HEADER LYASE 13-JAN-16 5HJX
TITLE STRUCTURE FUNCTION STUDIES OF R. PALUSTRIS RUBISCO (A47V MUTANT; CABP-
TITLE 2 BOUND)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: RUBISCO;
COMPND 5 EC: 4.1.1.39;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS;
SOURCE 3 ORGANISM_TAXID: 1076;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS RUBISCO, HEXAMER, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.ARBING,A.SHIN,S.SATAGOPAN,J.A.NORTH,F.R.TABITA
REVDAT 5 15-NOV-23 5HJX 1 REMARK
REVDAT 4 27-SEP-23 5HJX 1 LINK
REVDAT 3 04-DEC-19 5HJX 1 REMARK
REVDAT 2 27-SEP-17 5HJX 1 REMARK
REVDAT 1 18-JAN-17 5HJX 0
JRNL AUTH M.A.ARBING,S.SATAGOPAN,V.A.VARALJAY,A.SHIN,F.R.TABITA
JRNL TITL STRUCTURE FUNCTION STUDIES OF R. PALUSTRIS RUBISCO.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 87.22
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.1
REMARK 3 NUMBER OF REFLECTIONS : 208046
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 20803
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 87.3226 - 5.5898 0.85 6074 676 0.1688 0.1848
REMARK 3 2 5.5898 - 4.4368 0.89 6373 707 0.1417 0.1635
REMARK 3 3 4.4368 - 3.8760 0.83 5959 661 0.1398 0.1577
REMARK 3 4 3.8760 - 3.5216 0.84 6012 668 0.1538 0.1655
REMARK 3 5 3.5216 - 3.2692 0.85 6077 674 0.1722 0.1924
REMARK 3 6 3.2692 - 3.0764 0.88 6281 698 0.1784 0.2048
REMARK 3 7 3.0764 - 2.9223 0.89 6348 706 0.1848 0.2261
REMARK 3 8 2.9223 - 2.7951 0.86 6196 688 0.1887 0.2285
REMARK 3 9 2.7951 - 2.6875 0.86 6141 683 0.1830 0.2108
REMARK 3 10 2.6875 - 2.5948 0.84 5984 665 0.1843 0.2229
REMARK 3 11 2.5948 - 2.5136 0.89 6353 706 0.1745 0.2115
REMARK 3 12 2.5136 - 2.4418 0.88 6320 703 0.1810 0.2120
REMARK 3 13 2.4418 - 2.3775 0.91 6488 719 0.1768 0.2081
REMARK 3 14 2.3775 - 2.3195 0.92 6613 734 0.1854 0.2106
REMARK 3 15 2.3195 - 2.2667 0.88 6301 700 0.1887 0.2204
REMARK 3 16 2.2667 - 2.2185 0.79 5653 628 0.2185 0.2540
REMARK 3 17 2.2185 - 2.1741 0.89 6326 703 0.2054 0.2295
REMARK 3 18 2.1741 - 2.1331 0.88 6372 708 0.2106 0.2508
REMARK 3 19 2.1331 - 2.0950 0.89 6395 711 0.2085 0.2387
REMARK 3 20 2.0950 - 2.0595 0.77 5553 617 0.2404 0.2790
REMARK 3 21 2.0595 - 2.0263 0.90 6457 718 0.2254 0.2623
REMARK 3 22 2.0263 - 1.9951 0.92 6627 736 0.2217 0.2593
REMARK 3 23 1.9951 - 1.9657 0.91 6516 725 0.2209 0.2490
REMARK 3 24 1.9657 - 1.9380 0.88 6322 702 0.2467 0.2800
REMARK 3 25 1.9380 - 1.9119 0.79 5671 630 0.2961 0.3465
REMARK 3 26 1.9119 - 1.8870 0.89 6403 712 0.2750 0.2944
REMARK 3 27 1.8870 - 1.8634 0.87 6266 695 0.2705 0.2796
REMARK 3 28 1.8634 - 1.8410 0.93 6650 739 0.2502 0.2814
REMARK 3 29 1.8410 - 1.8196 0.93 6634 737 0.2741 0.3067
REMARK 3 30 1.8196 - 1.7991 0.81 5878 654 0.2866 0.3062
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.69
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.005 21832
REMARK 3 ANGLE : 0.827 29518
REMARK 3 CHIRALITY : 0.033 3070
REMARK 3 PLANARITY : 0.004 3908
REMARK 3 DIHEDRAL : 11.380 7836
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): -27.7646-117.4985 -2.0860
REMARK 3 T TENSOR
REMARK 3 T11: 0.2994 T22: 0.2187
REMARK 3 T33: 0.3891 T12: 0.0078
REMARK 3 T13: 0.0024 T23: 0.1821
REMARK 3 L TENSOR
REMARK 3 L11: 2.0630 L22: 0.3533
REMARK 3 L33: 0.3443 L12: 0.0504
REMARK 3 L13: -0.1849 L23: 0.1722
REMARK 3 S TENSOR
REMARK 3 S11: -0.0021 S12: -0.4604 S13: -0.6922
REMARK 3 S21: 0.0948 S22: -0.0191 S23: -0.0004
REMARK 3 S31: 0.1289 S32: 0.0472 S33: 0.0269
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -14.0487-117.0751 -26.3831
REMARK 3 T TENSOR
REMARK 3 T11: 0.2666 T22: 0.1524
REMARK 3 T33: 0.3768 T12: 0.0287
REMARK 3 T13: -0.0212 T23: -0.0942
REMARK 3 L TENSOR
REMARK 3 L11: 2.0558 L22: 0.5217
REMARK 3 L33: 0.2642 L12: 0.0794
REMARK 3 L13: 0.0332 L23: -0.0096
REMARK 3 S TENSOR
REMARK 3 S11: 0.0403 S12: 0.2784 S13: -0.6926
REMARK 3 S21: -0.0440 S22: 0.0078 S23: -0.0038
REMARK 3 S31: 0.0982 S32: 0.0929 S33: -0.0291
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): -29.6265 -90.9161 -50.1684
REMARK 3 T TENSOR
REMARK 3 T11: 0.3008 T22: 0.5896
REMARK 3 T33: 0.0887 T12: 0.0499
REMARK 3 T13: -0.0151 T23: -0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 2.2435 L22: 0.6889
REMARK 3 L33: 0.4966 L12: 0.1542
REMARK 3 L13: -0.1517 L23: -0.2325
REMARK 3 S TENSOR
REMARK 3 S11: 0.0992 S12: 0.9670 S13: -0.1219
REMARK 3 S21: -0.1808 S22: -0.0546 S23: 0.0487
REMARK 3 S31: 0.0204 S32: 0.0046 S33: -0.0110
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): -27.8388 -65.4066 -39.0781
REMARK 3 T TENSOR
REMARK 3 T11: 0.3251 T22: 0.2771
REMARK 3 T33: 0.3668 T12: 0.0132
REMARK 3 T13: 0.0376 T23: 0.2106
REMARK 3 L TENSOR
REMARK 3 L11: 2.0470 L22: 0.3807
REMARK 3 L33: 0.7362 L12: 0.1919
REMARK 3 L13: 0.1670 L23: 0.0523
REMARK 3 S TENSOR
REMARK 3 S11: 0.0055 S12: 0.5550 S13: 0.6741
REMARK 3 S21: -0.0783 S22: -0.0001 S23: 0.0744
REMARK 3 S31: -0.1899 S32: 0.0413 S33: -0.0148
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN E
REMARK 3 ORIGIN FOR THE GROUP (A): -43.3003 -64.8274 -3.7993
REMARK 3 T TENSOR
REMARK 3 T11: 0.2869 T22: 0.1906
REMARK 3 T33: 0.4016 T12: -0.0025
REMARK 3 T13: 0.0494 T23: -0.1375
REMARK 3 L TENSOR
REMARK 3 L11: 2.0669 L22: 0.4352
REMARK 3 L33: 0.5139 L12: 0.0315
REMARK 3 L13: 0.0870 L23: 0.0755
REMARK 3 S TENSOR
REMARK 3 S11: 0.0230 S12: -0.3685 S13: 0.7199
REMARK 3 S21: 0.0560 S22: -0.0033 S23: 0.0583
REMARK 3 S31: -0.1211 S32: -0.0515 S33: 0.0187
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN F
REMARK 3 ORIGIN FOR THE GROUP (A): -29.4073 -82.1560 13.1337
REMARK 3 T TENSOR
REMARK 3 T11: 0.3225 T22: 0.5356
REMARK 3 T33: 0.1406 T12: -0.0345
REMARK 3 T13: 0.0280 T23: -0.1058
REMARK 3 L TENSOR
REMARK 3 L11: 2.0507 L22: 0.5849
REMARK 3 L33: 0.3451 L12: -0.0440
REMARK 3 L13: -0.1381 L23: 0.0206
REMARK 3 S TENSOR
REMARK 3 S11: 0.0507 S12: -0.8612 S13: 0.2413
REMARK 3 S21: 0.1759 S22: -0.0037 S23: 0.0071
REMARK 3 S31: -0.0487 S32: 0.0536 S33: -0.0184
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 5HJX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000217120.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7-8
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) : 0.9797
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 208202
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.799
REMARK 200 RESOLUTION RANGE LOW (A) : 87.220
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.0
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.9800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.38500
REMARK 200 R SYM FOR SHELL (I) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4LF1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN STORAGE BUFFER: 20 MM TRIS, PH
REMARK 280 8.0, 300 MM NACL, 10% GLYCEROL, 10 MM MGCL2, 20 MM NAHCO3.
