HEADER STRUCTURAL PROTEIN 30-MAY-14 4QIF
TITLE CRYSTAL STRUCTURE OF PDUA WITH EDGE MUTATION K26A AND PORE MUTATION
TITLE 2 S40H
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROPANEDIOL UTILIZATION PROTEIN PDUA;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR
SOURCE 3 TYPHIMURIUM;
SOURCE 4 ORGANISM_TAXID: 99287;
SOURCE 5 STRAIN: LT2 / SGSC1412 / ATCC 700720;
SOURCE 6 GENE: PDUA, STM2038;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS BMC DOMAIN, STRUCTURAL PROTEIN, POTASSIUM, GLYCEROL, 1-2 PROPANEDIOL,
KEYWDS 2 TARTARIC ACID, SULFATE ION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.H.PANG,M.R.SAWAYA,T.O.YEATES
REVDAT 5 28-FEB-24 4QIF 1 REMARK SEQADV LINK
REVDAT 4 25-MAR-15 4QIF 1 JRNL
REVDAT 3 11-MAR-15 4QIF 1 JRNL
REVDAT 2 25-FEB-15 4QIF 1 JRNL
REVDAT 1 18-FEB-15 4QIF 0
JRNL AUTH C.CHOWDHURY,S.CHUN,A.PANG,M.R.SAWAYA,S.SINHA,T.O.YEATES,
JRNL AUTH 2 T.A.BOBIK
JRNL TITL SELECTIVE MOLECULAR TRANSPORT THROUGH THE PROTEIN SHELL OF A
JRNL TITL 2 BACTERIAL MICROCOMPARTMENT ORGANELLE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 112 2990 2015
JRNL REFN ISSN 0027-8424
JRNL PMID 25713376
JRNL DOI 10.1073/PNAS.1423672112
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1555)
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 94.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 79885
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7987
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 94.2853 - 6.1986 0.99 2718 302 0.1976 0.2235
REMARK 3 2 6.1986 - 4.9201 1.00 2528 281 0.1737 0.1971
REMARK 3 3 4.9201 - 4.2981 1.00 2486 275 0.1432 0.1866
REMARK 3 4 4.2981 - 3.9051 1.00 2454 273 0.1445 0.1638
REMARK 3 5 3.9051 - 3.6252 1.00 2435 271 0.1506 0.1759
REMARK 3 6 3.6252 - 3.4115 1.00 2447 272 0.1539 0.1890
REMARK 3 7 3.4115 - 3.2406 1.00 2444 271 0.1659 0.2145
REMARK 3 8 3.2406 - 3.0996 1.00 2410 268 0.1879 0.2187
REMARK 3 9 3.0996 - 2.9802 1.00 2417 268 0.1752 0.2123
REMARK 3 10 2.9802 - 2.8774 1.00 2419 269 0.1797 0.2257
REMARK 3 11 2.8774 - 2.7874 1.00 2384 265 0.1834 0.2357
REMARK 3 12 2.7874 - 2.7077 1.00 2419 269 0.1820 0.2101
REMARK 3 13 2.7077 - 2.6364 1.00 2408 267 0.1826 0.2247
REMARK 3 14 2.6364 - 2.5721 1.00 2379 265 0.1879 0.2243
REMARK 3 15 2.5721 - 2.5136 1.00 2379 264 0.1888 0.2365
REMARK 3 16 2.5136 - 2.4601 1.00 2393 266 0.1808 0.2313
REMARK 3 17 2.4601 - 2.4109 1.00 2383 265 0.1897 0.2288
REMARK 3 18 2.4109 - 2.3654 1.00 2380 264 0.1990 0.2380
REMARK 3 19 2.3654 - 2.3232 1.00 2381 265 0.2154 0.2616
REMARK 3 20 2.3232 - 2.2838 1.00 2382 265 0.2331 0.2950
REMARK 3 21 2.2838 - 2.2469 1.00 2386 265 0.2332 0.2710
REMARK 3 22 2.2469 - 2.2124 1.00 2351 261 0.2369 0.2763
REMARK 3 23 2.2124 - 2.1798 1.00 2365 263 0.2427 0.2829
REMARK 3 24 2.1798 - 2.1491 1.00 2398 266 0.2458 0.2965
REMARK 3 25 2.1491 - 2.1201 1.00 2358 262 0.2472 0.2665
REMARK 3 26 2.1201 - 2.0925 1.00 2351 262 0.2591 0.2823
REMARK 3 27 2.0925 - 2.0664 1.00 2384 264 0.2781 0.2928
REMARK 3 28 2.0664 - 2.0415 1.00 2359 262 0.2769 0.2998
REMARK 3 29 2.0415 - 2.0177 1.00 2366 263 0.2932 0.3285
REMARK 3 30 2.0177 - 1.9951 0.81 1934 215 0.3305 0.3266
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.510
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.94
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.15
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 : 0.008 5803
REMARK 3 ANGLE : 1.189 7874
REMARK 3 CHIRALITY : 0.050 983
REMARK 3 PLANARITY : 0.006 1001
REMARK 3 DIHEDRAL : 11.405 2029
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESSEQ -10:9999)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1015 -44.2336 18.0732
REMARK 3 T TENSOR
REMARK 3 T11: 0.2235 T22: 0.3562
REMARK 3 T33: 0.3158 T12: -0.0305
