO PRO GLY TYR ALA LEU ASP ALA LYS LEU
SEQRES 16 A 309 VAL ASP ALA GLU SER ALA PRO PHE TYR GLN VAL PHE ASP
SEQRES 17 A 309 ASP PRO ASN GLU ALA CYS LYS GLY ALA ASP LEU VAL THR
SEQRES 18 A 309 THR ASP VAL TRP THR SER MET GLY PHE GLU ALA GLU ASN
SEQRES 19 A 309 GLU ALA ARG LYS ARG ALA PHE ALA ASP TRP CYS VAL ASP
SEQRES 20 A 309 GLU GLU MET MET SER HIS ALA ASN SER ASP ALA LEU PHE
SEQRES 21 A 309 MET HIS CYS LEU PRO ALA HIS ARG GLY GLU GLU VAL THR
SEQRES 22 A 309 ALA GLY VAL ILE ASP GLY PRO GLN SER VAL VAL TRP ASP
SEQRES 23 A 309 GLU ALA GLU ASN ARG LEU HIS VAL GLN LYS ALA LEU MET
SEQRES 24 A 309 GLU PHE LEU LEU LEU GLY ARG LEU ASN HIS
HET EDO A 401 4
HET PO4 A 402 5
HET PO4 A 403 5
HET PO4 A 404 5
HET PO4 A 405 5
HET PO4 A 406 5
HET PO4 A 407 5
HET PO4 A 408 5
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PO4 PHOSPHATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO C2 H6 O2
FORMUL 3 PO4 7(O4 P 3-)
FORMUL 10 HOH *204(H2 O)
HELIX 1 1 GLN A 11 PHE A 15 5 5
HELIX 2 2 SER A 16 ASN A 36 1 21
HELIX 3 3 SER A 56 LEU A 70 1 15
HELIX 4 4 PRO A 89 VAL A 101 1 13
HELIX 5 5 GLU A 110 ASN A 120 1 11
HELIX 6 6 HIS A 134 GLY A 150 1 17
HELIX 7 7 ASN A 164 ASP A 178 1 15
HELIX 8 8 PRO A 186 ALA A 190 5 5
HELIX 9 9 ASP A 192 VAL A 196 5 5
HELIX 10 10 ASP A 197 PRO A 202 5 6
HELIX 11 11 ASP A 209 CYS A 214 1 6
HELIX 12 12 ALA A 241 CYS A 246 5 6
HELIX 13 13 ASP A 248 SER A 253 1 6
HELIX 14 14 THR A 274 ASP A 279 1 6
HELIX 15 15 VAL A 284 GLY A 306 1 23
SHEET 1 A 4 HIS A 73 MET A 77 0
SHEET 2 A 4 THR A 47 PHE A 52 1 N MET A 50 O MET A 77
SHEET 3 A 4 ILE A 103 ARG A 107 1 O MET A 105 N ILE A 51
SHEET 4 A 4 VAL A 125 LEU A 129 1 O ILE A 126 N ILE A 104
SHEET 1 B 2 GLN A 83 LEU A 84 0
SHEET 2 B 2 GLY A 87 GLU A 88 1 N GLU A 88 O GLN A 83
SHEET 1 C 5 TYR A 204 VAL A 206 0
SHEET 2 C 5 LYS A 180 SER A 184 1 N LEU A 183 O GLN A 205
SHEET 3 C 5 THR A 156 VAL A 160 1 N VAL A 157 O GLN A 182
SHEET 4 C 5 LEU A 219 THR A 222 1 O LEU A 219 N ALA A 158
SHEET 5 C 5 LEU A 260 HIS A 263 1 O LEU A 260 N VAL A 220
CISPEP 1 LEU A 265 PRO A 266 0 5.08
SITE 1 AC1 6 ARG A 7 HIS A 8 ASP A 14 PHE A 15
SITE 2 AC1 6 HOH A 533 HOH A 687
SITE 1 AC2 10 SER A 56 ARG A 58 THR A 59 ARG A 107
SITE 2 AC2 10 HIS A 134 CYS A 264 LEU A 265 ARG A 292
SITE 3 AC2 10 HOH A 527 HOH A 623
SITE 1 AC3 2 ARG A 60 PHE A 76
SITE 1 AC4 3 HIS A 73 HOH A 557 HOH A 601
SITE 1 AC5 7 ARG A 86 GLY A 87 GLU A 88 THR A 274
SITE 2 AC5 7 PO4 A 406 HOH A 570 HOH A 606
SITE 1 AC6 10 GLY A 85 ARG A 86 GLU A 88 PRO A 89
SITE 2 AC6 10 VAL A 90 ASP A 248 GLU A 249 THR A 274
SITE 3 AC6 10 PO4 A 405 HOH A 594
SITE 1 AC7 2 HIS A 148 ARG A 149
SITE 1 AC8 4 ARG A 26 LYS A 33 GLU A 38 HOH A 614
CRYST1 141.250 141.250 141.250 90.00 90.00 90.00 P 41 3 2 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 0.007080 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007080 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007080 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
