HEADER HYDROLASE 10-JUL-14 4QU4
TITLE IMPROVED REFINEMENT OF THE MTR4 APO CRYSTAL STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP-DEPENDENT RNA HELICASE DOB1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MRNA TRANSPORT REGULATOR MTR4;
COMPND 5 EC: 3.6.4.13;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: DOB1, J1158, MTR4, MTR4/YJL050W, YJL050W;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET151 DIRECTIONAL TOPO
KEYWDS REC-A FOLD, WINGED-HELIX-TURN-HELIX, ANTIPARALLEL-COILED-COIL, DSHCT
KEYWDS 2 DOMAIN, HELICASE, NUCLEOTIDE BINDING, PHOSPHOPROTEIN, RRNA
KEYWDS 3 PROCESSING, TRAMP, ATP BINDING, NUCLEUS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.J.JOHNSON,L.L.TAYLOR
REVDAT 3 28-FEB-24 4QU4 1 REMARK SEQADV
REVDAT 2 14-JAN-15 4QU4 1 JRNL
REVDAT 1 03-DEC-14 4QU4 0
SPRSDE 03-DEC-14 4QU4 3L9O
JRNL AUTH L.L.TAYLOR,R.N.JACKSON,M.REXHEPAJ,A.K.KING,L.K.LOTT,
JRNL AUTH 2 A.VAN HOOF,S.J.JOHNSON
JRNL TITL THE MTR4 RATCHET HELIX AND ARCH DOMAIN BOTH FUNCTION TO
JRNL TITL 2 PROMOTE RNA UNWINDING.
JRNL REF NUCLEIC ACIDS RES. V. 42 13861 2014
JRNL REFN ISSN 0305-1048
JRNL PMID 25414331
JRNL DOI 10.1093/NAR/GKU1208
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.N.JACKSON,A.A.KLAUER,B.J.HINTZE,H.ROBINSON,A.VAN HOOF,
REMARK 1 AUTH 2 S.J.JOHNSON
REMARK 1 TITL THE CRYSTAL STRUCTURE OF MTR4 REVEALS A NOVEL ARCH DOMAIN
REMARK 1 TITL 2 REQUIRED FOR RRNA PROCESSING.
REMARK 1 REF EMBO J. V. 29 2205 2010
REMARK 1 REFN ISSN 0261-4189
REMARK 2
REMARK 2 RESOLUTION. 3.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.76
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 26095
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.250
REMARK 3 R VALUE (WORKING SET) : 0.248
REMARK 3 FREE R VALUE : 0.299
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860
REMARK 3 FREE R VALUE TEST SET COUNT : 1268
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 28.7583 - 7.0255 1.00 3068 173 0.1983 0.2499
REMARK 3 2 7.0255 - 5.5898 1.00 2973 155 0.3124 0.3368
REMARK 3 3 5.5898 - 4.8871 1.00 2951 143 0.2519 0.3305
REMARK 3 4 4.8871 - 4.4420 1.00 2913 149 0.2219 0.2987
REMARK 3 5 4.4420 - 4.1246 1.00 2943 138 0.2485 0.3043
REMARK 3 6 4.1246 - 3.8821 1.00 2888 137 0.2930 0.3167
REMARK 3 7 3.8821 - 3.6881 0.99 2881 154 0.3206 0.3833
REMARK 3 8 3.6881 - 3.5278 0.85 2464 123 0.3423 0.4255
REMARK 3 9 3.5278 - 3.3920 0.60 1746 96 0.3539 0.3918
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.530
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.780
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 137.4
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 164.4
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.010 6789
REMARK 3 ANGLE : 1.463 9265
REMARK 3 CHIRALITY : 0.052 1123
REMARK 3 PLANARITY : 0.007 1196
REMARK 3 DIHEDRAL : 14.952 2290
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 79:122)
REMARK 3 ORIGIN FOR THE GROUP (A): 121.4053 54.1914 81.9824
REMARK 3 T TENSOR
REMARK 3 T11: 1.4882 T22: 1.6363
REMARK 3 T33: 1.8414 T12: -0.5718
REMARK 3 T13: 0.2647 T23: -0.3716
REMARK 3 L TENSOR
REMARK 3 L11: 1.4901 L22: 0.7245
REMARK 3 L33: 1.4770 L12: -1.0626
REMARK 3 L13: 1.5118 L23: -1.0392
REMARK 3 S TENSOR
REMARK 3 S11: -0.4911 S12: -0.5364 S13: 0.5464
REMARK 3 S21: 0.8397 S22: 0.5707 S23: -1.0894
REMARK 3 S31: 0.8878 S32: 0.6098 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 123:321)
REMARK 3 ORIGIN FOR THE GROUP (A): 117.5086 51.8302 55.8376
REMARK 3 T TENSOR
REMARK 3 T11: 0.8181 T22: 1.1179
REMARK 3 T33: 1.4826 T12: -0.1393
REMARK 3 T13: 0.2657 T23: -0.3027
REMARK 3 L TENSOR
REMARK 3 L11: 3.9461 L22: 4.4006
REMARK 3 L33: 6.6049 L12: 2.7957
REMARK 3 L13: 3.1836 L23: -0.7880
REMARK 3 S TENSOR
REMARK 3 S11: -0.0764 S12: -0.4919 S13: 0.7772
REMARK 3 S21: 0.0887 S22: -0.4164 S23: 0.3407
REMARK 3 S31: 0.2770 S32: -0.3368 S33: -0.0001
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 322:415)
REMARK 3 ORIGIN FOR THE GROUP (A): 101.9349 64.1837 87.3387
REMARK 3 T TENSOR
REMARK 3 T11: 1.5352 T22: 1.5788
REMARK 3 T33: 1.3137 T12: -0.3586
REMARK 3 T13: 0.1014 T23: -0.3172
REMARK 3 L TENSOR
REMARK 3 L11: 2.6638 L22: 5.4108
REMARK 3 L33: 3.2597 L12: 0.7969
REMARK 3 L13: -1.4461 L23: 1.6121
REMARK 3 S TENSOR
REMARK 3 S11: -0.0921 S12: -0.7313 S13: 0.6103
REMARK 3 S21: -0.6695 S22: 0.8091 S23: -0.7377
REMARK 3 S31: -0.2863 S32: 0.6662 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 416:496)