REMARK 280 RESERVOIR SOLUTION: 20-24% PEG 3350, 200 MM SODIUM SULFATE, 100
REMARK 280 MM BIS-TRIS PROPANE PH 7.0-8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
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
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: HEXAMERIC
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 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 LYS A 457
REMARK 465 PRO A 458
REMARK 465 GLN A 459
REMARK 465 ALA A 460
REMARK 465 ALA A 461
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 LEU B 456
REMARK 465 LYS B 457
REMARK 465 PRO B 458
REMARK 465 GLN B 459
REMARK 465 ALA B 460
REMARK 465 ALA B 461
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 LEU C 456
REMARK 465 LYS C 457
REMARK 465 PRO C 458
REMARK 465 GLN C 459
REMARK 465 ALA C 460
REMARK 465 ALA C 461
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 LEU D 456
REMARK 465 LYS D 457
REMARK 465 PRO D 458
REMARK 465 GLN D 459
REMARK 465 ALA D 460
REMARK 465 ALA D 461
REMARK 465 MET E -19
REMARK 465 GLY E -18
REMARK 465 SER E -17
REMARK 465 SER E -16
REMARK 465 HIS E -15
REMARK 465 HIS E -14
REMARK 465 HIS E -13
REMARK 465 HIS E -12
REMARK 465 HIS E -11
REMARK 465 HIS E -10
REMARK 465 SER E -9
REMARK 465 SER E -8
REMARK 465 GLY E -7
REMARK 465 LEU E -6
REMARK 465 VAL E -5
REMARK 465 PRO E -4
REMARK 465 ARG E -3
REMARK 465 GLY E -2
REMARK 465 SER E -1
REMARK 465 HIS E 0
REMARK 465 LYS E 457
REMARK 465 PRO E 458
REMARK 465 GLN E 459
REMARK 465 ALA E 460
REMARK 465 ALA E 461
REMARK 465 MET F -19
REMARK 465 GLY F -18
REMARK 465 SER F -17
REMARK 465 SER F -16
REMARK 465 HIS F -15
REMARK 465 HIS F -14
REMARK 465 HIS F -13
REMARK 465 HIS F -12
REMARK 465 HIS F -11
REMARK 465 HIS F -10
REMARK 465 SER F -9
REMARK 465 SER F -8
REMARK 465 GLY F -7
REMARK 465 LEU F -6
REMARK 465 VAL F -5
REMARK 465 PRO F -4
REMARK 465 ARG F -3
REMARK 465 GLY F -2
REMARK 465 SER F -1
REMARK 465 HIS F 0
REMARK 465 LEU F 456
REMARK 465 LYS F 457
REMARK 465 PRO F 458
REMARK 465 GLN F 459
REMARK 465 ALA F 460
REMARK 465 ALA F 461
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 PHE A 36 -143.13 -126.24
REMARK 500 SER A 51 -81.12 -148.99
REMARK 500 THR A 54 -158.34 -143.17
REMARK 500 ILE A 110 36.85 -141.65
REMARK 500 ALA A 253 -116.01 55.70
REMARK 500 PRO A 450 -79.24 -38.26
REMARK 500 ASN A 451 38.86 -79.84
REMARK 500 PHE B 36 -142.00 -126.22
REMARK 500 ASN B 38 -168.41 -73.18
REMARK 500 SER B 51 -80.17 -150.75
REMARK 500 THR B 54 -157.55 -143.73
REMARK 500 ILE B 110 37.45 -141.22
REMARK 500 ALA B 253 -114.87 55.87
REMARK 500 TYR B 353 -31.20 -137.17
REMARK 500 ASN B 451 41.14 -109.60
REMARK 500 PHE C 36 -141.89 -125.77
REMARK 500 ASN C 38 -168.04 -74.89
REMARK 500 SER C 51 -80.95 -150.13
REMARK 500 THR C 54 -157.43 -143.23
REMARK 500 ILE C 110 37.05 -140.79
REMARK 500 ALA C 253 -113.99 56.07
REMARK 500 TYR C 353 -30.80 -136.91
REMARK 500 PHE D 36 -142.51 -126.69
REMARK 500 ASN D 38 -168.70 -73.45
REMARK 500 SER D 51 -82.08 -150.41
REMARK 500 THR D 54 -157.13 -142.73
REMARK 500 ILE D 110 36.41 -141.10
REMARK 500 ALA D 253 -114.53 55.18
REMARK 500 PHE E 36 -143.45 -125.93
REMARK 500 ASN E 38 -169.58 -72.13
REMARK 500 SER E 51 -81.18 -150.36
REMARK 500 THR E 54 -157.63 -143.46
REMARK 500 ILE E 110 35.83 -140.16
REMARK 500 ALA E 253 -114.59 55.22
REMARK 500 TYR E 353 -31.11 -137.31
REMARK 500 PHE F 36 -142.90 -125.89
REMARK 500 ASN F 38 -169.81 -72.49
REMARK 500 SER F 51 -80.25 -150.09
REMARK 500 THR F 54 -157.27 -142.97
REMARK 500 ILE F 110 36.07 -140.72
REMARK 500 ALA F 253 -113.70 55.39
REMARK 500 TYR F 353 -30.55 -137.30
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 MG A 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX A 192 OQ2
REMARK 620 2 ASP A 194 OD1 89.9
REMARK 620 3 GLU A 195 OE1 94.7 90.2
REMARK 620 4 CAP A 500 O2 88.0 105.4 164.2
REMARK 620 5 CAP A 500 O3 89.1 176.1 86.1 78.3
REMARK 620 6 CAP A 500 O6 168.0 95.6 95.9 80.3 86.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX B 192 OQ2
REMARK 620 2 ASP B 194 OD1 84.9
REMARK 620 3 GLU B 195 OE1 92.7 89.8
REMARK 620 4 CAP B 500 O2 88.3 103.1 167.1
REMARK 620 5 CAP B 500 O3 91.5 176.3 89.2 77.9
REMARK 620 6 CAP B 500 O6 165.8 96.6 101.4 77.6 87.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX C 192 OQ2
REMARK 620 2 ASP C 194 OD1 84.9
REMARK 620 3 GLU C 195 OE1 95.6 90.1
REMARK 620 4 CAP C 500 O2 88.6 101.5 168.0
REMARK 620 5 CAP C 500 O3 94.3 178.1 88.2 80.2
REMARK 620 6 CAP C 500 O6 163.1 95.1 101.3 74.9 86.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX D 192 OQ2
REMARK 620 2 ASP D 194 OD1 87.5
REMARK 620 3 GLU D 195 OE1 93.0 86.7
REMARK 620 4 CAP D 500 O2 91.0 107.6 165.3
REMARK 620 5 CAP D 500 O3 91.3 173.8 87.3 78.5
REMARK 620 6 CAP D 500 O6 168.5 97.5 97.5 77.7 84.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX E 192 OQ2
REMARK 620 2 ASP E 194 OD1 88.2
REMARK 620 3 GLU E 195 OE1 91.0 86.9
REMARK 620 4 CAP E 500 O2 91.0 105.0 168.0
REMARK 620 5 CAP E 500 O3 92.4 176.2 89.3 78.8
REMARK 620 6 CAP E 500 O6 167.3 94.6 101.6 76.3 85.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX F 192 OQ2
REMARK 620 2 ASP F 194 OD1 87.7
REMARK 620 3 GLU F 195 OE1 97.0 87.1
REMARK 620 4 CAP F 500 O2 90.3 104.9 166.3
REMARK 620 5 CAP F 500 O3 93.5 178.3 91.6 76.3
REMARK 620 6 CAP F 500 O6 163.9 95.7 98.9 73.6 83.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAP A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAP B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAP C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAP D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAP E 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAP F 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG F 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5HAN RELATED DB: PDB
REMARK 900 RELATED ID: 5HAO RELATED DB: PDB
REMARK 900 RELATED ID: 5HAT RELATED DB: PDB
REMARK 900 RELATED ID: 5HJY RELATED DB: PDB
REMARK 900 RELATED ID: 5HK4 RELATED DB: PDB
REMARK 900 RELATED ID: 5HQL RELATED DB: PDB
REMARK 900 RELATED ID: 5HQM RELATED DB: PDB
DBREF 5HJX A 1 461 UNP Q6N0W9 RBL2_RHOPA 1 461
DBREF 5HJX B 1 461 UNP Q6N0W9 RBL2_RHOPA 1 461
DBREF 5HJX C 1 461 UNP Q6N0W9 RBL2_RHOPA 1 461
DBREF 5HJX D 1 461 UNP Q6N0W9 RBL2_RHOPA 1 461
DBREF 5HJX E 1 461 UNP Q6N0W9 RBL2_RHOPA 1 461
DBREF 5HJX F 1 461 UNP Q6N0W9 RBL2_RHOPA 1 461
SEQADV 5HJX MET A -19 UNP Q6N0W9 INITIATING METHIONINE