REMARK 3 T13: 0.0178 T23: -0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 3.2739 L22: 1.9289
REMARK 3 L33: 4.2198 L12: 1.0496
REMARK 3 L13: 0.3062 L23: -0.4657
REMARK 3 S TENSOR
REMARK 3 S11: 0.1387 S12: -0.5404 S13: 0.2298
REMARK 3 S21: 0.1148 S22: -0.0557 S23: 0.1137
REMARK 3 S31: -0.1194 S32: -0.1760 S33: -0.0656
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESSEQ -10:9999)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.9857 -27.5993 0.1277
REMARK 3 T TENSOR
REMARK 3 T11: 0.2046 T22: 0.2316
REMARK 3 T33: 0.2480 T12: 0.0076
REMARK 3 T13: 0.0013 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 3.0072 L22: 2.0865
REMARK 3 L33: 1.6000 L12: 1.5334
REMARK 3 L13: -0.2925 L23: -0.0418
REMARK 3 S TENSOR
REMARK 3 S11: -0.0455 S12: 0.0165 S13: 0.2490
REMARK 3 S21: -0.0956 S22: 0.0176 S23: 0.1738
REMARK 3 S31: -0.1143 S32: -0.0694 S33: 0.0211
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN C AND RESSEQ -10:9999)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9487 -43.8558 -18.5899
REMARK 3 T TENSOR
REMARK 3 T11: 0.3408 T22: 0.3308
REMARK 3 T33: 0.3244 T12: -0.1081
REMARK 3 T13: -0.0527 T23: 0.0418
REMARK 3 L TENSOR
REMARK 3 L11: 3.5596 L22: 3.1672
REMARK 3 L33: 4.1915 L12: 1.2295
REMARK 3 L13: 0.3818 L23: -1.1708
REMARK 3 S TENSOR
REMARK 3 S11: -0.3575 S12: 0.4930 S13: 0.2135
REMARK 3 S21: -0.3985 S22: 0.3236 S23: 0.3522
REMARK 3 S31: -0.0720 S32: -0.1759 S33: 0.0605
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN D AND RESSEQ -10:9999)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3750 -33.5474 -18.2221
REMARK 3 T TENSOR
REMARK 3 T11: 0.3156 T22: 0.3163
REMARK 3 T33: 0.3119 T12: -0.0976
REMARK 3 T13: -0.0797 T23: 0.0798
REMARK 3 L TENSOR
REMARK 3 L11: 2.4188 L22: 1.7510
REMARK 3 L33: 3.2043 L12: 1.5435
REMARK 3 L13: -1.2266 L23: 0.1583
REMARK 3 S TENSOR
REMARK 3 S11: -0.3289 S12: 0.5396 S13: 0.2370
REMARK 3 S21: -0.5076 S22: 0.3418 S23: 0.3415
REMARK 3 S31: 0.0459 S32: -0.3743 S33: -0.0235
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN E AND RESSEQ -10:9999)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1504 -49.7235 -0.7695
REMARK 3 T TENSOR
REMARK 3 T11: 0.2259 T22: 0.1658
REMARK 3 T33: 0.2677 T12: -0.0063
REMARK 3 T13: -0.0233 T23: 0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 3.9326 L22: 1.7404
REMARK 3 L33: 2.0726 L12: 2.1389
REMARK 3 L13: -0.0826 L23: -0.5064
REMARK 3 S TENSOR
REMARK 3 S11: -0.0756 S12: 0.0135 S13: 0.3527
REMARK 3 S21: -0.0727 S22: 0.1003 S23: 0.2195
REMARK 3 S31: -0.1467 S32: -0.0647 S33: -0.0241
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN F AND RESSEQ -10:9999)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.9576 -33.0937 18.1227
REMARK 3 T TENSOR
REMARK 3 T11: 0.1659 T22: 0.2070
REMARK 3 T33: 0.2006 T12: -0.0248
REMARK 3 T13: 0.0368 T23: -0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 3.2911 L22: 2.6162
REMARK 3 L33: 4.5106 L12: 0.1776
REMARK 3 L13: 0.0228 L23: 0.8537
REMARK 3 S TENSOR
REMARK 3 S11: 0.1263 S12: -0.2719 S13: 0.3861
REMARK 3 S21: 0.0304 S22: -0.0781 S23: 0.0920
REMARK 3 S31: -0.3896 S32: 0.0670 S33: -0.0115
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN G AND RESSEQ -10:9999)
REMARK 3 ORIGIN FOR THE GROUP (A): 58.1250 -11.5142 -18.5784
REMARK 3 T TENSOR
REMARK 3 T11: 0.3069 T22: 0.2098
REMARK 3 T33: 0.2798 T12: 0.0042
REMARK 3 T13: 0.0515 T23: -0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 1.4043 L22: 3.1377
REMARK 3 L33: 3.1518 L12: 0.2380
REMARK 3 L13: 0.5255 L23: -0.8517
REMARK 3 S TENSOR
REMARK 3 S11: -0.0066 S12: 0.1705 S13: -0.0511
REMARK 3 S21: -0.4902 S22: 0.0448 S23: -0.1629
REMARK 3 S31: 0.1386 S32: 0.1200 S33: -0.0588
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN H AND RESSEQ -10:9999)
REMARK 3 ORIGIN FOR THE GROUP (A): 58.9375 -10.7498 18.8849