REMARK 3 ORIGIN FOR THE GROUP (A): 95.3732 79.6656 66.3684
REMARK 3 T TENSOR
REMARK 3 T11: 4.9842 T22: 1.0150
REMARK 3 T33: 1.6650 T12: 0.0373
REMARK 3 T13: -0.2247 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 2.2277 L22: 0.7423
REMARK 3 L33: 1.4946 L12: 0.1277
REMARK 3 L13: -0.0808 L23: 0.1020
REMARK 3 S TENSOR
REMARK 3 S11: 0.1456 S12: -0.1949 S13: 0.3534
REMARK 3 S21: -1.9922 S22: -0.5973 S23: 0.0948
REMARK 3 S31: -2.5728 S32: -0.9086 S33: -0.1419
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 497:599)
REMARK 3 ORIGIN FOR THE GROUP (A): 100.1560 55.5452 71.3988
REMARK 3 T TENSOR
REMARK 3 T11: 1.8011 T22: 1.5463
REMARK 3 T33: 1.4673 T12: -0.4140
REMARK 3 T13: 0.1673 T23: -0.1893
REMARK 3 L TENSOR
REMARK 3 L11: 1.0902 L22: 3.3927
REMARK 3 L33: 6.2213 L12: 0.2529
REMARK 3 L13: 1.2392 L23: 4.6278
REMARK 3 S TENSOR
REMARK 3 S11: -0.6396 S12: 0.2996 S13: 0.2742
REMARK 3 S21: -1.5229 S22: 0.6201 S23: -0.0506
REMARK 3 S31: -1.4309 S32: 0.3780 S33: -0.0004
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 600:661)
REMARK 3 ORIGIN FOR THE GROUP (A): 90.4966 22.5567 70.4676
REMARK 3 T TENSOR
REMARK 3 T11: 1.5943 T22: 1.7975
REMARK 3 T33: 1.5463 T12: 0.0425
REMARK 3 T13: 0.2550 T23: 0.0688
REMARK 3 L TENSOR
REMARK 3 L11: 1.0427 L22: 2.6099
REMARK 3 L33: 1.7790 L12: 1.7733
REMARK 3 L13: -0.8313 L23: -1.5578
REMARK 3 S TENSOR
REMARK 3 S11: -0.3803 S12: -0.8651 S13: -0.5577
REMARK 3 S21: -0.5251 S22: 0.0030 S23: -0.7333
REMARK 3 S31: 0.1924 S32: 0.9719 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 662:780)
REMARK 3 ORIGIN FOR THE GROUP (A): 71.4543 44.5331 82.5487
REMARK 3 T TENSOR
REMARK 3 T11: 1.3807 T22: 1.5862
REMARK 3 T33: 1.4364 T12: 0.3554
REMARK 3 T13: 0.0293 T23: -0.0746
REMARK 3 L TENSOR
REMARK 3 L11: 5.5218 L22: 3.0745
REMARK 3 L33: 3.8979 L12: 1.6466
REMARK 3 L13: 1.8740 L23: 0.6717
REMARK 3 S TENSOR
REMARK 3 S11: 0.3039 S12: -0.5016 S13: -0.1094
REMARK 3 S21: 0.3716 S22: 0.0191 S23: 0.0622
REMARK 3 S31: 0.4900 S32: 0.4328 S33: -0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 781:877)
REMARK 3 ORIGIN FOR THE GROUP (A): 72.6577 25.5875 83.1105
REMARK 3 T TENSOR
REMARK 3 T11: 1.6927 T22: 1.5141
REMARK 3 T33: 1.5345 T12: -0.0018
REMARK 3 T13: 0.0756 T23: 0.1765
REMARK 3 L TENSOR
REMARK 3 L11: 1.4806 L22: 3.5586
REMARK 3 L33: 2.1061 L12: -1.1511
REMARK 3 L13: -0.7719 L23: 0.1584
REMARK 3 S TENSOR
REMARK 3 S11: -0.0988 S12: -0.5361 S13: 0.0787
REMARK 3 S21: -0.1549 S22: 0.0281 S23: 0.3412
REMARK 3 S31: -0.2593 S32: 0.3228 S33: 0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN A AND RESID 878:995)
REMARK 3 ORIGIN FOR THE GROUP (A): 82.7170 46.1998 43.0707
REMARK 3 T TENSOR
REMARK 3 T11: 2.3586 T22: 2.3193
REMARK 3 T33: 1.8799 T12: -0.1513
REMARK 3 T13: -0.2126 T23: -0.0516
REMARK 3 L TENSOR
REMARK 3 L11: 0.8322 L22: 2.2311
REMARK 3 L33: -0.0238 L12: -0.7501
REMARK 3 L13: 0.2044 L23: -0.2693
REMARK 3 S TENSOR
REMARK 3 S11: -0.5877 S12: 0.1623 S13: 0.0311
REMARK 3 S21: -1.6456 S22: 0.1160 S23: 1.1313
REMARK 3 S31: -0.7490 S32: -0.6646 S33: -0.0001
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN A AND RESID 996:1072)
REMARK 3 ORIGIN FOR THE GROUP (A): 85.9075 67.1731 45.1656
REMARK 3 T TENSOR
REMARK 3 T11: 3.5475 T22: 2.5358
REMARK 3 T33: 1.5350 T12: 0.3674
REMARK 3 T13: -0.2059 T23: 0.2104
REMARK 3 L TENSOR
REMARK 3 L11: 1.0882 L22: 0.0394
REMARK 3 L33: 0.5071 L12: -0.1273
REMARK 3 L13: -0.5264 L23: 0.2121
REMARK 3 S TENSOR
REMARK 3 S11: -0.4152 S12: -0.2002 S13: 0.6948
REMARK 3 S21: 0.2790 S22: -0.6791 S23: 0.0441
REMARK 3 S31: -1.0321 S32: -0.9230 S33: -0.0180
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 4QU4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000086515.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JAN-08
REMARK 200 TEMPERATURE (KELVIN) : 190
REMARK 200 PH : 8.5
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) : 0.9793
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26177
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.389
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 10.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.39
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.52
REMARK 200 COMPLETENESS FOR SHELL (%) : 59.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M AMMONIUM DIHYDROGEN PHOSPHATE,
REMARK 280 0.1 M TRIS, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.64967