SEQADV 5HJX GLY A -18 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER A -17 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER A -16 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS A -15 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS A -14 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS A -13 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS A -12 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS A -11 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS A -10 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER A -9 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER A -8 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX GLY A -7 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX LEU A -6 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX VAL A -5 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX PRO A -4 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX ARG A -3 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX GLY A -2 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER A -1 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS A 0 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX VAL A 47 UNP Q6N0W9 ALA 47 ENGINEERED MUTATION
SEQADV 5HJX MET B -19 UNP Q6N0W9 INITIATING METHIONINE
SEQADV 5HJX GLY B -18 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER B -17 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER B -16 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS B -15 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS B -14 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS B -13 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS B -12 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS B -11 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS B -10 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER B -9 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER B -8 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX GLY B -7 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX LEU B -6 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX VAL B -5 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX PRO B -4 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX ARG B -3 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX GLY B -2 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER B -1 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS B 0 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX VAL B 47 UNP Q6N0W9 ALA 47 ENGINEERED MUTATION
SEQADV 5HJX MET C -19 UNP Q6N0W9 INITIATING METHIONINE
SEQADV 5HJX GLY C -18 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER C -17 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER C -16 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS C -15 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS C -14 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS C -13 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS C -12 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS C -11 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS C -10 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER C -9 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER C -8 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX GLY C -7 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX LEU C -6 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX VAL C -5 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX PRO C -4 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX ARG C -3 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX GLY C -2 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER C -1 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS C 0 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX VAL C 47 UNP Q6N0W9 ALA 47 ENGINEERED MUTATION
SEQADV 5HJX MET D -19 UNP Q6N0W9 INITIATING METHIONINE
SEQADV 5HJX GLY D -18 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER D -17 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER D -16 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS D -15 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS D -14 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS D -13 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS D -12 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS D -11 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS D -10 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER D -9 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER D -8 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX GLY D -7 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX LEU D -6 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX VAL D -5 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX PRO D -4 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX ARG D -3 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX GLY D -2 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER D -1 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS D 0 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX VAL D 47 UNP Q6N0W9 ALA 47 ENGINEERED MUTATION
SEQADV 5HJX MET E -19 UNP Q6N0W9 INITIATING METHIONINE
SEQADV 5HJX GLY E -18 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER E -17 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER E -16 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS E -15 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS E -14 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS E -13 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS E -12 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS E -11 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS E -10 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER E -9 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER E -8 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX GLY E -7 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX LEU E -6 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX VAL E -5 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX PRO E -4 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX ARG E -3 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX GLY E -2 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER E -1 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS E 0 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX VAL E 47 UNP Q6N0W9 ALA 47 ENGINEERED MUTATION
SEQADV 5HJX MET F -19 UNP Q6N0W9 INITIATING METHIONINE