REMARK 3 T TENSOR
REMARK 3 T11: 0.2861 T22: 0.2830
REMARK 3 T33: 0.2641 T12: 0.0279
REMARK 3 T13: -0.0650 T23: 0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 1.0482 L22: 3.3613
REMARK 3 L33: 3.5316 L12: -0.3697
REMARK 3 L13: -0.6468 L23: -0.5523
REMARK 3 S TENSOR
REMARK 3 S11: -0.0358 S12: -0.1313 S13: -0.1074
REMARK 3 S21: 0.2572 S22: 0.0756 S23: -0.2615
REMARK 3 S31: 0.2114 S32: 0.2194 S33: -0.0462
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN I AND RESSEQ -10:9999)
REMARK 3 ORIGIN FOR THE GROUP (A): 58.8908 -21.1074 0.7243
REMARK 3 T TENSOR
REMARK 3 T11: 0.1976 T22: 0.2101
REMARK 3 T33: 0.2460 T12: 0.0170
REMARK 3 T13: -0.0168 T23: -0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 1.3370 L22: 3.4675
REMARK 3 L33: 2.7657 L12: 0.4608
REMARK 3 L13: 0.4162 L23: 0.3161
REMARK 3 S TENSOR
REMARK 3 S11: 0.0703 S12: 0.0113 S13: -0.2016
REMARK 3 S21: -0.0214 S22: -0.0093 S23: -0.3354
REMARK 3 S31: 0.2313 S32: 0.2637 S33: -0.0838
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4QIF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000086094.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : .9793
REMARK 200 MONOCHROMATOR : CRYO-COOLED DOUBLE CRYSTAL
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80002
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.995
REMARK 200 RESOLUTION RANGE LOW (A) : 94.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.050
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX (PHASER-MR)
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NA/K TARTRATE, 2.2M AMMONIUM
REMARK 280 SULFATE, PH 9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 222.86000
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 111.43000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 167.14500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 55.71500
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 278.57500
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 222.86000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 111.43000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 55.71500
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 167.14500
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 278.57500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -227.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -178.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I
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 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 GLY A 0
REMARK 465 THR A 1
REMARK 465 SER A 93
REMARK 465 GLN A 94
REMARK 465 MET B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 GLY B 0
REMARK 465 THR B 1
REMARK 465 GLN B 2
REMARK 465 GLN B 3
REMARK 465 LYS B 90
REMARK 465 GLY B 91
REMARK 465 ILE B 92
REMARK 465 SER B 93
REMARK 465 GLN B 94
REMARK 465 MET C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 GLY C 0
REMARK 465 THR C 1
REMARK 465 GLN C 2
REMARK 465 GLN C 3
REMARK 465 GLN C 94
REMARK 465 MET D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 GLY D 0
REMARK 465 THR D 1
REMARK 465 GLN D 2
REMARK 465 GLY D 91
REMARK 465 ILE D 92
REMARK 465 SER D 93
REMARK 465 GLN D 94
REMARK 465 MET E -7
REMARK 465 HIS E -6
REMARK 465 HIS E -5
REMARK 465 HIS E -4
REMARK 465 HIS E -3
REMARK 465 HIS E -2
REMARK 465 HIS E -1
REMARK 465 GLY E 0
REMARK 465 THR E 1
REMARK 465 GLN E 2
REMARK 465 PRO E 89
REMARK 465 LYS E 90
REMARK 465 GLY E 91
REMARK 465 ILE E 92
REMARK 465 SER E 93
REMARK 465 GLN E 94
REMARK 465 MET F -7
REMARK 465 HIS F -6
REMARK 465 HIS F -5
REMARK 465 HIS F -4
REMARK 465 HIS F -3
REMARK 465 HIS F -2
REMARK 465 HIS F -1
REMARK 465 GLY F 0
REMARK 465 THR F 1
REMARK 465 GLN F 2
REMARK 465 GLN F 94
REMARK 465 MET G -7