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 127.29933
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 127.29933
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 63.64967
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -34
REMARK 465 HIS A -33
REMARK 465 HIS A -32
REMARK 465 HIS A -31
REMARK 465 HIS A -30
REMARK 465 HIS A -29
REMARK 465 HIS A -28
REMARK 465 GLY A -27
REMARK 465 LYS A -26
REMARK 465 PRO A -25
REMARK 465 ILE A -24
REMARK 465 PRO A -23
REMARK 465 ASN A -22
REMARK 465 PRO A -21
REMARK 465 LEU A -20
REMARK 465 LEU A -19
REMARK 465 GLY A -18
REMARK 465 LEU A -17
REMARK 465 ASP A -16
REMARK 465 SER A -15
REMARK 465 THR A -14
REMARK 465 GLU A -13
REMARK 465 ASN A -12
REMARK 465 LEU A -11
REMARK 465 TYR A -10
REMARK 465 PHE A -9
REMARK 465 GLN A -8
REMARK 465 GLY A -7
REMARK 465 ILE A -6
REMARK 465 ASP A -5
REMARK 465 PRO A -4
REMARK 465 PHE A -3
REMARK 465 THR A -2
REMARK 465 GLU A -1
REMARK 465 PHE A 0
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 SER A 3
REMARK 465 THR A 4
REMARK 465 ASP A 5
REMARK 465 LEU A 6
REMARK 465 PHE A 7
REMARK 465 ASP A 8
REMARK 465 VAL A 9
REMARK 465 PHE A 10
REMARK 465 GLU A 11
REMARK 465 GLU A 12
REMARK 465 THR A 13
REMARK 465 PRO A 14
REMARK 465 VAL A 15
REMARK 465 GLU A 16
REMARK 465 LEU A 17
REMARK 465 PRO A 18
REMARK 465 THR A 19
REMARK 465 ASP A 20
REMARK 465 SER A 21
REMARK 465 ASN A 22
REMARK 465 GLY A 23
REMARK 465 GLU A 24
REMARK 465 LYS A 25
REMARK 465 ASN A 26
REMARK 465 ALA A 27
REMARK 465 ASP A 28
REMARK 465 THR A 29
REMARK 465 ASN A 30
REMARK 465 VAL A 31
REMARK 465 GLY A 32
REMARK 465 ASP A 33
REMARK 465 THR A 34
REMARK 465 PRO A 35
REMARK 465 ASP A 36
REMARK 465 HIS A 37
REMARK 465 THR A 38
REMARK 465 GLN A 39
REMARK 465 ASP A 40
REMARK 465 LYS A 41
REMARK 465 LYS A 42
REMARK 465 HIS A 43
REMARK 465 GLY A 44
REMARK 465 LEU A 45
REMARK 465 GLU A 46
REMARK 465 GLU A 47
REMARK 465 GLU A 48
REMARK 465 LYS A 49
REMARK 465 GLU A 50
REMARK 465 GLU A 51
REMARK 465 HIS A 52
REMARK 465 GLU A 53
REMARK 465 GLU A 54
REMARK 465 ASN A 55
REMARK 465 ASN A 56
REMARK 465 SER A 57
REMARK 465 GLU A 58
REMARK 465 ASN A 59
REMARK 465 LYS A 60
REMARK 465 LYS A 61
REMARK 465 ILE A 62
REMARK 465 LYS A 63
REMARK 465 SER A 64
REMARK 465 ASN A 65
REMARK 465 LYS A 66
REMARK 465 SER A 67
REMARK 465 LYS A 68
REMARK 465 THR A 69
REMARK 465 GLU A 70
REMARK 465 ASP A 71
REMARK 465 LYS A 72
REMARK 465 ASN A 73
REMARK 465 LYS A 74
REMARK 465 LYS A 75
REMARK 465 VAL A 76
REMARK 465 VAL A 77
REMARK 465 VAL A 78
REMARK 465 ASP A 94
REMARK 465 SER A 361
REMARK 465 ASN A 362
REMARK 465 GLN A 363
REMARK 465 ILE A 364
REMARK 465 GLY A 365
REMARK 465 ASP A 366
REMARK 465 ASP A 367
REMARK 465 PRO A 368
REMARK 465 ASN A 369
REMARK 465 SER A 370
REMARK 465 THR A 371
REMARK 465 ASP A 372
REMARK 465 SER A 373
REMARK 465 ARG A 374
REMARK 465 GLY A 375
REMARK 465 LYS A 376
REMARK 465 LYS A 377
REMARK 465 GLY A 378
REMARK 465 GLN A 379
REMARK 465 THR A 380
REMARK 465 TYR A 381
REMARK 465 LYS A 382
REMARK 465 GLY A 383
REMARK 465 GLY A 384
REMARK 465 SER A 385
REMARK 465 ALA A 386
REMARK 465 LYS A 387
REMARK 465 GLY A 388
REMARK 465 ASP A 389
REMARK 465 SER A 873
REMARK 465 GLN A 874
REMARK 465 PHE A 943
REMARK 465 ALA A 944
REMARK 465 PHE A 945
REMARK 465 GLN A 946
REMARK 465 GLU A 947
REMARK 465 ARG A 948
REMARK 465 CYS A 949
REMARK 465 LYS A 950
REMARK 465 GLU A 951
REMARK 465 ALA A 952
REMARK 465 PRO A 953
REMARK 465 ARG A 954
REMARK 465 LEU A 955
REMARK 465 LYS A 956
REMARK 465 PRO A 957
REMARK 465 GLU A 958
REMARK 465 ALA A 1008
REMARK 465 VAL A 1039
REMARK 465 ASN A 1043
REMARK 465 GLY A 1046
REMARK 465 LEU A 1073
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 86 CG CD OE1 OE2
REMARK 470 ARG A 91 CD NE CZ NH1 NH2
REMARK 470 LYS A 97 CG CD CE NZ
REMARK 470 LEU A 99 CG CD1 CD2
REMARK 470 GLU A 103 CG CD OE1 OE2
REMARK 470 LEU A 105 CG CD1 CD2
REMARK 470 GLN A 106 CG CD OE1 NE2
REMARK 470 GLU A 108 OE1
REMARK 470 LYS A 112 CD CE NZ
REMARK 470 ARG A 114 CD NE CZ NH1 NH2
REMARK 470 GLN A 118 CD OE1 NE2
REMARK 470 ARG A 120 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 136 CG CD OE1 OE2
REMARK 470 LYS A 138 CD CE NZ
REMARK 470 ARG A 163 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 177 CG CD CE NZ
REMARK 470 LYS A 190 CD CE NZ
REMARK 470 LYS A 192 CD CE NZ
REMARK 470 ARG A 194 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 201 CG1 CD1