SEQADV 5HJX GLY F -18 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER F -17 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER F -16 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS F -15 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS F -14 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS F -13 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS F -12 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS F -11 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS F -10 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER F -9 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER F -8 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX GLY F -7 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX LEU F -6 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX VAL F -5 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX PRO F -4 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX ARG F -3 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX GLY F -2 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX SER F -1 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX HIS F 0 UNP Q6N0W9 EXPRESSION TAG
SEQADV 5HJX VAL F 47 UNP Q6N0W9 ALA 47 ENGINEERED MUTATION
SEQRES 1 A 481 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 481 LEU VAL PRO ARG GLY SER HIS MET ASP GLN SER ASN ARG
SEQRES 3 A 481 TYR ALA ASN LEU ASN LEU LYS GLU SER GLU LEU ILE ALA
SEQRES 4 A 481 GLY GLY ARG HIS VAL LEU CYS ALA TYR ILE MET LYS PRO
SEQRES 5 A 481 LYS ALA GLY PHE GLY ASN PHE ILE GLN THR ALA ALA HIS
SEQRES 6 A 481 PHE VAL ALA GLU SER SER THR GLY THR ASN VAL GLU VAL
SEQRES 7 A 481 SER THR THR ASP ASP PHE THR ARG GLY VAL ASP ALA LEU
SEQRES 8 A 481 VAL TYR GLU VAL ASP GLU ALA ASN SER LEU MET LYS ILE
SEQRES 9 A 481 ALA TYR PRO ILE GLU LEU PHE ASP ARG ASN VAL ILE ASP
SEQRES 10 A 481 GLY ARG ALA MET ILE ALA SER PHE LEU THR LEU THR ILE
SEQRES 11 A 481 GLY ASN ASN GLN GLY MET GLY ASP VAL GLU TYR ALA LYS
SEQRES 12 A 481 MET TYR ASP PHE TYR VAL PRO PRO ALA TYR LEU LYS LEU
SEQRES 13 A 481 PHE ASP GLY PRO SER THR THR ILE LYS ASP LEU TRP ARG
SEQRES 14 A 481 VAL LEU GLY ARG PRO VAL ILE ASN GLY GLY PHE ILE VAL
SEQRES 15 A 481 GLY THR ILE ILE LYS PRO LYS LEU GLY LEU ARG PRO GLN
SEQRES 16 A 481 PRO PHE ALA ASN ALA CYS TYR ASP PHE TRP LEU GLY GLY
SEQRES 17 A 481 ASP PHE ILE KCX ASN ASP GLU PRO GLN GLY ASN GLN VAL
SEQRES 18 A 481 PHE ALA PRO PHE LYS ASP THR VAL ARG ALA VAL ALA ASP
SEQRES 19 A 481 ALA MET ARG ARG ALA GLN ASP LYS THR GLY GLU ALA LYS
SEQRES 20 A 481 LEU PHE SER PHE ASN ILE THR ALA ASP ASP HIS TYR GLU
SEQRES 21 A 481 MET LEU ALA ARG GLY GLU PHE ILE LEU GLU THR PHE ALA
SEQRES 22 A 481 ASP ASN ALA ASP HIS ILE ALA PHE LEU VAL ASP GLY TYR
SEQRES 23 A 481 VAL ALA GLY PRO ALA ALA VAL THR THR ALA ARG ARG ALA
SEQRES 24 A 481 PHE PRO LYS GLN TYR LEU HIS TYR HIS ARG ALA GLY HIS
SEQRES 25 A 481 GLY ALA VAL THR SER PRO GLN SER LYS ARG GLY TYR THR
SEQRES 26 A 481 ALA PHE VAL LEU SER LYS MET ALA ARG LEU GLN GLY ALA
SEQRES 27 A 481 SER GLY ILE HIS THR GLY THR MET GLY PHE GLY LYS MET
SEQRES 28 A 481 GLU GLY GLU ALA ALA ASP ARG ALA ILE ALA TYR MET ILE
SEQRES 29 A 481 THR GLU ASP ALA ALA ASP GLY PRO TYR PHE HIS GLN GLU
SEQRES 30 A 481 TRP LEU GLY MET ASN PRO THR THR PRO ILE ILE SER GLY
SEQRES 31 A 481 GLY MET ASN ALA LEU ARG MET PRO GLY PHE PHE ASP ASN
SEQRES 32 A 481 LEU GLY HIS SER ASN LEU ILE MET THR ALA GLY GLY GLY
SEQRES 33 A 481 ALA PHE GLY HIS VAL ASP GLY GLY ALA ALA GLY ALA LYS
SEQRES 34 A 481 SER LEU ARG GLN ALA GLU GLN CYS TRP LYS GLN GLY ALA
SEQRES 35 A 481 ASP PRO VAL GLU PHE ALA LYS ASP HIS ARG GLU PHE ALA
SEQRES 36 A 481 ARG ALA PHE GLU SER PHE PRO GLN ASP ALA ASP LYS LEU
SEQRES 37 A 481 TYR PRO ASN TRP ARG ALA LYS LEU LYS PRO GLN ALA ALA
SEQRES 1 B 481 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 481 LEU VAL PRO ARG GLY SER HIS MET ASP GLN SER ASN ARG
SEQRES 3 B 481 TYR ALA ASN LEU ASN LEU LYS GLU SER GLU LEU ILE ALA
SEQRES 4 B 481 GLY GLY ARG HIS VAL LEU CYS ALA TYR ILE MET LYS PRO
SEQRES 5 B 481 LYS ALA GLY PHE GLY ASN PHE ILE GLN THR ALA ALA HIS
SEQRES 6 B 481 PHE VAL ALA GLU SER SER THR GLY THR ASN VAL GLU VAL
SEQRES 7 B 481 SER THR THR ASP ASP PHE THR ARG GLY VAL ASP ALA LEU
SEQRES 8 B 481 VAL TYR GLU VAL ASP GLU ALA ASN SER LEU MET LYS ILE
SEQRES 9 B 481 ALA TYR PRO ILE GLU LEU PHE ASP ARG ASN VAL ILE ASP
SEQRES 10 B 481 GLY ARG ALA MET ILE ALA SER PHE LEU THR LEU THR ILE
SEQRES 11 B 481 GLY ASN ASN GLN GLY MET GLY ASP VAL GLU TYR ALA LYS
SEQRES 12 B 481 MET TYR ASP PHE TYR VAL PRO PRO ALA TYR LEU LYS LEU
SEQRES 13 B 481 PHE ASP GLY PRO SER THR THR ILE LYS ASP LEU TRP ARG
SEQRES 14 B 481 VAL LEU GLY ARG PRO VAL ILE ASN GLY GLY PHE ILE VAL
SEQRES 15 B 481 GLY THR ILE ILE LYS PRO LYS LEU GLY LEU ARG PRO GLN
SEQRES 16 B 481 PRO PHE ALA ASN ALA CYS TYR ASP PHE TRP LEU GLY GLY
SEQRES 17 B 481 ASP PHE ILE KCX ASN ASP GLU PRO GLN GLY ASN GLN VAL
SEQRES 18 B 481 PHE ALA PRO PHE LYS ASP THR VAL ARG ALA VAL ALA ASP
SEQRES 19 B 481 ALA MET ARG ARG ALA GLN ASP LYS THR GLY GLU ALA LYS
SEQRES 20 B 481 LEU PHE SER PHE ASN ILE THR ALA ASP ASP HIS TYR GLU
SEQRES 21 B 481 MET LEU ALA ARG GLY GLU PHE ILE LEU GLU THR PHE ALA
SEQRES 22 B 481 ASP ASN ALA ASP HIS ILE ALA PHE LEU VAL ASP GLY TYR
SEQRES 23 B 481 VAL ALA GLY PRO ALA ALA VAL THR THR ALA ARG ARG ALA
SEQRES 24 B 481 PHE PRO LYS GLN TYR LEU HIS TYR HIS ARG ALA GLY HIS
SEQRES 25 B 481 GLY ALA VAL THR SER PRO GLN SER LYS ARG GLY TYR THR
SEQRES 26 B 481 ALA PHE VAL LEU SER LYS MET ALA ARG LEU GLN GLY ALA
SEQRES 27 B 481 SER GLY ILE HIS THR GLY THR MET GLY PHE GLY LYS MET
SEQRES 28 B 481 GLU GLY GLU ALA ALA ASP ARG ALA ILE ALA TYR MET ILE
SEQRES 29 B 481 THR GLU ASP ALA ALA ASP GLY PRO TYR PHE HIS GLN GLU
SEQRES 30 B 481 TRP LEU GLY MET ASN PRO THR THR PRO ILE ILE SER GLY
SEQRES 31 B 481 GLY MET ASN ALA LEU ARG MET PRO GLY PHE PHE ASP ASN
SEQRES 32 B 481 LEU GLY HIS SER ASN LEU ILE MET THR ALA GLY GLY GLY
SEQRES 33 B 481 ALA PHE GLY HIS VAL ASP GLY GLY ALA ALA GLY ALA LYS
SEQRES 34 B 481 SER LEU ARG GLN ALA GLU GLN CYS TRP LYS GLN GLY ALA
SEQRES 35 B 481 ASP PRO VAL GLU PHE ALA LYS ASP HIS ARG GLU PHE ALA
SEQRES 36 B 481 ARG ALA PHE GLU SER PHE PRO GLN ASP ALA ASP LYS LEU
SEQRES 37 B 481 TYR PRO ASN TRP ARG ALA LYS LEU LYS PRO GLN ALA ALA
SEQRES 1 C 481 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 481 LEU VAL PRO ARG GLY SER HIS MET ASP GLN SER ASN ARG
SEQRES 3 C 481 TYR ALA ASN LEU ASN LEU LYS GLU SER GLU LEU ILE ALA
SEQRES 4 C 481 GLY GLY ARG HIS VAL LEU CYS ALA TYR ILE MET LYS PRO
SEQRES 5 C 481 LYS ALA GLY PHE GLY ASN PHE ILE GLN THR ALA ALA HIS
SEQRES 6 C 481 PHE VAL ALA GLU SER SER THR GLY THR ASN VAL GLU VAL
SEQRES 7 C 481 SER THR THR ASP ASP PHE THR ARG GLY VAL ASP ALA LEU
SEQRES 8 C 481 VAL TYR GLU VAL ASP GLU ALA ASN SER LEU MET LYS ILE
SEQRES 9 C 481 ALA TYR PRO ILE GLU LEU PHE ASP ARG ASN VAL ILE ASP
SEQRES 10 C 481 GLY ARG ALA MET ILE ALA SER PHE LEU THR LEU THR ILE
SEQRES 11 C 481 GLY ASN ASN GLN GLY MET GLY ASP VAL GLU TYR ALA LYS
SEQRES 12 C 481 MET TYR ASP PHE TYR VAL PRO PRO ALA TYR LEU LYS LEU