REMARK 465 HIS G -6
REMARK 465 HIS G -5
REMARK 465 HIS G -4
REMARK 465 HIS G -3
REMARK 465 HIS G -2
REMARK 465 HIS G -1
REMARK 465 GLY G 0
REMARK 465 THR G 1
REMARK 465 GLN G 2
REMARK 465 GLN G 3
REMARK 465 LEU G 88
REMARK 465 PRO G 89
REMARK 465 LYS G 90
REMARK 465 GLY G 91
REMARK 465 ILE G 92
REMARK 465 SER G 93
REMARK 465 GLN G 94
REMARK 465 MET H -7
REMARK 465 HIS H -6
REMARK 465 HIS H -5
REMARK 465 HIS H -4
REMARK 465 HIS H -3
REMARK 465 HIS H -2
REMARK 465 HIS H -1
REMARK 465 GLY H 0
REMARK 465 ILE H 92
REMARK 465 SER H 93
REMARK 465 GLN H 94
REMARK 465 MET I -7
REMARK 465 HIS I -6
REMARK 465 HIS I -5
REMARK 465 HIS I -4
REMARK 465 HIS I -3
REMARK 465 HIS I -2
REMARK 465 HIS I -1
REMARK 465 GLY I 0
REMARK 465 THR I 1
REMARK 465 GLN I 2
REMARK 465 GLN I 3
REMARK 465 LEU I 88
REMARK 465 PRO I 89
REMARK 465 LYS I 90
REMARK 465 GLY I 91
REMARK 465 ILE I 92
REMARK 465 SER I 93
REMARK 465 GLN I 94
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 C 86 CG CD CE NZ
REMARK 470 ARG E 48 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 86 CG CD CE NZ
REMARK 470 LYS G 86 CG CD CE NZ
REMARK 470 LYS I 86 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG C 79 NE - CZ - NH1 ANGL. DEV. = -3.9 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 ALA A 28 2.02 -69.13
REMARK 500 ASN E 29 31.94 -94.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 101 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 238 O
REMARK 620 2 HOH I 220 O 109.6
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO C 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR D 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR D 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR G 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGO I 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NGK RELATED DB: PDB
REMARK 900 RELATED ID: 4PPD RELATED DB: PDB
REMARK 900 RELATED ID: 4P2S RELATED DB: PDB
DBREF 4QIF A 2 94 UNP P0A1C7 PDUA_SALTY 2 94
DBREF 4QIF B 2 94 UNP P0A1C7 PDUA_SALTY 2 94
DBREF 4QIF C 2 94 UNP P0A1C7 PDUA_SALTY 2 94
DBREF 4QIF D 2 94 UNP P0A1C7 PDUA_SALTY 2 94
DBREF 4QIF E 2 94 UNP P0A1C7 PDUA_SALTY 2 94
DBREF 4QIF F 2 94 UNP P0A1C7 PDUA_SALTY 2 94
DBREF 4QIF G 2 94 UNP P0A1C7 PDUA_SALTY 2 94
DBREF 4QIF H 2 94 UNP P0A1C7 PDUA_SALTY 2 94
DBREF 4QIF I 2 94 UNP P0A1C7 PDUA_SALTY 2 94
SEQADV 4QIF MET A -7 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS A -6 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS A -5 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS A -4 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS A -3 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS A -2 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS A -1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF GLY A 0 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF THR A 1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF ALA A 26 UNP P0A1C7 LYS 26 ENGINEERED MUTATION
SEQADV 4QIF HIS A 40 UNP P0A1C7 SER 40 ENGINEERED MUTATION
SEQADV 4QIF MET B -7 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS B -6 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS B -5 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS B -4 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS B -3 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS B -2 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS B -1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF GLY B 0 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF THR B 1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF ALA B 26 UNP P0A1C7 LYS 26 ENGINEERED MUTATION
SEQADV 4QIF HIS B 40 UNP P0A1C7 SER 40 ENGINEERED MUTATION