REMARK 470 LYS A 202 CD CE NZ
REMARK 470 ARG A 210 CD NE CZ NH1 NH2
REMARK 470 ILE A 226 CG1 CG2 CD1
REMARK 470 ASP A 231 CG OD1 OD2
REMARK 470 GLU A 240 CG CD OE1 OE2
REMARK 470 ARG A 248 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 254 CD NE CZ NH1 NH2
REMARK 470 GLU A 255 CD OE1 OE2
REMARK 470 LYS A 270 CD CE NZ
REMARK 470 ARG A 272 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 278 CD OE1 OE2
REMARK 470 LYS A 286 CD CE NZ
REMARK 470 ILE A 296 CG1 CG2 CD1
REMARK 470 GLU A 301 CG CD OE1 OE2
REMARK 470 GLU A 304 CD OE1 OE2
REMARK 470 LYS A 308 CG CD CE NZ
REMARK 470 ASN A 320 OD1 ND2
REMARK 470 HIS A 334 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A 343 CG OD1 OD2
REMARK 470 LYS A 345 CD CE NZ
REMARK 470 LYS A 355 CD CE NZ
REMARK 470 LYS A 391 CD CE NZ
REMARK 470 LYS A 396 CG CD CE NZ
REMARK 470 LYS A 399 CD CE NZ
REMARK 470 LYS A 403 CD CE NZ
REMARK 470 LYS A 404 CD CE NZ
REMARK 470 LYS A 405 CG CD CE NZ
REMARK 470 ASN A 407 CG OD1 ND2
REMARK 470 ILE A 410 CG1 CG2 CD1
REMARK 470 GLU A 420 CG CD OE1 OE2
REMARK 470 LEU A 422 CG CD1 CD2
REMARK 470 LEU A 424 CG CD1 CD2
REMARK 470 LYS A 425 CD CE NZ
REMARK 470 MET A 426 SD CE
REMARK 470 LYS A 428 CD CE NZ
REMARK 470 LEU A 429 CD1 CD2
REMARK 470 PHE A 431 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A 432 CG OD1 ND2
REMARK 470 ASP A 435 CG OD1 OD2
REMARK 470 GLU A 436 CG CD OE1 OE2
REMARK 470 GLU A 438 CG CD OE1 OE2
REMARK 470 LYS A 442 CG CD CE NZ
REMARK 470 PHE A 444 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 453 CG CD OE1 OE2
REMARK 470 ARG A 456 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 457 CG CD OE1 OE2
REMARK 470 LEU A 458 CG CD1 CD2
REMARK 470 GLN A 460 CG CD OE1 NE2
REMARK 470 ILE A 461 CG1 CG2 CD1
REMARK 470 LYS A 462 CG CD CE NZ
REMARK 470 ILE A 464 CG1 CG2 CD1
REMARK 470 PRO A 466 O
REMARK 470 LEU A 467 CD1 CD2
REMARK 470 ARG A 469 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 470 NE CZ NH1 NH2
REMARK 470 ILE A 474 CG1 CG2 CD1
REMARK 470 HIS A 476 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 484 CG CD CE NZ
REMARK 470 GLU A 488 CG CD OE1 OE2
REMARK 470 PHE A 491 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 492 CD OE1 NE2
REMARK 470 GLU A 493 CG CD OE1 OE2
REMARK 470 PHE A 495 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 497 CG CD CE NZ
REMARK 470 PHE A 500 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR A 502 OG1
REMARK 470 GLU A 503 CG CD OE1 OE2
REMARK 470 ILE A 507 CG1 CG2 CD1
REMARK 470 LYS A 514 CD CE NZ
REMARK 470 LYS A 523 CD CE NZ
REMARK 470 TRP A 524 CD1 CD2 NE1 CE2 CE3 CZ2 CZ3
REMARK 470 TRP A 524 CH2
REMARK 470 GLN A 527 CD OE1 NE2
REMARK 470 PHE A 529 CD1 CE1 CE2 CZ
REMARK 470 ARG A 530 CD NE CZ NH1 NH2
REMARK 470 GLN A 539 CG CD OE1 NE2
REMARK 470 ARG A 543 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 547 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 561 CG CD OE1 OE2
REMARK 470 LYS A 562 CD CE NZ
REMARK 470 LYS A 569 CD CE NZ
REMARK 470 PHE A 583 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 585 CD1 CD2
REMARK 470 ASN A 588 CG OD1 ND2
REMARK 470 ARG A 595 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 606 CD OE1 OE2
REMARK 470 GLN A 611 CD OE1 NE2
REMARK 470 LYS A 623 CD CE NZ
REMARK 470 LYS A 624 CD CE NZ
REMARK 470 LEU A 628 CD1 CD2
REMARK 470 LYS A 629 CG CD CE NZ
REMARK 470 LYS A 630 CD CE NZ
REMARK 470 PHE A 632 CD1 CE1 CE2 CZ
REMARK 470 ILE A 635 CD1
REMARK 470 GLU A 636 CG CD OE1 OE2
REMARK 470 ASP A 639 OD1 OD2
REMARK 470 GLU A 640 CD OE1 OE2
REMARK 470 GLU A 641 CG CD OE1 OE2
REMARK 470 LYS A 644 CD CE NZ
REMARK 470 GLU A 650 CD OE1 OE2
REMARK 470 LYS A 654 CD CE NZ
REMARK 470 GLU A 681 CD OE1 OE2
REMARK 470 LYS A 687 CE NZ
REMARK 470 LYS A 700 CD CE NZ
REMARK 470 ILE A 702 CG1 CG2 CD1
REMARK 470 LYS A 704 CG CD CE NZ
REMARK 470 ARG A 705 CG CD NE CZ NH1 NH2
REMARK 470 SER A 708 OG
REMARK 470 LYS A 736 CG CD CE NZ
REMARK 470 GLU A 744 CD OE1 OE2
REMARK 470 ARG A 747 CD NE CZ NH1 NH2
REMARK 470 GLU A 751 CG CD OE1 OE2
REMARK 470 LYS A 754 CG CD CE NZ
REMARK 470 LEU A 764 CD1 CD2
REMARK 470 ASP A 765 OD1 OD2
REMARK 470 LYS A 768 CD CE NZ
REMARK 470 LYS A 779 CG CD CE NZ
REMARK 470 ASP A 780 CG OD1 OD2
REMARK 470 ARG A 782 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 786 CD OE1 NE2
REMARK 470 LYS A 787 CE NZ
REMARK 470 LYS A 792 CD CE NZ
REMARK 470 ARG A 795 CD NE CZ NH1 NH2