SEQRES 13 C 481 PHE ASP GLY PRO SER THR THR ILE LYS ASP LEU TRP ARG
SEQRES 14 C 481 VAL LEU GLY ARG PRO VAL ILE ASN GLY GLY PHE ILE VAL
SEQRES 15 C 481 GLY THR ILE ILE LYS PRO LYS LEU GLY LEU ARG PRO GLN
SEQRES 16 C 481 PRO PHE ALA ASN ALA CYS TYR ASP PHE TRP LEU GLY GLY
SEQRES 17 C 481 ASP PHE ILE KCX ASN ASP GLU PRO GLN GLY ASN GLN VAL
SEQRES 18 C 481 PHE ALA PRO PHE LYS ASP THR VAL ARG ALA VAL ALA ASP
SEQRES 19 C 481 ALA MET ARG ARG ALA GLN ASP LYS THR GLY GLU ALA LYS
SEQRES 20 C 481 LEU PHE SER PHE ASN ILE THR ALA ASP ASP HIS TYR GLU
SEQRES 21 C 481 MET LEU ALA ARG GLY GLU PHE ILE LEU GLU THR PHE ALA
SEQRES 22 C 481 ASP ASN ALA ASP HIS ILE ALA PHE LEU VAL ASP GLY TYR
SEQRES 23 C 481 VAL ALA GLY PRO ALA ALA VAL THR THR ALA ARG ARG ALA
SEQRES 24 C 481 PHE PRO LYS GLN TYR LEU HIS TYR HIS ARG ALA GLY HIS
SEQRES 25 C 481 GLY ALA VAL THR SER PRO GLN SER LYS ARG GLY TYR THR
SEQRES 26 C 481 ALA PHE VAL LEU SER LYS MET ALA ARG LEU GLN GLY ALA
SEQRES 27 C 481 SER GLY ILE HIS THR GLY THR MET GLY PHE GLY LYS MET
SEQRES 28 C 481 GLU GLY GLU ALA ALA ASP ARG ALA ILE ALA TYR MET ILE
SEQRES 29 C 481 THR GLU ASP ALA ALA ASP GLY PRO TYR PHE HIS GLN GLU
SEQRES 30 C 481 TRP LEU GLY MET ASN PRO THR THR PRO ILE ILE SER GLY
SEQRES 31 C 481 GLY MET ASN ALA LEU ARG MET PRO GLY PHE PHE ASP ASN
SEQRES 32 C 481 LEU GLY HIS SER ASN LEU ILE MET THR ALA GLY GLY GLY
SEQRES 33 C 481 ALA PHE GLY HIS VAL ASP GLY GLY ALA ALA GLY ALA LYS
SEQRES 34 C 481 SER LEU ARG GLN ALA GLU GLN CYS TRP LYS GLN GLY ALA
SEQRES 35 C 481 ASP PRO VAL GLU PHE ALA LYS ASP HIS ARG GLU PHE ALA
SEQRES 36 C 481 ARG ALA PHE GLU SER PHE PRO GLN ASP ALA ASP LYS LEU
SEQRES 37 C 481 TYR PRO ASN TRP ARG ALA LYS LEU LYS PRO GLN ALA ALA
SEQRES 1 D 481 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 481 LEU VAL PRO ARG GLY SER HIS MET ASP GLN SER ASN ARG
SEQRES 3 D 481 TYR ALA ASN LEU ASN LEU LYS GLU SER GLU LEU ILE ALA
SEQRES 4 D 481 GLY GLY ARG HIS VAL LEU CYS ALA TYR ILE MET LYS PRO
SEQRES 5 D 481 LYS ALA GLY PHE GLY ASN PHE ILE GLN THR ALA ALA HIS
SEQRES 6 D 481 PHE VAL ALA GLU SER SER THR GLY THR ASN VAL GLU VAL
SEQRES 7 D 481 SER THR THR ASP ASP PHE THR ARG GLY VAL ASP ALA LEU
SEQRES 8 D 481 VAL TYR GLU VAL ASP GLU ALA ASN SER LEU MET LYS ILE
SEQRES 9 D 481 ALA TYR PRO ILE GLU LEU PHE ASP ARG ASN VAL ILE ASP
SEQRES 10 D 481 GLY ARG ALA MET ILE ALA SER PHE LEU THR LEU THR ILE
SEQRES 11 D 481 GLY ASN ASN GLN GLY MET GLY ASP VAL GLU TYR ALA LYS
SEQRES 12 D 481 MET TYR ASP PHE TYR VAL PRO PRO ALA TYR LEU LYS LEU
SEQRES 13 D 481 PHE ASP GLY PRO SER THR THR ILE LYS ASP LEU TRP ARG
SEQRES 14 D 481 VAL LEU GLY ARG PRO VAL ILE ASN GLY GLY PHE ILE VAL
SEQRES 15 D 481 GLY THR ILE ILE LYS PRO LYS LEU GLY LEU ARG PRO GLN
SEQRES 16 D 481 PRO PHE ALA ASN ALA CYS TYR ASP PHE TRP LEU GLY GLY
SEQRES 17 D 481 ASP PHE ILE KCX ASN ASP GLU PRO GLN GLY ASN GLN VAL
SEQRES 18 D 481 PHE ALA PRO PHE LYS ASP THR VAL ARG ALA VAL ALA ASP
SEQRES 19 D 481 ALA MET ARG ARG ALA GLN ASP LYS THR GLY GLU ALA LYS
SEQRES 20 D 481 LEU PHE SER PHE ASN ILE THR ALA ASP ASP HIS TYR GLU
SEQRES 21 D 481 MET LEU ALA ARG GLY GLU PHE ILE LEU GLU THR PHE ALA
SEQRES 22 D 481 ASP ASN ALA ASP HIS ILE ALA PHE LEU VAL ASP GLY TYR
SEQRES 23 D 481 VAL ALA GLY PRO ALA ALA VAL THR THR ALA ARG ARG ALA
SEQRES 24 D 481 PHE PRO LYS GLN TYR LEU HIS TYR HIS ARG ALA GLY HIS
SEQRES 25 D 481 GLY ALA VAL THR SER PRO GLN SER LYS ARG GLY TYR THR
SEQRES 26 D 481 ALA PHE VAL LEU SER LYS MET ALA ARG LEU GLN GLY ALA
SEQRES 27 D 481 SER GLY ILE HIS THR GLY THR MET GLY PHE GLY LYS MET
SEQRES 28 D 481 GLU GLY GLU ALA ALA ASP ARG ALA ILE ALA TYR MET ILE
SEQRES 29 D 481 THR GLU ASP ALA ALA ASP GLY PRO TYR PHE HIS GLN GLU
SEQRES 30 D 481 TRP LEU GLY MET ASN PRO THR THR PRO ILE ILE SER GLY
SEQRES 31 D 481 GLY MET ASN ALA LEU ARG MET PRO GLY PHE PHE ASP ASN
SEQRES 32 D 481 LEU GLY HIS SER ASN LEU ILE MET THR ALA GLY GLY GLY
SEQRES 33 D 481 ALA PHE GLY HIS VAL ASP GLY GLY ALA ALA GLY ALA LYS
SEQRES 34 D 481 SER LEU ARG GLN ALA GLU GLN CYS TRP LYS GLN GLY ALA
SEQRES 35 D 481 ASP PRO VAL GLU PHE ALA LYS ASP HIS ARG GLU PHE ALA
SEQRES 36 D 481 ARG ALA PHE GLU SER PHE PRO GLN ASP ALA ASP LYS LEU
SEQRES 37 D 481 TYR PRO ASN TRP ARG ALA LYS LEU LYS PRO GLN ALA ALA
SEQRES 1 E 481 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 E 481 LEU VAL PRO ARG GLY SER HIS MET ASP GLN SER ASN ARG
SEQRES 3 E 481 TYR ALA ASN LEU ASN LEU LYS GLU SER GLU LEU ILE ALA
SEQRES 4 E 481 GLY GLY ARG HIS VAL LEU CYS ALA TYR ILE MET LYS PRO
SEQRES 5 E 481 LYS ALA GLY PHE GLY ASN PHE ILE GLN THR ALA ALA HIS
SEQRES 6 E 481 PHE VAL ALA GLU SER SER THR GLY THR ASN VAL GLU VAL
SEQRES 7 E 481 SER THR THR ASP ASP PHE THR ARG GLY VAL ASP ALA LEU
SEQRES 8 E 481 VAL TYR GLU VAL ASP GLU ALA ASN SER LEU MET LYS ILE
SEQRES 9 E 481 ALA TYR PRO ILE GLU LEU PHE ASP ARG ASN VAL ILE ASP
SEQRES 10 E 481 GLY ARG ALA MET ILE ALA SER PHE LEU THR LEU THR ILE
SEQRES 11 E 481 GLY ASN ASN GLN GLY MET GLY ASP VAL GLU TYR ALA LYS
SEQRES 12 E 481 MET TYR ASP PHE TYR VAL PRO PRO ALA TYR LEU LYS LEU
SEQRES 13 E 481 PHE ASP GLY PRO SER THR THR ILE LYS ASP LEU TRP ARG
SEQRES 14 E 481 VAL LEU GLY ARG PRO VAL ILE ASN GLY GLY PHE ILE VAL
SEQRES 15 E 481 GLY THR ILE ILE LYS PRO LYS LEU GLY LEU ARG PRO GLN
SEQRES 16 E 481 PRO PHE ALA ASN ALA CYS TYR ASP PHE TRP LEU GLY GLY
SEQRES 17 E 481 ASP PHE ILE KCX ASN ASP GLU PRO GLN GLY ASN GLN VAL
SEQRES 18 E 481 PHE ALA PRO PHE LYS ASP THR VAL ARG ALA VAL ALA ASP
SEQRES 19 E 481 ALA MET ARG ARG ALA GLN ASP LYS THR GLY GLU ALA LYS
SEQRES 20 E 481 LEU PHE SER PHE ASN ILE THR ALA ASP ASP HIS TYR GLU
SEQRES 21 E 481 MET LEU ALA ARG GLY GLU PHE ILE LEU GLU THR PHE ALA
SEQRES 22 E 481 ASP ASN ALA ASP HIS ILE ALA PHE LEU VAL ASP GLY TYR
SEQRES 23 E 481 VAL ALA GLY PRO ALA ALA VAL THR THR ALA ARG ARG ALA
SEQRES 24 E 481 PHE PRO LYS GLN TYR LEU HIS TYR HIS ARG ALA GLY HIS
SEQRES 25 E 481 GLY ALA VAL THR SER PRO GLN SER LYS ARG GLY TYR THR
SEQRES 26 E 481 ALA PHE VAL LEU SER LYS MET ALA ARG LEU GLN GLY ALA
SEQRES 27 E 481 SER GLY ILE HIS THR GLY THR MET GLY PHE GLY LYS MET
SEQRES 28 E 481 GLU GLY GLU ALA ALA ASP ARG ALA ILE ALA TYR MET ILE
SEQRES 29 E 481 THR GLU ASP ALA ALA ASP GLY PRO TYR PHE HIS GLN GLU
SEQRES 30 E 481 TRP LEU GLY MET ASN PRO THR THR PRO ILE ILE SER GLY
SEQRES 31 E 481 GLY MET ASN ALA LEU ARG MET PRO GLY PHE PHE ASP ASN
SEQRES 32 E 481 LEU GLY HIS SER ASN LEU ILE MET THR ALA GLY GLY GLY
SEQRES 33 E 481 ALA PHE GLY HIS VAL ASP GLY GLY ALA ALA GLY ALA LYS
SEQRES 34 E 481 SER LEU ARG GLN ALA GLU GLN CYS TRP LYS GLN GLY ALA
SEQRES 35 E 481 ASP PRO VAL GLU PHE ALA LYS ASP HIS ARG GLU PHE ALA
SEQRES 36 E 481 ARG ALA PHE GLU SER PHE PRO GLN ASP ALA ASP LYS LEU