SEQADV 4QIF MET C -7 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS C -6 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS C -5 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS C -4 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS C -3 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS C -2 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS C -1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF GLY C 0 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF THR C 1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF ALA C 26 UNP P0A1C7 LYS 26 ENGINEERED MUTATION
SEQADV 4QIF HIS C 40 UNP P0A1C7 SER 40 ENGINEERED MUTATION
SEQADV 4QIF MET D -7 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS D -6 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS D -5 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS D -4 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS D -3 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS D -2 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS D -1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF GLY D 0 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF THR D 1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF ALA D 26 UNP P0A1C7 LYS 26 ENGINEERED MUTATION
SEQADV 4QIF HIS D 40 UNP P0A1C7 SER 40 ENGINEERED MUTATION
SEQADV 4QIF MET E -7 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS E -6 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS E -5 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS E -4 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS E -3 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS E -2 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS E -1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF GLY E 0 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF THR E 1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF ALA E 26 UNP P0A1C7 LYS 26 ENGINEERED MUTATION
SEQADV 4QIF HIS E 40 UNP P0A1C7 SER 40 ENGINEERED MUTATION
SEQADV 4QIF MET F -7 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS F -6 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS F -5 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS F -4 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS F -3 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS F -2 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS F -1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF GLY F 0 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF THR F 1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF ALA F 26 UNP P0A1C7 LYS 26 ENGINEERED MUTATION
SEQADV 4QIF HIS F 40 UNP P0A1C7 SER 40 ENGINEERED MUTATION
SEQADV 4QIF MET G -7 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS G -6 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS G -5 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS G -4 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS G -3 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS G -2 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS G -1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF GLY G 0 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF THR G 1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF ALA G 26 UNP P0A1C7 LYS 26 ENGINEERED MUTATION
SEQADV 4QIF HIS G 40 UNP P0A1C7 SER 40 ENGINEERED MUTATION
SEQADV 4QIF MET H -7 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS H -6 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS H -5 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS H -4 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS H -3 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS H -2 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS H -1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF GLY H 0 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF THR H 1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF ALA H 26 UNP P0A1C7 LYS 26 ENGINEERED MUTATION