REMARK 470 ARG A 799 CD NE CZ NH1 NH2
REMARK 470 ARG A 800 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 803 CG OD1 OD2
REMARK 470 LYS A 812 CD CE NZ
REMARK 470 GLU A 817 CG CD OE1 OE2
REMARK 470 GLU A 819 CD OE1 OE2
REMARK 470 ASP A 820 CG OD1 OD2
REMARK 470 LEU A 822 CD1
REMARK 470 LYS A 823 CG CD CE NZ
REMARK 470 LYS A 826 CD CE NZ
REMARK 470 LYS A 834 CD CE NZ
REMARK 470 ASN A 842 CG OD1 ND2
REMARK 470 GLU A 847 OE1 OE2
REMARK 470 GLU A 848 CD OE1 OE2
REMARK 470 LYS A 852 CD CE NZ
REMARK 470 ARG A 855 NE CZ NH1 NH2
REMARK 470 LYS A 856 CD CE NZ
REMARK 470 LYS A 864 CG CD CE NZ
REMARK 470 GLN A 865 CD NE2
REMARK 470 LEU A 866 CD1 CD2
REMARK 470 LYS A 867 CD CE NZ
REMARK 470 LYS A 869 CE NZ
REMARK 470 VAL A 876 CG1 CG2
REMARK 470 GLN A 878 CD OE1 NE2
REMARK 470 ARG A 883 CD NE CZ NH1 NH2
REMARK 470 ARG A 885 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 887 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 891 NE CZ NH1 NH2
REMARK 470 LEU A 892 CG CD1 CD2
REMARK 470 PHE A 894 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A 899 OD1 OD2
REMARK 470 ILE A 900 CD1
REMARK 470 ILE A 901 CG1 CG2 CD1
REMARK 470 GLU A 902 CG CD OE1 OE2
REMARK 470 LYS A 904 CG CD CE NZ
REMARK 470 ARG A 906 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 907 CG1 CG2
REMARK 470 CYS A 909 SG
REMARK 470 LEU A 917 CG CD1 CD2
REMARK 470 ASN A 927 CG OD1 ND2
REMARK 470 PHE A 928 CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 930 CD OE1 OE2
REMARK 470 LEU A 931 CG CD1 CD2
REMARK 470 LYS A 932 CD CE NZ
REMARK 470 GLU A 934 CG CD OE1 OE2
REMARK 470 GLN A 935 CG CD OE1 NE2
REMARK 470 LEU A 959 CD1 CD2
REMARK 470 GLU A 961 CD OE1 OE2
REMARK 470 LEU A 963 CG CD1 CD2
REMARK 470 LYS A 964 CG CD CE NZ
REMARK 470 ARG A 967 CD NE CZ NH1 NH2
REMARK 470 GLU A 968 CG CD OE1 OE2
REMARK 470 LYS A 972 CG CD CE NZ
REMARK 470 LYS A 975 CG CD CE NZ
REMARK 470 LYS A 978 CD CE NZ
REMARK 470 ASP A 979 OD1 OD2
REMARK 470 LYS A 981 CD CE NZ
REMARK 470 GLU A 983 CD OE1 OE2
REMARK 470 VAL A 985 CG1 CG2
REMARK 470 GLU A 986 CG CD OE1 OE2
REMARK 470 LYS A 987 CG CD CE NZ
REMARK 470 ASP A 988 CG OD1 OD2
REMARK 470 TYR A 989 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 991 CD OE1 OE2
REMARK 470 ARG A 994 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 995 CG ND1 CD2 CE1 NE2
REMARK 470 LEU A 997 CG CD1 CD2
REMARK 470 GLU A 999 CD OE1 OE2
REMARK 470 VAL A1000 CG1 CG2
REMARK 470 TYR A1002 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A1003 CG CD OE1 OE2
REMARK 470 TRP A1004 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A1004 CZ3 CH2
REMARK 470 CYS A1005 CB SG
REMARK 470 ARG A1006 CG CD NE CZ NH1 NH2
REMARK 470 THR A1009 OG1 CG2
REMARK 470 PHE A1010 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR A1011 OG1 CG2
REMARK 470 GLN A1012 CG CD OE1 NE2
REMARK 470 ILE A1013 CB CG1 CG2 CD1
REMARK 470 LYS A1015 CD CE NZ
REMARK 470 MET A1016 CG SD CE
REMARK 470 ASP A1018 CG OD1 OD2
REMARK 470 VAL A1019 CG1 CG2
REMARK 470 TYR A1020 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A1021 CD OE1 OE2
REMARK 470 ILE A1025 CD1
REMARK 470 ARG A1026 CG CD NE CZ NH1 NH2
REMARK 470 MET A1027 SD CE
REMARK 470 PHE A1028 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A1029 NZ
REMARK 470 ARG A1030 CZ NH1 NH2
REMARK 470 GLU A1032 CG CD OE1 OE2
REMARK 470 LEU A1034 CG CD1 CD2
REMARK 470 LYS A1036 CG CD CE NZ
REMARK 470 ILE A1045 CG1 CG2 CD1
REMARK 470 LYS A1051 CG CD CE NZ
REMARK 470 GLU A1052 CG CD OE1 OE2
REMARK 470 LYS A1053 CG CD CE NZ
REMARK 470 MET A1054 CG SD CE
REMARK 470 GLU A1055 CD OE1 OE2
REMARK 470 LEU A1058 CG CD1 CD2
REMARK 470 LYS A1059 CG CD CE NZ
REMARK 470 LEU A1060 CG CD1 CD2
REMARK 470 ILE A1061 CD1
REMARK 470 ARG A1063 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU A 910 OG SER A 913 2.09
REMARK 500 O GLU A 986 N ASP A 988 2.15
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 LEU A 735 CA - CB - CG ANGL. DEV. = 17.4 DEGREES
REMARK 500 LEU A 775 CA - CB - CG ANGL. DEV. = 17.6 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 GLU A 142 108.27 -59.39
REMARK 500 ALA A 143 -76.98 -56.76
REMARK 500 THR A 173 60.12 -63.48
REMARK 500 ASN A 229 77.13 18.72
REMARK 500 ARG A 248 -141.32 -79.24
REMARK 500 SER A 250 82.67 -52.69
REMARK 500 MET A 253 -41.73 -10.21
REMARK 500 GLU A 271 -98.86 -90.68
REMARK 500 ARG A 272 -9.95 -46.42
REMARK 500 LEU A 283 150.58 -23.52