SEQRES 37 E 481 TYR PRO ASN TRP ARG ALA LYS LEU LYS PRO GLN ALA ALA
SEQRES 1 F 481 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 F 481 LEU VAL PRO ARG GLY SER HIS MET ASP GLN SER ASN ARG
SEQRES 3 F 481 TYR ALA ASN LEU ASN LEU LYS GLU SER GLU LEU ILE ALA
SEQRES 4 F 481 GLY GLY ARG HIS VAL LEU CYS ALA TYR ILE MET LYS PRO
SEQRES 5 F 481 LYS ALA GLY PHE GLY ASN PHE ILE GLN THR ALA ALA HIS
SEQRES 6 F 481 PHE VAL ALA GLU SER SER THR GLY THR ASN VAL GLU VAL
SEQRES 7 F 481 SER THR THR ASP ASP PHE THR ARG GLY VAL ASP ALA LEU
SEQRES 8 F 481 VAL TYR GLU VAL ASP GLU ALA ASN SER LEU MET LYS ILE
SEQRES 9 F 481 ALA TYR PRO ILE GLU LEU PHE ASP ARG ASN VAL ILE ASP
SEQRES 10 F 481 GLY ARG ALA MET ILE ALA SER PHE LEU THR LEU THR ILE
SEQRES 11 F 481 GLY ASN ASN GLN GLY MET GLY ASP VAL GLU TYR ALA LYS
SEQRES 12 F 481 MET TYR ASP PHE TYR VAL PRO PRO ALA TYR LEU LYS LEU
SEQRES 13 F 481 PHE ASP GLY PRO SER THR THR ILE LYS ASP LEU TRP ARG
SEQRES 14 F 481 VAL LEU GLY ARG PRO VAL ILE ASN GLY GLY PHE ILE VAL
SEQRES 15 F 481 GLY THR ILE ILE LYS PRO LYS LEU GLY LEU ARG PRO GLN
SEQRES 16 F 481 PRO PHE ALA ASN ALA CYS TYR ASP PHE TRP LEU GLY GLY
SEQRES 17 F 481 ASP PHE ILE KCX ASN ASP GLU PRO GLN GLY ASN GLN VAL
SEQRES 18 F 481 PHE ALA PRO PHE LYS ASP THR VAL ARG ALA VAL ALA ASP
SEQRES 19 F 481 ALA MET ARG ARG ALA GLN ASP LYS THR GLY GLU ALA LYS
SEQRES 20 F 481 LEU PHE SER PHE ASN ILE THR ALA ASP ASP HIS TYR GLU
SEQRES 21 F 481 MET LEU ALA ARG GLY GLU PHE ILE LEU GLU THR PHE ALA
SEQRES 22 F 481 ASP ASN ALA ASP HIS ILE ALA PHE LEU VAL ASP GLY TYR
SEQRES 23 F 481 VAL ALA GLY PRO ALA ALA VAL THR THR ALA ARG ARG ALA
SEQRES 24 F 481 PHE PRO LYS GLN TYR LEU HIS TYR HIS ARG ALA GLY HIS
SEQRES 25 F 481 GLY ALA VAL THR SER PRO GLN SER LYS ARG GLY TYR THR
SEQRES 26 F 481 ALA PHE VAL LEU SER LYS MET ALA ARG LEU GLN GLY ALA
SEQRES 27 F 481 SER GLY ILE HIS THR GLY THR MET GLY PHE GLY LYS MET
SEQRES 28 F 481 GLU GLY GLU ALA ALA ASP ARG ALA ILE ALA TYR MET ILE
SEQRES 29 F 481 THR GLU ASP ALA ALA ASP GLY PRO TYR PHE HIS GLN GLU
SEQRES 30 F 481 TRP LEU GLY MET ASN PRO THR THR PRO ILE ILE SER GLY
SEQRES 31 F 481 GLY MET ASN ALA LEU ARG MET PRO GLY PHE PHE ASP ASN
SEQRES 32 F 481 LEU GLY HIS SER ASN LEU ILE MET THR ALA GLY GLY GLY
SEQRES 33 F 481 ALA PHE GLY HIS VAL ASP GLY GLY ALA ALA GLY ALA LYS
SEQRES 34 F 481 SER LEU ARG GLN ALA GLU GLN CYS TRP LYS GLN GLY ALA
SEQRES 35 F 481 ASP PRO VAL GLU PHE ALA LYS ASP HIS ARG GLU PHE ALA
SEQRES 36 F 481 ARG ALA PHE GLU SER PHE PRO GLN ASP ALA ASP LYS LEU
SEQRES 37 F 481 TYR PRO ASN TRP ARG ALA LYS LEU LYS PRO GLN ALA ALA
MODRES 5HJX KCX A 192 LYS MODIFIED RESIDUE
MODRES 5HJX KCX B 192 LYS MODIFIED RESIDUE
MODRES 5HJX KCX C 192 LYS MODIFIED RESIDUE
MODRES 5HJX KCX D 192 LYS MODIFIED RESIDUE
MODRES 5HJX KCX E 192 LYS MODIFIED RESIDUE
MODRES 5HJX KCX F 192 LYS MODIFIED RESIDUE
HET KCX A 192 21
HET KCX B 192 21
HET KCX C 192 21
HET KCX D 192 21
HET KCX E 192 21
HET KCX F 192 21
HET CAP A 500 28
HET MG A 501 1
HET CAP B 500 28
HET MG B 501 1
HET CAP C 500 28
HET MG C 501 1
HET CAP D 500 28
HET MG D 501 1
HET CAP E 500 28
HET MG E 501 1
HET CAP F 500 28
HET MG F 501 1
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 1 KCX 6(C7 H14 N2 O4)
FORMUL 7 CAP 6(C6 H14 O13 P2)
FORMUL 8 MG 6(MG 2+)
FORMUL 19 HOH *1637(H2 O)
HELIX 1 AA1 GLN A 3 ALA A 8 1 6
HELIX 2 AA2 LYS A 13 GLY A 21 1 9
HELIX 3 AA3 ASN A 38 GLU A 49 1 12
HELIX 4 AA4 ASP A 62 VAL A 68 1 7
HELIX 5 AA5 GLU A 77 ASN A 79 5 3
HELIX 6 AA6 GLU A 89 PHE A 91 5 3
HELIX 7 AA7 MET A 101 ILE A 110 1 10
HELIX 8 AA8 GLY A 111 GLY A 115 5 5
HELIX 9 AA9 PRO A 130 LYS A 135 1 6
HELIX 10 AB1 THR A 143 GLY A 152 1 10
HELIX 11 AB2 ARG A 173 LEU A 186 1 14
HELIX 12 AB3 PRO A 204 GLY A 224 1 21
HELIX 13 AB4 ASP A 237 ALA A 253 1 17
HELIX 14 AB5 ASP A 254 ASP A 257 5 4
HELIX 15 AB6 GLY A 265 GLY A 269 1 5
HELIX 16 AB7 GLY A 269 PHE A 280 1 12
HELIX 17 AB8 HIS A 292 SER A 297 1 6
HELIX 18 AB9 THR A 305 GLY A 317 1 13
HELIX 19 AC1 GLU A 334 ALA A 336 5 3
HELIX 20 AC2 ASP A 337 GLU A 346 1 10
HELIX 21 AC3 ARG A 376 GLY A 385 1 10
HELIX 22 AC4 ALA A 393 GLY A 399 1 7
HELIX 23 AC5 GLY A 403 GLN A 420 1 18
HELIX 24 AC6 ASP A 423 LYS A 429 1 7
HELIX 25 AC7 HIS A 431 PHE A 441 1 11
HELIX 26 AC8 PHE A 441 TYR A 449 1 9
HELIX 27 AC9 PRO A 450 ARG A 453 5 4
HELIX 28 AD1 GLN B 3 ALA B 8 1 6
HELIX 29 AD2 LYS B 13 GLY B 21 1 9
HELIX 30 AD3 ASN B 38 GLU B 49 1 12
HELIX 31 AD4 ASP B 62 VAL B 68 1 7
HELIX 32 AD5 GLU B 77 ASN B 79 5 3
HELIX 33 AD6 GLU B 89 PHE B 91 5 3
HELIX 34 AD7 MET B 101 ILE B 110 1 10
HELIX 35 AD8 GLY B 111 GLY B 115 5 5
HELIX 36 AD9 PRO B 130 LYS B 135 1 6
HELIX 37 AE1 THR B 143 GLY B 152 1 10
HELIX 38 AE2 ARG B 173 LEU B 186 1 14
HELIX 39 AE3 PRO B 204 GLY B 224 1 21
HELIX 40 AE4 ASP B 237 ALA B 253 1 17
HELIX 41 AE5 ASP B 254 ASP B 257 5 4
HELIX 42 AE6 GLY B 265 GLY B 269 1 5
HELIX 43 AE7 GLY B 269 PHE B 280 1 12
HELIX 44 AE8 HIS B 292 SER B 297 1 6
HELIX 45 AE9 THR B 305 GLY B 317 1 13
HELIX 46 AF1 GLU B 334 ALA B 336 5 3
HELIX 47 AF2 ASP B 337 GLU B 346 1 10
HELIX 48 AF3 ASN B 373 LEU B 375 5 3
HELIX 49 AF4 ARG B 376 GLY B 385 1 10
HELIX 50 AF5 ALA B 393 GLY B 399 1 7
HELIX 51 AF6 GLY B 403 GLN B 420 1 18
HELIX 52 AF7 ASP B 423 LYS B 429 1 7
HELIX 53 AF8 HIS B 431 PHE B 441 1 11
HELIX 54 AF9 PHE B 441 TYR B 449 1 9
HELIX 55 AG1 GLN C 3 ALA C 8 1 6
HELIX 56 AG2 LYS C 13 GLY C 21 1 9
HELIX 57 AG3 ASN C 38 GLU C 49 1 12
HELIX 58 AG4 ASP C 62 VAL C 68 1 7
HELIX 59 AG5 GLU C 77 ASN C 79 5 3
HELIX 60 AG6 GLU C 89 PHE C 91 5 3
HELIX 61 AG7 MET C 101 ILE C 110 1 10
HELIX 62 AG8 GLY C 111 GLY C 115 5 5
HELIX 63 AG9 PRO C 130 LYS C 135 1 6
HELIX 64 AH1 THR C 143 GLY C 152 1 10
HELIX 65 AH2 ARG C 173 LEU C 186 1 14
HELIX 66 AH3 PRO C 204 GLY C 224 1 21
HELIX 67 AH4 ASP C 237 ALA C 253 1 17
HELIX 68 AH5 ASP C 254 ASP C 257 5 4
HELIX 69 AH6 GLY C 265 GLY C 269 1 5
HELIX 70 AH7 GLY C 269 PHE C 280 1 12
HELIX 71 AH8 HIS C 292 SER C 297 1 6
HELIX 72 AH9 THR C 305 GLY C 317 1 13
HELIX 73 AI1 GLU C 334 ALA C 336 5 3
HELIX 74 AI2 ASP C 337 GLU C 346 1 10
HELIX 75 AI3 ARG C 376 GLY C 385 1 10
HELIX 76 AI4 ALA C 393 GLY C 399 1 7
HELIX 77 AI5 GLY C 403 GLY C 421 1 19
HELIX 78 AI6 ASP C 423 LYS C 429 1 7
HELIX 79 AI7 HIS C 431 PHE C 441 1 11
HELIX 80 AI8 PHE C 441 TYR C 449 1 9
HELIX 81 AI9 GLN D 3 ALA D 8 1 6
HELIX 82 AJ1 LYS D 13 GLY D 21 1 9
HELIX 83 AJ2 ASN D 38 GLU D 49 1 12
HELIX 84 AJ3 ASP D 62 VAL D 68 1 7
HELIX 85 AJ4 GLU D 77 ASN D 79 5 3
HELIX 86 AJ5 GLU D 89 PHE D 91 5 3
HELIX 87 AJ6 MET D 101 ILE D 110 1 10
HELIX 88 AJ7 GLY D 111 GLY D 115 5 5
HELIX 89 AJ8 PRO D 130 LYS D 135 1 6
HELIX 90 AJ9 THR D 143 GLY D 152 1 10
HELIX 91 AK1 ARG D 173 LEU D 186 1 14
HELIX 92 AK2 PRO D 204 GLY D 224 1 21