SEQADV 4QIF HIS H 40 UNP P0A1C7 SER 40 ENGINEERED MUTATION
SEQADV 4QIF MET I -7 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS I -6 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS I -5 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS I -4 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS I -3 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS I -2 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF HIS I -1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF GLY I 0 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF THR I 1 UNP P0A1C7 EXPRESSION TAG
SEQADV 4QIF ALA I 26 UNP P0A1C7 LYS 26 ENGINEERED MUTATION
SEQADV 4QIF HIS I 40 UNP P0A1C7 SER 40 ENGINEERED MUTATION
SEQRES 1 A 102 MET HIS HIS HIS HIS HIS HIS GLY THR GLN GLN GLU ALA
SEQRES 2 A 102 LEU GLY MET VAL GLU THR LYS GLY LEU THR ALA ALA ILE
SEQRES 3 A 102 GLU ALA ALA ASP ALA MET VAL ALA SER ALA ASN VAL MET
SEQRES 4 A 102 LEU VAL GLY TYR GLU LYS ILE GLY HIS GLY LEU VAL THR
SEQRES 5 A 102 VAL ILE VAL ARG GLY ASP VAL GLY ALA VAL LYS ALA ALA
SEQRES 6 A 102 THR ASP ALA GLY ALA ALA ALA ALA ARG ASN VAL GLY GLU
SEQRES 7 A 102 VAL LYS ALA VAL HIS VAL ILE PRO ARG PRO HIS THR ASP
SEQRES 8 A 102 VAL GLU LYS ILE LEU PRO LYS GLY ILE SER GLN
SEQRES 1 B 102 MET HIS HIS HIS HIS HIS HIS GLY THR GLN GLN GLU ALA
SEQRES 2 B 102 LEU GLY MET VAL GLU THR LYS GLY LEU THR ALA ALA ILE
SEQRES 3 B 102 GLU ALA ALA ASP ALA MET VAL ALA SER ALA ASN VAL MET
SEQRES 4 B 102 LEU VAL GLY TYR GLU LYS ILE GLY HIS GLY LEU VAL THR
SEQRES 5 B 102 VAL ILE VAL ARG GLY ASP VAL GLY ALA VAL LYS ALA ALA
SEQRES 6 B 102 THR ASP ALA GLY ALA ALA ALA ALA ARG ASN VAL GLY GLU
SEQRES 7 B 102 VAL LYS ALA VAL HIS VAL ILE PRO ARG PRO HIS THR ASP
SEQRES 8 B 102 VAL GLU LYS ILE LEU PRO LYS GLY ILE SER GLN
SEQRES 1 C 102 MET HIS HIS HIS HIS HIS HIS GLY THR GLN GLN GLU ALA
SEQRES 2 C 102 LEU GLY MET VAL GLU THR LYS GLY LEU THR ALA ALA ILE
SEQRES 3 C 102 GLU ALA ALA ASP ALA MET VAL ALA SER ALA ASN VAL MET
SEQRES 4 C 102 LEU VAL GLY TYR GLU LYS ILE GLY HIS GLY LEU VAL THR
SEQRES 5 C 102 VAL ILE VAL ARG GLY ASP VAL GLY ALA VAL LYS ALA ALA
SEQRES 6 C 102 THR ASP ALA GLY ALA ALA ALA ALA ARG ASN VAL GLY GLU
SEQRES 7 C 102 VAL LYS ALA VAL HIS VAL ILE PRO ARG PRO HIS THR ASP
SEQRES 8 C 102 VAL GLU LYS ILE LEU PRO LYS GLY ILE SER GLN
SEQRES 1 D 102 MET HIS HIS HIS HIS HIS HIS GLY THR GLN GLN GLU ALA
SEQRES 2 D 102 LEU GLY MET VAL GLU THR LYS GLY LEU THR ALA ALA ILE
SEQRES 3 D 102 GLU ALA ALA ASP ALA MET VAL ALA SER ALA ASN VAL MET
SEQRES 4 D 102 LEU VAL GLY TYR GLU LYS ILE GLY HIS GLY LEU VAL THR
SEQRES 5 D 102 VAL ILE VAL ARG GLY ASP VAL GLY ALA VAL LYS ALA ALA
SEQRES 6 D 102 THR ASP ALA GLY ALA ALA ALA ALA ARG ASN VAL GLY GLU
SEQRES 7 D 102 VAL LYS ALA VAL HIS VAL ILE PRO ARG PRO HIS THR ASP
SEQRES 8 D 102 VAL GLU LYS ILE LEU PRO LYS GLY ILE SER GLN
SEQRES 1 E 102 MET HIS HIS HIS HIS HIS HIS GLY THR GLN GLN GLU ALA
SEQRES 2 E 102 LEU GLY MET VAL GLU THR LYS GLY LEU THR ALA ALA ILE
SEQRES 3 E 102 GLU ALA ALA ASP ALA MET VAL ALA SER ALA ASN VAL MET
SEQRES 4 E 102 LEU VAL GLY TYR GLU LYS ILE GLY HIS GLY LEU VAL THR
SEQRES 5 E 102 VAL ILE VAL ARG GLY ASP VAL GLY ALA VAL LYS ALA ALA
SEQRES 6 E 102 THR ASP ALA GLY ALA ALA ALA ALA ARG ASN VAL GLY GLU
SEQRES 7 E 102 VAL LYS ALA VAL HIS VAL ILE PRO ARG PRO HIS THR ASP
SEQRES 8 E 102 VAL GLU LYS ILE LEU PRO LYS GLY ILE SER GLN
SEQRES 1 F 102 MET HIS HIS HIS HIS HIS HIS GLY THR GLN GLN GLU ALA
SEQRES 2 F 102 LEU GLY MET VAL GLU THR LYS GLY LEU THR ALA ALA ILE
SEQRES 3 F 102 GLU ALA ALA ASP ALA MET VAL ALA SER ALA ASN VAL MET
SEQRES 4 F 102 LEU VAL GLY TYR GLU LYS ILE GLY HIS GLY LEU VAL THR