REMARK 500 ASP A 285 -14.95 -40.75
REMARK 500 PRO A 297 -75.72 -55.93
REMARK 500 SER A 311 78.78 17.63
REMARK 500 PRO A 323 98.49 -59.11
REMARK 500 THR A 324 101.61 73.41
REMARK 500 ASP A 336 -39.22 -154.33
REMARK 500 LEU A 340 104.61 -53.85
REMARK 500 LYS A 345 -50.37 -133.39
REMARK 500 ARG A 349 70.14 -69.66
REMARK 500 SER A 359 29.17 -76.45
REMARK 500 TYR A 406 71.02 -104.77
REMARK 500 LEU A 429 -96.64 -71.99
REMARK 500 ASP A 430 40.85 -64.53
REMARK 500 ASN A 432 -155.13 -68.73
REMARK 500 GLU A 438 30.91 -69.07
REMARK 500 ALA A 439 -27.23 -164.13
REMARK 500 ASN A 446 19.90 -62.69
REMARK 500 ALA A 447 -70.95 -146.37
REMARK 500 GLU A 457 -133.73 -91.50
REMARK 500 LEU A 458 166.67 62.19
REMARK 500 PRO A 459 42.54 -69.47
REMARK 500 GLN A 460 -65.71 -93.56
REMARK 500 HIS A 463 -137.99 55.09
REMARK 500 ILE A 464 -60.71 50.83
REMARK 500 HIS A 476 -127.55 14.97
REMARK 500 LEU A 479 -137.42 -75.51
REMARK 500 SER A 506 8.80 -55.29
REMARK 500 ALA A 513 -112.85 -138.49
REMARK 500 LYS A 514 -56.41 54.47
REMARK 500 ASP A 525 62.46 -173.68
REMARK 500 MET A 558 106.06 -51.65
REMARK 500 ASP A 560 28.05 -170.00
REMARK 500 ASN A 588 19.61 -52.33
REMARK 500 MET A 589 -36.98 -135.46
REMARK 500 ARG A 595 -81.96 -58.52
REMARK 500 GLU A 602 -17.79 -42.50
REMARK 500 PHE A 673 -153.16 -88.18
REMARK 500 PRO A 743 151.04 -44.35
REMARK 500 GLU A 751 106.95 -54.86
REMARK 500 ASN A 772 42.15 -90.22
REMARK 500
REMARK 500 THIS ENTRY HAS 93 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 HIS A 334 GLY A 335 149.91
REMARK 500 TYR A 406 ASN A 407 -137.89
REMARK 500 HIS A 476 SER A 477 -131.85
REMARK 500 GLN A 527 GLN A 528 147.02
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 PO4 A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1103
DBREF 4QU4 A 1 1073 UNP P47047 MTR4_YEAST 1 1073
SEQADV 4QU4 MET A -34 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 HIS A -33 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 HIS A -32 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 HIS A -31 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 HIS A -30 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 HIS A -29 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 HIS A -28 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 GLY A -27 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 LYS A -26 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 PRO A -25 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 ILE A -24 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 PRO A -23 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 ASN A -22 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 PRO A -21 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 LEU A -20 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 LEU A -19 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 GLY A -18 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 LEU A -17 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 ASP A -16 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 SER A -15 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 THR A -14 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 GLU A -13 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 ASN A -12 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 LEU A -11 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 TYR A -10 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 PHE A -9 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 GLN A -8 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 GLY A -7 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 ILE A -6 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 ASP A -5 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 PRO A -4 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 PHE A -3 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 THR A -2 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 GLU A -1 UNP P47047 EXPRESSION TAG
SEQADV 4QU4 PHE A 0 UNP P47047 EXPRESSION TAG
SEQRES 1 A 1108 MET HIS HIS HIS HIS HIS HIS GLY LYS PRO ILE PRO ASN
SEQRES 2 A 1108 PRO LEU LEU GLY LEU ASP SER THR GLU ASN LEU TYR PHE
SEQRES 3 A 1108 GLN GLY ILE ASP PRO PHE THR GLU PHE MET ASP SER THR
SEQRES 4 A 1108 ASP LEU PHE ASP VAL PHE GLU GLU THR PRO VAL GLU LEU
SEQRES 5 A 1108 PRO THR ASP SER ASN GLY GLU LYS ASN ALA ASP THR ASN
SEQRES 6 A 1108 VAL GLY ASP THR PRO ASP HIS THR GLN ASP LYS LYS HIS