HELIX 93 AK3 ASP D 237 ALA D 253 1 17
HELIX 94 AK4 ASP D 254 ASP D 257 5 4
HELIX 95 AK5 GLY D 265 GLY D 269 1 5
HELIX 96 AK6 GLY D 269 PHE D 280 1 12
HELIX 97 AK7 HIS D 292 SER D 297 1 6
HELIX 98 AK8 THR D 305 GLY D 317 1 13
HELIX 99 AK9 GLU D 334 ALA D 336 5 3
HELIX 100 AL1 ASP D 337 GLU D 346 1 10
HELIX 101 AL2 ARG D 376 GLY D 385 1 10
HELIX 102 AL3 ALA D 393 GLY D 399 1 7
HELIX 103 AL4 GLY D 403 GLN D 420 1 18
HELIX 104 AL5 ASP D 423 LYS D 429 1 7
HELIX 105 AL6 HIS D 431 PHE D 441 1 11
HELIX 106 AL7 PHE D 441 TYR D 449 1 9
HELIX 107 AL8 GLN E 3 ALA E 8 1 6
HELIX 108 AL9 LYS E 13 GLY E 21 1 9
HELIX 109 AM1 ASN E 38 GLU E 49 1 12
HELIX 110 AM2 ASP E 62 VAL E 68 1 7
HELIX 111 AM3 GLU E 77 ASN E 79 5 3
HELIX 112 AM4 GLU E 89 PHE E 91 5 3
HELIX 113 AM5 MET E 101 ILE E 110 1 10
HELIX 114 AM6 GLY E 111 GLY E 115 5 5
HELIX 115 AM7 PRO E 130 LYS E 135 1 6
HELIX 116 AM8 THR E 143 GLY E 152 1 10
HELIX 117 AM9 ARG E 173 LEU E 186 1 14
HELIX 118 AN1 PRO E 204 GLY E 224 1 21
HELIX 119 AN2 ASP E 237 ALA E 253 1 17
HELIX 120 AN3 ASP E 254 ASP E 257 5 4
HELIX 121 AN4 GLY E 265 GLY E 269 1 5
HELIX 122 AN5 GLY E 269 PHE E 280 1 12
HELIX 123 AN6 HIS E 292 SER E 297 1 6
HELIX 124 AN7 THR E 305 GLY E 317 1 13
HELIX 125 AN8 GLU E 334 ALA E 336 5 3
HELIX 126 AN9 ASP E 337 GLU E 346 1 10
HELIX 127 AO1 ARG E 376 GLY E 385 1 10
HELIX 128 AO2 ALA E 393 GLY E 399 1 7
HELIX 129 AO3 GLY E 403 GLN E 420 1 18
HELIX 130 AO4 ASP E 423 LYS E 429 1 7
HELIX 131 AO5 HIS E 431 PHE E 441 1 11
HELIX 132 AO6 PHE E 441 TYR E 449 1 9
HELIX 133 AO7 ASN E 451 LEU E 456 1 6
HELIX 134 AO8 GLN F 3 ALA F 8 1 6
HELIX 135 AO9 LYS F 13 GLY F 21 1 9
HELIX 136 AP1 ASN F 38 GLU F 49 1 12
HELIX 137 AP2 ASP F 62 VAL F 68 1 7
HELIX 138 AP3 GLU F 77 ASN F 79 5 3
HELIX 139 AP4 GLU F 89 PHE F 91 5 3
HELIX 140 AP5 MET F 101 ILE F 110 1 10
HELIX 141 AP6 GLY F 111 GLY F 115 5 5
HELIX 142 AP7 PRO F 130 LYS F 135 1 6
HELIX 143 AP8 THR F 143 GLY F 152 1 10
HELIX 144 AP9 ARG F 173 LEU F 186 1 14
HELIX 145 AQ1 PRO F 204 GLY F 224 1 21
HELIX 146 AQ2 ASP F 237 ALA F 253 1 17
HELIX 147 AQ3 ASP F 254 ASP F 257 5 4
HELIX 148 AQ4 GLY F 265 GLY F 269 1 5
HELIX 149 AQ5 GLY F 269 PHE F 280 1 12
HELIX 150 AQ6 HIS F 292 SER F 297 1 6
HELIX 151 AQ7 THR F 305 GLY F 317 1 13
HELIX 152 AQ8 GLU F 334 ALA F 336 5 3
HELIX 153 AQ9 ASP F 337 GLU F 346 1 10
HELIX 154 AR1 ARG F 376 GLY F 385 1 10
HELIX 155 AR2 GLY F 394 GLY F 399 1 6
HELIX 156 AR3 GLY F 403 GLN F 420 1 18
HELIX 157 AR4 ASP F 423 LYS F 429 1 7
HELIX 158 AR5 HIS F 431 PHE F 441 1 11
HELIX 159 AR6 PHE F 441 TYR F 449 1 9
SHEET 1 AA1 5 LEU A 71 ASP A 76 0
SHEET 2 AA1 5 LEU A 81 PRO A 87 -1 O ALA A 85 N LEU A 71
SHEET 3 AA1 5 HIS A 23 PRO A 32 -1 N VAL A 24 O TYR A 86
SHEET 4 AA1 5 VAL A 119 TYR A 128 -1 O TYR A 128 N LEU A 25
SHEET 5 AA1 5 GLY A 303 TYR A 304 1 O GLY A 303 N MET A 124
SHEET 1 AA2 9 ILE A 161 ILE A 165 0
SHEET 2 AA2 9 PHE A 190 KCX A 192 1 O PHE A 190 N VAL A 162
SHEET 3 AA2 9 LEU A 228 ASN A 232 1 O SER A 230 N ILE A 191
SHEET 4 AA2 9 ILE A 259 ASP A 264 1 O LEU A 262 N PHE A 231
SHEET 5 AA2 9 TYR A 284 HIS A 288 1 O HIS A 286 N PHE A 261
SHEET 6 AA2 9 GLY A 320 HIS A 322 1 O GLY A 320 N TYR A 287
SHEET 7 AA2 9 THR A 365 SER A 369 1 O ILE A 367 N ILE A 321
SHEET 8 AA2 9 ILE A 390 THR A 392 1 O ILE A 390 N ILE A 368
SHEET 9 AA2 9 ILE A 161 ILE A 165 1 N GLY A 163 O MET A 391
SHEET 1 AA3 2 ALA A 348 ASP A 350 0
SHEET 2 AA3 2 HIS A 355 GLU A 357 -1 O GLN A 356 N ALA A 349
SHEET 1 AA4 5 LEU B 71 ASP B 76 0
SHEET 2 AA4 5 LEU B 81 PRO B 87 -1 O ALA B 85 N LEU B 71
SHEET 3 AA4 5 HIS B 23 PRO B 32 -1 N VAL B 24 O TYR B 86
SHEET 4 AA4 5 VAL B 119 TYR B 128 -1 O TYR B 125 N ALA B 27
SHEET 5 AA4 5 GLY B 303 TYR B 304 1 O GLY B 303 N MET B 124
SHEET 1 AA5 9 ILE B 161 ILE B 165 0
SHEET 2 AA5 9 PHE B 190 KCX B 192 1 O PHE B 190 N VAL B 162
SHEET 3 AA5 9 LEU B 228 ASN B 232 1 O SER B 230 N ILE B 191
SHEET 4 AA5 9 ILE B 259 ASP B 264 1 O LEU B 262 N PHE B 231
SHEET 5 AA5 9 TYR B 284 HIS B 288 1 O HIS B 286 N PHE B 261
SHEET 6 AA5 9 GLY B 320 HIS B 322 1 O GLY B 320 N TYR B 287
SHEET 7 AA5 9 THR B 365 SER B 369 1 O ILE B 367 N ILE B 321
SHEET 8 AA5 9 ILE B 390 THR B 392 1 O ILE B 390 N ILE B 368
SHEET 9 AA5 9 ILE B 161 ILE B 165 1 N GLY B 163 O MET B 391
SHEET 1 AA6 2 ALA B 348 ASP B 350 0
SHEET 2 AA6 2 HIS B 355 GLU B 357 -1 O GLN B 356 N ALA B 349
SHEET 1 AA7 5 LEU C 71 ASP C 76 0
SHEET 2 AA7 5 LEU C 81 PRO C 87 -1 O ALA C 85 N LEU C 71
SHEET 3 AA7 5 HIS C 23 PRO C 32 -1 N VAL C 24 O TYR C 86
SHEET 4 AA7 5 VAL C 119 TYR C 128 -1 O TYR C 125 N ALA C 27
SHEET 5 AA7 5 GLY C 303 TYR C 304 1 O GLY C 303 N MET C 124
SHEET 1 AA8 9 ILE C 161 ILE C 165 0
SHEET 2 AA8 9 PHE C 190 KCX C 192 1 O PHE C 190 N VAL C 162
SHEET 3 AA8 9 LEU C 228 ASN C 232 1 O SER C 230 N ILE C 191
SHEET 4 AA8 9 ILE C 259 ASP C 264 1 O LEU C 262 N PHE C 231
SHEET 5 AA8 9 TYR C 284 HIS C 288 1 O HIS C 286 N PHE C 261
SHEET 6 AA8 9 GLY C 320 HIS C 322 1 O GLY C 320 N TYR C 287
SHEET 7 AA8 9 THR C 365 SER C 369 1 O ILE C 367 N ILE C 321
SHEET 8 AA8 9 ILE C 390 THR C 392 1 O ILE C 390 N ILE C 368
SHEET 9 AA8 9 ILE C 161 ILE C 165 1 N GLY C 163 O MET C 391
SHEET 1 AA9 2 ALA C 348 ASP C 350 0
SHEET 2 AA9 2 HIS C 355 GLU C 357 -1 O GLN C 356 N ALA C 349
SHEET 1 AB1 5 LEU D 71 ASP D 76 0
SHEET 2 AB1 5 LEU D 81 PRO D 87 -1 O ALA D 85 N LEU D 71
SHEET 3 AB1 5 HIS D 23 PRO D 32 -1 N VAL D 24 O TYR D 86
SHEET 4 AB1 5 VAL D 119 TYR D 128 -1 O TYR D 125 N ALA D 27
SHEET 5 AB1 5 GLY D 303 TYR D 304 1 O GLY D 303 N MET D 124
SHEET 1 AB2 9 ILE D 161 ILE D 165 0
SHEET 2 AB2 9 PHE D 190 KCX D 192 1 O PHE D 190 N VAL D 162
SHEET 3 AB2 9 LEU D 228 ASN D 232 1 O SER D 230 N ILE D 191
SHEET 4 AB2 9 ILE D 259 ASP D 264 1 O LEU D 262 N PHE D 231
SHEET 5 AB2 9 TYR D 284 HIS D 288 1 O HIS D 286 N PHE D 261
SHEET 6 AB2 9 GLY D 320 HIS D 322 1 O GLY D 320 N TYR D 287
SHEET 7 AB2 9 THR D 365 SER D 369 1 O ILE D 367 N ILE D 321
SHEET 8 AB2 9 ILE D 390 THR D 392 1 O ILE D 390 N ILE D 368
SHEET 9 AB2 9 ILE D 161 ILE D 165 1 N GLY D 163 O MET D 391
SHEET 1 AB3 2 ALA D 348 ASP D 350 0
SHEET 2 AB3 2 HIS D 355 GLU D 357 -1 O GLN D 356 N ALA D 349
SHEET 1 AB4 5 LEU E 71 ASP E 76 0
SHEET 2 AB4 5 LEU E 81 PRO E 87 -1 O ALA E 85 N LEU E 71
SHEET 3 AB4 5 HIS E 23 PRO E 32 -1 N VAL E 24 O TYR E 86
SHEET 4 AB4 5 VAL E 119 TYR E 128 -1 O TYR E 125 N ALA E 27
SHEET 5 AB4 5 GLY E 303 TYR E 304 1 O GLY E 303 N MET E 124
SHEET 1 AB5 9 ILE E 161 ILE E 165 0
SHEET 2 AB5 9 PHE E 190 KCX E 192 1 O PHE E 190 N VAL E 162
SHEET 3 AB5 9 LEU E 228 ASN E 232 1 O SER E 230 N ILE E 191
SHEET 4 AB5 9 ILE E 259 ASP E 264 1 O LEU E 262 N PHE E 231
SHEET 5 AB5 9 TYR E 284 HIS E 288 1 O HIS E 286 N PHE E 261