SEQRES 5 F 102 VAL ILE VAL ARG GLY ASP VAL GLY ALA VAL LYS ALA ALA
SEQRES 6 F 102 THR ASP ALA GLY ALA ALA ALA ALA ARG ASN VAL GLY GLU
SEQRES 7 F 102 VAL LYS ALA VAL HIS VAL ILE PRO ARG PRO HIS THR ASP
SEQRES 8 F 102 VAL GLU LYS ILE LEU PRO LYS GLY ILE SER GLN
SEQRES 1 G 102 MET HIS HIS HIS HIS HIS HIS GLY THR GLN GLN GLU ALA
SEQRES 2 G 102 LEU GLY MET VAL GLU THR LYS GLY LEU THR ALA ALA ILE
SEQRES 3 G 102 GLU ALA ALA ASP ALA MET VAL ALA SER ALA ASN VAL MET
SEQRES 4 G 102 LEU VAL GLY TYR GLU LYS ILE GLY HIS GLY LEU VAL THR
SEQRES 5 G 102 VAL ILE VAL ARG GLY ASP VAL GLY ALA VAL LYS ALA ALA
SEQRES 6 G 102 THR ASP ALA GLY ALA ALA ALA ALA ARG ASN VAL GLY GLU
SEQRES 7 G 102 VAL LYS ALA VAL HIS VAL ILE PRO ARG PRO HIS THR ASP
SEQRES 8 G 102 VAL GLU LYS ILE LEU PRO LYS GLY ILE SER GLN
SEQRES 1 H 102 MET HIS HIS HIS HIS HIS HIS GLY THR GLN GLN GLU ALA
SEQRES 2 H 102 LEU GLY MET VAL GLU THR LYS GLY LEU THR ALA ALA ILE
SEQRES 3 H 102 GLU ALA ALA ASP ALA MET VAL ALA SER ALA ASN VAL MET
SEQRES 4 H 102 LEU VAL GLY TYR GLU LYS ILE GLY HIS GLY LEU VAL THR
SEQRES 5 H 102 VAL ILE VAL ARG GLY ASP VAL GLY ALA VAL LYS ALA ALA
SEQRES 6 H 102 THR ASP ALA GLY ALA ALA ALA ALA ARG ASN VAL GLY GLU
SEQRES 7 H 102 VAL LYS ALA VAL HIS VAL ILE PRO ARG PRO HIS THR ASP
SEQRES 8 H 102 VAL GLU LYS ILE LEU PRO LYS GLY ILE SER GLN
SEQRES 1 I 102 MET HIS HIS HIS HIS HIS HIS GLY THR GLN GLN GLU ALA
SEQRES 2 I 102 LEU GLY MET VAL GLU THR LYS GLY LEU THR ALA ALA ILE
SEQRES 3 I 102 GLU ALA ALA ASP ALA MET VAL ALA SER ALA ASN VAL MET
SEQRES 4 I 102 LEU VAL GLY TYR GLU LYS ILE GLY HIS GLY LEU VAL THR
SEQRES 5 I 102 VAL ILE VAL ARG GLY ASP VAL GLY ALA VAL LYS ALA ALA
SEQRES 6 I 102 THR ASP ALA GLY ALA ALA ALA ALA ARG ASN VAL GLY GLU
SEQRES 7 I 102 VAL LYS ALA VAL HIS VAL ILE PRO ARG PRO HIS THR ASP
SEQRES 8 I 102 VAL GLU LYS ILE LEU PRO LYS GLY ILE SER GLN
HET PGO A 101 5
HET SO4 A 102 5
HET SO4 A 103 10
HET SO4 A 104 5
HET SO4 A 105 5
HET K B 101 1
HET GOL B 102 6
HET SO4 B 103 5
HET SO4 B 104 5
HET SO4 C 101 5
HET PGO C 102 5
HET TAR D 101 10
HET TAR D 102 10
HET GOL D 103 6
HET SO4 D 104 5
HET GOL E 101 6
HET GOL E 102 6
HET SO4 E 103 5
HET SO4 F 101 5
HET GOL F 102 6
HET GOL F 103 6
HET TAR G 101 10
HET GOL G 102 6
HET SO4 G 103 5
HET GOL H 101 6
HET SO4 H 102 5
HET SO4 H 103 5
HET PGO I 101 5
HETNAM PGO S-1,2-PROPANEDIOL
HETNAM SO4 SULFATE ION
HETNAM K POTASSIUM ION
HETNAM GOL GLYCEROL
HETNAM TAR D(-)-TARTARIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 10 PGO 3(C3 H8 O2)
FORMUL 11 SO4 13(O4 S 2-)
FORMUL 15 K K 1+
FORMUL 16 GOL 8(C3 H8 O3)
FORMUL 21 TAR 3(C4 H6 O6)
FORMUL 38 HOH *300(H2 O)
HELIX 1 1 GLY A 13 VAL A 25 1 13
HELIX 2 2 VAL A 51 ASN A 67 1 17
HELIX 3 3 GLY B 13 VAL B 25 1 13
HELIX 4 4 ASP B 50 ARG B 66 1 17
HELIX 5 5 HIS B 81 ILE B 87 5 7
HELIX 6 6 GLY C 13 ALA C 28 1 16
HELIX 7 7 ASP C 50 ASN C 67 1 18
HELIX 8 8 ASP C 83 LEU C 88 1 6
HELIX 9 9 GLY D 13 ALA D 28 1 16
HELIX 10 10 VAL D 51 ASN D 67 1 17
HELIX 11 11 GLY E 13 VAL E 25 1 13
HELIX 12 12 ASP E 50 ARG E 66 1 17
HELIX 13 13 ASP E 83 ILE E 87 5 5
HELIX 14 14 GLY F 13 ALA F 28 1 16
HELIX 15 15 ASP F 50 ASN F 67 1 18
HELIX 16 16 ASP F 83 LEU F 88 1 6
HELIX 17 17 GLY G 13 ALA G 28 1 16
HELIX 18 18 ASP G 50 ASN G 67 1 18
HELIX 19 19 THR G 82 ILE G 87 5 6
HELIX 20 20 GLY H 13 ALA H 28 1 16
HELIX 21 21 VAL H 51 GLY H 69 1 19
HELIX 22 22 GLY I 13 VAL I 25 1 13
HELIX 23 23 ASP I 50 ARG I 66 1 17
HELIX 24 24 ASP I 83 ILE I 87 5 5
SHEET 1 A 4 VAL A 30 GLY A 39 0
SHEET 2 A 4 LEU A 42 ASP A 50 -1 O ILE A 46 N GLY A 34
SHEET 3 A 4 GLU A 4 LYS A 12 -1 N VAL A 9 O VAL A 45
SHEET 4 A 4 GLU A 70 PRO A 78 -1 O LYS A 72 N GLU A 10
SHEET 1 B 4 VAL B 30 GLY B 39 0
SHEET 2 B 4 LEU B 42 GLY B 49 -1 O ARG B 48 N MET B 31