SEQRES 7 A 1108 GLY LEU GLU GLU GLU LYS GLU GLU HIS GLU GLU ASN ASN
SEQRES 8 A 1108 SER GLU ASN LYS LYS ILE LYS SER ASN LYS SER LYS THR
SEQRES 9 A 1108 GLU ASP LYS ASN LYS LYS VAL VAL VAL PRO VAL LEU ALA
SEQRES 10 A 1108 ASP SER PHE GLU GLN GLU ALA SER ARG GLU VAL ASP ALA
SEQRES 11 A 1108 SER LYS GLY LEU THR ASN SER GLU THR LEU GLN VAL GLU
SEQRES 12 A 1108 GLN ASP GLY LYS VAL ARG LEU SER HIS GLN VAL ARG HIS
SEQRES 13 A 1108 GLN VAL ALA LEU PRO PRO ASN TYR ASP TYR THR PRO ILE
SEQRES 14 A 1108 ALA GLU HIS LYS ARG VAL ASN GLU ALA ARG THR TYR PRO
SEQRES 15 A 1108 PHE THR LEU ASP PRO PHE GLN ASP THR ALA ILE SER CYS
SEQRES 16 A 1108 ILE ASP ARG GLY GLU SER VAL LEU VAL SER ALA HIS THR
SEQRES 17 A 1108 SER ALA GLY LYS THR VAL VAL ALA GLU TYR ALA ILE ALA
SEQRES 18 A 1108 GLN SER LEU LYS ASN LYS GLN ARG VAL ILE TYR THR SER
SEQRES 19 A 1108 PRO ILE LYS ALA LEU SER ASN GLN LYS TYR ARG GLU LEU
SEQRES 20 A 1108 LEU ALA GLU PHE GLY ASP VAL GLY LEU MET THR GLY ASP
SEQRES 21 A 1108 ILE THR ILE ASN PRO ASP ALA GLY CYS LEU VAL MET THR
SEQRES 22 A 1108 THR GLU ILE LEU ARG SER MET LEU TYR ARG GLY SER GLU
SEQRES 23 A 1108 VAL MET ARG GLU VAL ALA TRP VAL ILE PHE ASP GLU VAL
SEQRES 24 A 1108 HIS TYR MET ARG ASP LYS GLU ARG GLY VAL VAL TRP GLU
SEQRES 25 A 1108 GLU THR ILE ILE LEU LEU PRO ASP LYS VAL ARG TYR VAL
SEQRES 26 A 1108 PHE LEU SER ALA THR ILE PRO ASN ALA MET GLU PHE ALA
SEQRES 27 A 1108 GLU TRP ILE CYS LYS ILE HIS SER GLN PRO CYS HIS ILE
SEQRES 28 A 1108 VAL TYR THR ASN PHE ARG PRO THR PRO LEU GLN HIS TYR
SEQRES 29 A 1108 LEU PHE PRO ALA HIS GLY ASP GLY ILE TYR LEU VAL VAL
SEQRES 30 A 1108 ASP GLU LYS SER THR PHE ARG GLU GLU ASN PHE GLN LYS
SEQRES 31 A 1108 ALA MET ALA SER ILE SER ASN GLN ILE GLY ASP ASP PRO
SEQRES 32 A 1108 ASN SER THR ASP SER ARG GLY LYS LYS GLY GLN THR TYR
SEQRES 33 A 1108 LYS GLY GLY SER ALA LYS GLY ASP ALA LYS GLY ASP ILE
SEQRES 34 A 1108 TYR LYS ILE VAL LYS MET ILE TRP LYS LYS LYS TYR ASN
SEQRES 35 A 1108 PRO VAL ILE VAL PHE SER PHE SER LYS ARG ASP CYS GLU
SEQRES 36 A 1108 GLU LEU ALA LEU LYS MET SER LYS LEU ASP PHE ASN SER
SEQRES 37 A 1108 ASP ASP GLU LYS GLU ALA LEU THR LYS ILE PHE ASN ASN
SEQRES 38 A 1108 ALA ILE ALA LEU LEU PRO GLU THR ASP ARG GLU LEU PRO
SEQRES 39 A 1108 GLN ILE LYS HIS ILE LEU PRO LEU LEU ARG ARG GLY ILE
SEQRES 40 A 1108 GLY ILE HIS HIS SER GLY LEU LEU PRO ILE LEU LYS GLU
SEQRES 41 A 1108 VAL ILE GLU ILE LEU PHE GLN GLU GLY PHE LEU LYS VAL
SEQRES 42 A 1108 LEU PHE ALA THR GLU THR PHE SER ILE GLY LEU ASN MET
SEQRES 43 A 1108 PRO ALA LYS THR VAL VAL PHE THR SER VAL ARG LYS TRP
SEQRES 44 A 1108 ASP GLY GLN GLN PHE ARG TRP VAL SER GLY GLY GLU TYR
SEQRES 45 A 1108 ILE GLN MET SER GLY ARG ALA GLY ARG ARG GLY LEU ASP
SEQRES 46 A 1108 ASP ARG GLY ILE VAL ILE MET MET ILE ASP GLU LYS MET
SEQRES 47 A 1108 GLU PRO GLN VAL ALA LYS GLY MET VAL LYS GLY GLN ALA
SEQRES 48 A 1108 ASP ARG LEU ASP SER ALA PHE HIS LEU GLY TYR ASN MET
SEQRES 49 A 1108 ILE LEU ASN LEU MET ARG VAL GLU GLY ILE SER PRO GLU
SEQRES 50 A 1108 PHE MET LEU GLU HIS SER PHE PHE GLN PHE GLN ASN VAL
SEQRES 51 A 1108 ILE SER VAL PRO VAL MET GLU LYS LYS LEU ALA GLU LEU
SEQRES 52 A 1108 LYS LYS ASP PHE ASP GLY ILE GLU VAL GLU ASP GLU GLU
SEQRES 53 A 1108 ASN VAL LYS GLU TYR HIS GLU ILE GLU GLN ALA ILE LYS
SEQRES 54 A 1108 GLY TYR ARG GLU ASP VAL ARG GLN VAL VAL THR HIS PRO
SEQRES 55 A 1108 ALA ASN ALA LEU SER PHE LEU GLN PRO GLY ARG LEU VAL
SEQRES 56 A 1108 GLU ILE SER VAL ASN GLY LYS ASP ASN TYR GLY TRP GLY
SEQRES 57 A 1108 ALA VAL VAL ASP PHE ALA LYS ARG ILE ASN LYS ARG ASN
SEQRES 58 A 1108 PRO SER ALA VAL TYR THR ASP HIS GLU SER TYR ILE VAL
SEQRES 59 A 1108 ASN VAL VAL VAL ASN THR MET TYR ILE ASP SER PRO VAL
SEQRES 60 A 1108 ASN LEU LEU LYS PRO PHE ASN PRO THR LEU PRO GLU GLY
SEQRES 61 A 1108 ILE ARG PRO ALA GLU GLU GLY GLU LYS SER ILE CYS ALA
SEQRES 62 A 1108 VAL ILE PRO ILE THR LEU ASP SER ILE LYS SER ILE GLY
SEQRES 63 A 1108 ASN LEU ARG LEU TYR MET PRO LYS ASP ILE ARG ALA SER
SEQRES 64 A 1108 GLY GLN LYS GLU THR VAL GLY LYS SER LEU ARG GLU VAL
SEQRES 65 A 1108 ASN ARG ARG PHE PRO ASP GLY ILE PRO VAL LEU ASP PRO
SEQRES 66 A 1108 VAL LYS ASN MET LYS ILE GLU ASP GLU ASP PHE LEU LYS
SEQRES 67 A 1108 LEU MET LYS LYS ILE ASP VAL LEU ASN THR LYS LEU SER
SEQRES 68 A 1108 SER ASN PRO LEU THR ASN SER MET ARG LEU GLU GLU LEU
SEQRES 69 A 1108 TYR GLY LYS TYR SER ARG LYS HIS ASP LEU HIS GLU ASP