SHEET 6 AB5 9 GLY E 320 HIS E 322 1 O GLY E 320 N TYR E 287
SHEET 7 AB5 9 THR E 365 SER E 369 1 O ILE E 367 N ILE E 321
SHEET 8 AB5 9 ILE E 390 THR E 392 1 O ILE E 390 N ILE E 368
SHEET 9 AB5 9 ILE E 161 ILE E 165 1 N GLY E 163 O MET E 391
SHEET 1 AB6 2 ALA E 348 ASP E 350 0
SHEET 2 AB6 2 HIS E 355 GLU E 357 -1 O GLN E 356 N ALA E 349
SHEET 1 AB7 5 LEU F 71 ASP F 76 0
SHEET 2 AB7 5 LEU F 81 PRO F 87 -1 O ALA F 85 N LEU F 71
SHEET 3 AB7 5 HIS F 23 PRO F 32 -1 N VAL F 24 O TYR F 86
SHEET 4 AB7 5 VAL F 119 TYR F 128 -1 O TYR F 125 N ALA F 27
SHEET 5 AB7 5 GLY F 303 TYR F 304 1 O GLY F 303 N MET F 124
SHEET 1 AB8 9 ILE F 161 ILE F 165 0
SHEET 2 AB8 9 PHE F 190 KCX F 192 1 O PHE F 190 N VAL F 162
SHEET 3 AB8 9 LEU F 228 ASN F 232 1 O SER F 230 N ILE F 191
SHEET 4 AB8 9 ILE F 259 ASP F 264 1 O LEU F 262 N PHE F 231
SHEET 5 AB8 9 TYR F 284 HIS F 288 1 O HIS F 286 N PHE F 261
SHEET 6 AB8 9 GLY F 320 HIS F 322 1 O GLY F 320 N TYR F 287
SHEET 7 AB8 9 THR F 365 SER F 369 1 O ILE F 367 N ILE F 321
SHEET 8 AB8 9 ILE F 390 THR F 392 1 O ILE F 390 N ILE F 368
SHEET 9 AB8 9 ILE F 161 ILE F 165 1 N GLY F 163 O MET F 391
SHEET 1 AB9 2 ALA F 348 ASP F 350 0
SHEET 2 AB9 2 HIS F 355 GLU F 357 -1 O GLN F 356 N ALA F 349
LINK C ILE A 191 N KCX A 192 1555 1555 1.33
LINK C KCX A 192 N ASN A 193 1555 1555 1.33
LINK C ILE B 191 N KCX B 192 1555 1555 1.33
LINK C KCX B 192 N ASN B 193 1555 1555 1.33
LINK C ILE C 191 N KCX C 192 1555 1555 1.33
LINK C KCX C 192 N ASN C 193 1555 1555 1.33
LINK C ILE D 191 N KCX D 192 1555 1555 1.33
LINK C KCX D 192 N ASN D 193 1555 1555 1.33
LINK C ILE E 191 N KCX E 192 1555 1555 1.33
LINK C KCX E 192 N ASN E 193 1555 1555 1.33
LINK C ILE F 191 N KCX F 192 1555 1555 1.33
LINK C KCX F 192 N ASN F 193 1555 1555 1.33
LINK OQ2 KCX A 192 MG MG A 501 1555 1555 1.98
LINK OD1 ASP A 194 MG MG A 501 1555 1555 2.09
LINK OE1 GLU A 195 MG MG A 501 1555 1555 2.06
LINK O2 CAP A 500 MG MG A 501 1555 1555 2.16
LINK O3 CAP A 500 MG MG A 501 1555 1555 2.21
LINK O6 CAP A 500 MG MG A 501 1555 1555 2.04
LINK OQ2 KCX B 192 MG MG B 501 1555 1555 2.06
LINK OD1 ASP B 194 MG MG B 501 1555 1555 2.07
LINK OE1 GLU B 195 MG MG B 501 1555 1555 1.99
LINK O2 CAP B 500 MG MG B 501 1555 1555 2.18
LINK O3 CAP B 500 MG MG B 501 1555 1555 2.12
LINK O6 CAP B 500 MG MG B 501 1555 1555 2.15
LINK OQ2 KCX C 192 MG MG C 501 1555 1555 2.05
LINK OD1 ASP C 194 MG MG C 501 1555 1555 2.09
LINK OE1 GLU C 195 MG MG C 501 1555 1555 2.01
LINK O2 CAP C 500 MG MG C 501 1555 1555 2.20
LINK O3 CAP C 500 MG MG C 501 1555 1555 2.13
LINK O6 CAP C 500 MG MG C 501 1555 1555 2.21
LINK OQ2 KCX D 192 MG MG D 501 1555 1555 2.08
LINK OD1 ASP D 194 MG MG D 501 1555 1555 2.08
LINK OE1 GLU D 195 MG MG D 501 1555 1555 2.04
LINK O2 CAP D 500 MG MG D 501 1555 1555 2.15
LINK O3 CAP D 500 MG MG D 501 1555 1555 2.21
LINK O6 CAP D 500 MG MG D 501 1555 1555 2.13
LINK OQ2 KCX E 192 MG MG E 501 1555 1555 2.02
LINK OD1 ASP E 194 MG MG E 501 1555 1555 2.08
LINK OE1 GLU E 195 MG MG E 501 1555 1555 2.01
LINK O2 CAP E 500 MG MG E 501 1555 1555 2.19
LINK O3 CAP E 500 MG MG E 501 1555 1555 2.14
LINK O6 CAP E 500 MG MG E 501 1555 1555 2.12
LINK OQ2 KCX F 192 MG MG F 501 1555 1555 1.94
LINK OD1 ASP F 194 MG MG F 501 1555 1555 2.08
LINK OE1 GLU F 195 MG MG F 501 1555 1555 2.00
LINK O2 CAP F 500 MG MG F 501 1555 1555 2.27
LINK O3 CAP F 500 MG MG F 501 1555 1555 2.20
LINK O6 CAP F 500 MG MG F 501 1555 1555 2.26
CISPEP 1 LYS A 167 PRO A 168 0 -0.35
CISPEP 2 LYS B 167 PRO B 168 0 -0.21
CISPEP 3 LYS C 167 PRO C 168 0 0.26
CISPEP 4 LYS D 167 PRO D 168 0 -0.09
CISPEP 5 LYS E 167 PRO E 168 0 -0.54
CISPEP 6 LYS F 167 PRO F 168 0 -0.41
SITE 1 AC1 27 ILE A 165 LYS A 167 LYS A 169 KCX A 192
SITE 2 AC1 27 ASP A 194 GLU A 195 HIS A 288 ARG A 289
SITE 3 AC1 27 HIS A 322 LYS A 330 MET A 331 SER A 369
SITE 4 AC1 27 GLY A 370 GLY A 371 GLY A 394 GLY A 395
SITE 5 AC1 27 MG A 501 HOH A 637 HOH A 657 HOH A 658
SITE 6 AC1 27 HOH A 663 HOH A 666 HOH A 696 HOH A 701
SITE 7 AC1 27 GLU B 49 THR B 54 ASN B 112
SITE 1 AC2 5 KCX A 192 ASP A 194 GLU A 195 CAP A 500
SITE 2 AC2 5 ASN B 112
SITE 1 AC3 28 GLU A 49 THR A 54 ASN A 112 HOH A 719
SITE 2 AC3 28 ILE B 165 LYS B 167 LYS B 169 KCX B 192
SITE 3 AC3 28 ASP B 194 GLU B 195 HIS B 288 ARG B 289
SITE 4 AC3 28 HIS B 322 LYS B 330 MET B 331 SER B 369
SITE 5 AC3 28 GLY B 370 GLY B 371 GLY B 394 GLY B 395
SITE 6 AC3 28 MG B 501 HOH B 635 HOH B 673 HOH B 679
SITE 7 AC3 28 HOH B 724 HOH B 727 HOH B 742 HOH B 743
SITE 1 AC4 6 ASN A 112 LYS B 169 KCX B 192 ASP B 194
SITE 2 AC4 6 GLU B 195 CAP B 500
SITE 1 AC5 28 ILE C 165 LYS C 167 LYS C 169 KCX C 192
SITE 2 AC5 28 ASP C 194 GLU C 195 HIS C 288 ARG C 289
SITE 3 AC5 28 HIS C 322 LYS C 330 SER C 369 GLY C 370
SITE 4 AC5 28 GLY C 371 ALA C 393 GLY C 394 GLY C 395
SITE 5 AC5 28 MG C 501 HOH C 620 HOH C 678 HOH C 682
SITE 6 AC5 28 HOH C 690 HOH C 700 HOH C 708 HOH C 716
SITE 7 AC5 28 GLU D 49 THR D 54 ASN D 112 HOH D 747
SITE 1 AC6 6 LYS C 169 KCX C 192 ASP C 194 GLU C 195
SITE 2 AC6 6 CAP C 500 ASN D 112
SITE 1 AC7 27 GLU C 49 THR C 54 ASN C 112 ILE D 165
SITE 2 AC7 27 LYS D 167 LYS D 169 KCX D 192 ASP D 194
SITE 3 AC7 27 GLU D 195 HIS D 288 ARG D 289 HIS D 322
SITE 4 AC7 27 LYS D 330 MET D 331 SER D 369 GLY D 370
SITE 5 AC7 27 GLY D 371 GLY D 394 GLY D 395 MG D 501
SITE 6 AC7 27 HOH D 630 HOH D 655 HOH D 668 HOH D 690
SITE 7 AC7 27 HOH D 708 HOH D 713 HOH D 724
SITE 1 AC8 5 ASN C 112 KCX D 192 ASP D 194 GLU D 195
SITE 2 AC8 5 CAP D 500
SITE 1 AC9 29 ILE E 165 LYS E 167 LYS E 169 KCX E 192
SITE 2 AC9 29 ASP E 194 GLU E 195 HIS E 288 ARG E 289
SITE 3 AC9 29 HIS E 322 LYS E 330 MET E 331 SER E 369
SITE 4 AC9 29 GLY E 370 GLY E 371 GLY E 394 GLY E 395
SITE 5 AC9 29 MG E 501 HOH E 634 HOH E 650 HOH E 656
SITE 6 AC9 29 HOH E 661 HOH E 686 HOH E 712 HOH E 728
SITE 7 AC9 29 GLU F 49 THR F 54 ASN F 112 HOH F 663
SITE 8 AC9 29 HOH F 712
SITE 1 AD1 6 LYS E 169 KCX E 192 ASP E 194 GLU E 195
SITE 2 AD1 6 CAP E 500 ASN F 112
SITE 1 AD2 29 GLU E 49 THR E 54 ASN E 112 HOH E 619
SITE 2 AD2 29 HOH E 716 ILE F 165 LYS F 167 LYS F 169
SITE 3 AD2 29 KCX F 192 ASP F 194 GLU F 195 HIS F 288
SITE 4 AD2 29 ARG F 289 HIS F 322 LYS F 330 MET F 331
SITE 5 AD2 29 SER F 369 GLY F 370 GLY F 371 GLY F 394
SITE 6 AD2 29 GLY F 395 MG F 501 HOH F 626 HOH F 630
SITE 7 AD2 29 HOH F 632 HOH F 649 HOH F 660 HOH F 729
SITE 8 AD2 29 HOH F 762
SITE 1 AD3 6 ASN E 112 LYS F 169 KCX F 192 ASP F 194
SITE 2 AD3 6 GLU F 195 CAP F 500
CRYST1 75.960 100.250 100.380 113.06 108.07 88.89 P 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 0.013165 -0.000255 0.004585 0.00000
SCALE2 0.000000 0.009977 0.004430 0.00000
SCALE3 0.000000 0.000000 0.011465 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