SHEET 3 B 4 ALA B 5 LYS B 12 -1 N VAL B 9 O VAL B 45
SHEET 4 B 4 GLU B 70 ILE B 77 -1 O LYS B 72 N GLU B 10
SHEET 1 C 4 VAL C 30 GLY C 39 0
SHEET 2 C 4 LEU C 42 GLY C 49 -1 O ARG C 48 N MET C 31
SHEET 3 C 4 ALA C 5 LYS C 12 -1 N VAL C 9 O VAL C 45
SHEET 4 C 4 GLU C 70 ILE C 77 -1 O LYS C 72 N GLU C 10
SHEET 1 D 4 MET D 31 LYS D 37 0
SHEET 2 D 4 LEU D 42 ASP D 50 -1 O ARG D 48 N MET D 31
SHEET 3 D 4 GLU D 4 LYS D 12 -1 N THR D 11 O VAL D 43
SHEET 4 D 4 GLU D 70 ARG D 79 -1 O LYS D 72 N GLU D 10
SHEET 1 E 4 MET E 31 GLY E 39 0
SHEET 2 E 4 LEU E 42 GLY E 49 -1 O ARG E 48 N MET E 31
SHEET 3 E 4 ALA E 5 LYS E 12 -1 N VAL E 9 O VAL E 45
SHEET 4 E 4 GLU E 70 ILE E 77 -1 O LYS E 72 N GLU E 10
SHEET 1 F 4 MET F 31 GLY F 39 0
SHEET 2 F 4 LEU F 42 GLY F 49 -1 O ILE F 46 N VAL F 33
SHEET 3 F 4 ALA F 5 LYS F 12 -1 N VAL F 9 O VAL F 45
SHEET 4 F 4 GLU F 70 ILE F 77 -1 O LYS F 72 N GLU F 10
SHEET 1 G 4 MET G 31 LYS G 37 0
SHEET 2 G 4 LEU G 42 GLY G 49 -1 O ILE G 46 N VAL G 33
SHEET 3 G 4 ALA G 5 LYS G 12 -1 N GLY G 7 O VAL G 47
SHEET 4 G 4 GLU G 70 ILE G 77 -1 O ALA G 73 N GLU G 10
SHEET 1 H 4 MET H 31 LYS H 37 0
SHEET 2 H 4 LEU H 42 ASP H 50 -1 O ARG H 48 N MET H 31
SHEET 3 H 4 GLU H 4 LYS H 12 -1 N VAL H 9 O VAL H 45
SHEET 4 H 4 GLU H 70 ARG H 79 -1 O ILE H 77 N LEU H 6
SHEET 1 I 4 VAL I 30 GLY I 39 0
SHEET 2 I 4 LEU I 42 GLY I 49 -1 O ARG I 48 N MET I 31
SHEET 3 I 4 ALA I 5 LYS I 12 -1 N VAL I 9 O VAL I 45
SHEET 4 I 4 GLU I 70 ILE I 77 -1 O LYS I 72 N GLU I 10
LINK K K B 101 O HOH B 238 1555 1555 3.17
LINK K K B 101 O HOH I 220 1555 1555 3.04
SITE 1 AC1 5 ILE A 38 HOH A 240 SO4 C 101 LYS F 37
SITE 2 AC1 5 GLY F 39
SITE 1 AC2 5 ARG A 48 HIS A 81 ASP A 83 VAL A 84
SITE 2 AC2 5 GLU A 85
SITE 1 AC3 7 HIS A 40 HIS B 40 HIS C 40 HIS D 40
SITE 2 AC3 7 TAR D 101 HIS E 40 HIS F 40
SITE 1 AC4 7 LYS A 12 HIS A 40 LYS A 72 HOH A 236
SITE 2 AC4 7 LYS F 12 GOL F 102 GOL F 103
SITE 1 AC5 4 GLU A 36 PRO A 89 TYR F 35 LYS F 37
SITE 1 AC6 2 HOH E 209 HOH I 220
SITE 1 AC7 4 LYS B 12 HIS B 40 LYS B 72 LYS D 12
SITE 1 AC8 4 LYS B 37 HOH B 218 HOH B 239 LYS F 37
SITE 1 AC9 5 PGO A 101 HOH A 240 ILE B 38 LYS C 37
SITE 2 AC9 5 GLY D 39
SITE 1 BC1 3 MET B 31 LEU B 32 THR F 82
SITE 1 BC2 6 HOH A 240 LYS C 37 GLY C 39 ILE D 38
SITE 2 BC2 6 SO4 E 103 SO4 F 101
SITE 1 BC3 17 GLY A 39 HIS A 40 SO4 A 103 HOH A 207
SITE 2 BC3 17 HOH A 240 GLY B 39 HIS B 40 GLY C 39
SITE 3 BC3 17 HIS C 40 GLY D 39 HIS D 40 HOH D 205
SITE 4 BC3 17 HOH D 232 GLY E 39 HIS E 40 GLY F 39
SITE 5 BC3 17 HIS F 40
SITE 1 BC4 5 LYS C 12 LYS D 12 HIS D 40 LYS D 72
SITE 2 BC4 5 GOL F 102
SITE 1 BC5 2 TYR D 35 GLU D 36
SITE 1 BC6 4 ARG D 48 ASP D 83 VAL D 84 GLU D 85
SITE 1 BC7 6 ARG B 66 ASN B 67 GLY B 69 ALA E 26
SITE 2 BC7 6 SER E 27 ALA E 28
SITE 1 BC8 4 LYS A 12 LYS E 12 HIS E 40 LYS E 72
SITE 1 BC9 4 LYS C 37 PGO C 102 HOH C 228 LYS E 37
SITE 1 CC1 4 PGO C 102 HOH D 232 ILE E 38 LYS F 37
SITE 1 CC2 5 HIS A 40 SO4 A 104 HOH A 236 TAR D 102
SITE 2 CC2 5 HIS F 40
SITE 1 CC3 3 LYS A 72 SO4 A 104 LYS F 12
SITE 1 CC4 8 GLY G 39 HIS G 40 GLY H 39 HIS H 40
SITE 2 CC4 8 SO4 H 102 HOH H 206 GLY I 39 HIS I 40
SITE 1 CC5 4 HOH A 229 ALA G 56 ASP G 59 ALA G 60
SITE 1 CC6 4 LYS G 12 HIS G 40 LYS G 72 LYS H 12
SITE 1 CC7 4 ARG H 48 HIS H 81 VAL H 84 GLU H 85
SITE 1 CC8 5 HIS G 40 TAR G 101 HIS H 40 HOH H 226
SITE 2 CC8 5 HIS I 40
SITE 1 CC9 5 GLU H 36 LYS H 37 PRO H 89 GLY H 91
SITE 2 CC9 5 LYS I 37
SITE 1 DC1 4 LYS G 12 LYS I 12 HIS I 40 LYS I 72
CRYST1 108.750 108.750 334.290 90.00 90.00 120.00 P 65 2 2 108
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 0.009195 0.005309 0.000000 0.00000
SCALE2 0.000000 0.010618 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002991 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