SEQRES 70 A 1108 MET LYS GLN LEU LYS ARG LYS ILE SER GLU SER GLN ALA
SEQRES 71 A 1108 VAL ILE GLN LEU ASP ASP LEU ARG ARG ARG LYS ARG VAL
SEQRES 72 A 1108 LEU ARG ARG LEU GLY PHE CYS THR PRO ASN ASP ILE ILE
SEQRES 73 A 1108 GLU LEU LYS GLY ARG VAL ALA CYS GLU ILE SER SER GLY
SEQRES 74 A 1108 ASP GLU LEU LEU LEU THR GLU LEU ILE PHE ASN GLY ASN
SEQRES 75 A 1108 PHE ASN GLU LEU LYS PRO GLU GLN ALA ALA ALA LEU LEU
SEQRES 76 A 1108 SER CYS PHE ALA PHE GLN GLU ARG CYS LYS GLU ALA PRO
SEQRES 77 A 1108 ARG LEU LYS PRO GLU LEU ALA GLU PRO LEU LYS ALA MET
SEQRES 78 A 1108 ARG GLU ILE ALA ALA LYS ILE ALA LYS ILE MET LYS ASP
SEQRES 79 A 1108 SER LYS ILE GLU VAL VAL GLU LYS ASP TYR VAL GLU SER
SEQRES 80 A 1108 PHE ARG HIS GLU LEU MET GLU VAL VAL TYR GLU TRP CYS
SEQRES 81 A 1108 ARG GLY ALA THR PHE THR GLN ILE CYS LYS MET THR ASP
SEQRES 82 A 1108 VAL TYR GLU GLY SER LEU ILE ARG MET PHE LYS ARG LEU
SEQRES 83 A 1108 GLU GLU LEU VAL LYS GLU LEU VAL ASP VAL ALA ASN THR
SEQRES 84 A 1108 ILE GLY ASN SER SER LEU LYS GLU LYS MET GLU ALA VAL
SEQRES 85 A 1108 LEU LYS LEU ILE HIS ARG ASP ILE VAL SER ALA GLY SER
SEQRES 86 A 1108 LEU TYR LEU
HET PO4 A1101 5
HET PO4 A1102 5
HET PO4 A1103 5
HETNAM PO4 PHOSPHATE ION
FORMUL 2 PO4 3(O4 P 3-)
HELIX 1 1 ASP A 151 GLY A 164 1 14
HELIX 2 2 GLY A 176 ASN A 191 1 16
HELIX 3 3 ILE A 201 GLY A 217 1 17
HELIX 4 4 THR A 239 ARG A 248 1 10
HELIX 5 5 GLU A 251 ARG A 254 5 4
HELIX 6 6 VAL A 264 ASP A 269 5 6
HELIX 7 7 ARG A 272 LEU A 283 1 12
HELIX 8 8 ALA A 299 HIS A 310 1 12
HELIX 9 9 ARG A 349 SER A 359 1 11
HELIX 10 10 LYS A 391 LYS A 404 1 14
HELIX 11 11 SER A 415 LYS A 425 1 11
HELIX 12 12 GLU A 436 ALA A 449 1 14
HELIX 13 13 GLU A 453 ARG A 456 5 4
HELIX 14 14 GLU A 457 LYS A 462 1 6
HELIX 15 15 ILE A 464 ARG A 469 1 6
HELIX 16 16 ILE A 482 GLU A 493 1 12
HELIX 17 17 SER A 533 GLY A 542 1 10
HELIX 18 18 GLU A 564 LYS A 573 1 10
HELIX 19 19 GLY A 586 VAL A 596 1 11
HELIX 20 20 SER A 600 GLU A 606 1 7
HELIX 21 21 SER A 608 ASP A 633 1 26
HELIX 22 22 ASP A 639 THR A 665 1 27
HELIX 23 23 ASN A 669 PHE A 673 5 5
HELIX 24 24 ASN A 685 LYS A 687 5 3
HELIX 25 25 PRO A 731 LEU A 735 5 5
HELIX 26 26 GLY A 785 PHE A 801 1 17
HELIX 27 27 ASP A 818 SER A 837 1 20
HELIX 28 28 ARG A 845 ILE A 870 1 26
HELIX 29 29 GLN A 878 ARG A 891 1 14
HELIX 30 30 ASP A 915 PHE A 924 1 10
HELIX 31 31 ALA A 936 SER A 941 1 6
HELIX 32 32 LEU A 963 SER A 980 1 18
HELIX 33 33 GLU A 999 CYS A 1005 1 7
HELIX 34 34 PHE A 1010 CYS A 1014 1 5
HELIX 35 35 SER A 1023 LYS A 1036 1 14
HELIX 36 36 SER A 1048 ARG A 1063 1 16
HELIX 37 37 ASP A 1064 VAL A 1066 5 3
SHEET 1 A10 VAL A 80 VAL A 93 0
SHEET 2 A10 VAL A 113 LEU A 125 -1 O HIS A 117 N ALA A 89
SHEET 3 A10 CYS A 314 THR A 319 -1 O TYR A 318 N ARG A 120
SHEET 4 A10 SER A 166 SER A 170 1 N LEU A 168 O HIS A 315
SHEET 5 A10 ARG A 288 SER A 293 1 O SER A 293 N VAL A 169
SHEET 6 A10 VAL A 256 ASP A 262 1 N VAL A 259 O ARG A 288
SHEET 7 A10 ARG A 194 SER A 199 1 N ARG A 194 O ALA A 257
SHEET 8 A10 CYS A 234 THR A 238 1 O LEU A 235 N TYR A 197
SHEET 9 A10 VAL A 219 MET A 222 1 N GLY A 220 O VAL A 236
SHEET 10 A10 THR A 227 ILE A 228 -1 O ILE A 228 N LEU A 221
SHEET 1 B 7 TYR A 339 VAL A 342 0
SHEET 2 B 7 LEU A 326 PHE A 331 -1 N HIS A 328 O VAL A 341
SHEET 3 B 7 GLY A 553 MET A 558 1 O VAL A 555 N TYR A 329
SHEET 4 B 7 THR A 515 PHE A 518 1 N VAL A 516 O ILE A 554
SHEET 5 B 7 VAL A 409 ILE A 410 1 N ILE A 410 O THR A 515
SHEET 6 B 7 VAL A 498 ALA A 501 1 O LEU A 499 N VAL A 409
SHEET 7 B 7 ILE A 472 HIS A 475 1 N GLY A 473 O PHE A 500
SHEET 1 C 2 ARG A 522 LYS A 523 0
SHEET 2 C 2 ARG A 530 TRP A 531 -1 O ARG A 530 N LYS A 523
SHEET 1 D 5 SER A 755 THR A 763 0
SHEET 2 D 5 TYR A 717 TYR A 727 -1 N VAL A 719 O ILE A 762
SHEET 3 D 5 ASP A 688 LYS A 700 -1 N ALA A 694 O VAL A 722
SHEET 4 D 5 ARG A 678 VAL A 684 -1 N ARG A 678 O VAL A 695
SHEET 5 D 5 ILE A 767 ARG A 774 -1 O SER A 769 N GLU A 681
CISPEP 1 LYS A 345 SER A 346 0 7.09
CISPEP 2 ILE A 507 GLY A 508 0 4.72
CISPEP 3 GLY A 526 GLN A 527 0 -10.86
SITE 1 AC1 3 GLU A 263 TYR A 266 GLY A 508
SITE 1 AC2 5 LYS A 416 HIS A 476 SER A 477 THR A 502
SITE 2 AC2 5 THR A 504
SITE 1 AC3 1 LYS A 827
CRYST1 133.516 133.516 190.949 90.00 90.00 120.00 P 31 2 1 6
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 0.007490 0.004324 0.000000 0.00000
SCALE2 0.000000 0.008648 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005237 0.00000
(ATOM LINES ARE NOT SHOWN.)
END