HEADER ISOMERASE 06-APR-13 4K1W
TITLE CRYSTAL STRUCTURE OF THE A314P MUTANT OF MANNONATE DEHYDRATASE FROM
TITLE 2 NOVOSPHINGOBIUM AROMATICIVORANS COMPLEXED WITH MG AND D-MANNONATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MANDELATE RACEMASE/MUCONATE LACTONIZING ENZYME, N-TERMINAL
COMPND 3 DOMAIN PROTEIN;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOVOSPHINGOBIUM AROMATICIVORANS;
SOURCE 3 ORGANISM_TAXID: 279238;
SOURCE 4 STRAIN: DSM 12444;
SOURCE 5 GENE: SARO_3675;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENOLASE FOLD, MANNONATE DEHYDRATASE, D-MANNONATE, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.FEDOROV,E.V.FEDOROV,D.WICHELECKI,J.A.GERLT,S.C.ALMO
REVDAT 2 20-SEP-23 4K1W 1 REMARK SEQADV LINK
REVDAT 1 09-APR-14 4K1W 0
SPRSDE 09-APR-14 4K1W 3R4E
JRNL AUTH A.A.FEDOROV,E.V.FEDOROV,D.WICHELECKI,J.A.GERLT,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF THE A314P MUTANT OF MANNONATE
JRNL TITL 2 DEHYDRATASE FROM NOVOSPHINGOBIUM AROMATICIVORANS COMPLEXED
JRNL TITL 3 WITH MG AND D-MANNONATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.21
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 191348
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 9615
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 46.2320 - 5.1114 1.00 6407 344 0.1602 0.1742
REMARK 3 2 5.1114 - 4.0578 1.00 6245 323 0.1280 0.1480
REMARK 3 3 4.0578 - 3.5451 1.00 6201 335 0.1341 0.1423
REMARK 3 4 3.5451 - 3.2211 1.00 6181 322 0.1479 0.1657
REMARK 3 5 3.2211 - 2.9902 1.00 6179 314 0.1597 0.1849
REMARK 3 6 2.9902 - 2.8140 1.00 6142 325 0.1617 0.1892
REMARK 3 7 2.8140 - 2.6731 1.00 6126 332 0.1502 0.1800
REMARK 3 8 2.6731 - 2.5567 1.00 6125 336 0.1513 0.1868
REMARK 3 9 2.5567 - 2.4583 1.00 6084 340 0.1467 0.1814
REMARK 3 10 2.4583 - 2.3735 1.00 6122 338 0.1500 0.1768
REMARK 3 11 2.3735 - 2.2993 1.00 6053 325 0.1531 0.1918
REMARK 3 12 2.2993 - 2.2335 1.00 6141 309 0.1530 0.1832
REMARK 3 13 2.2335 - 2.1747 1.00 6097 326 0.1474 0.1842
REMARK 3 14 2.1747 - 2.1217 0.99 6029 323 0.1527 0.1924
REMARK 3 15 2.1217 - 2.0734 0.99 6073 320 0.1599 0.1929
REMARK 3 16 2.0734 - 2.0293 0.99 6096 300 0.1580 0.2091
REMARK 3 17 2.0293 - 1.9887 0.99 6020 342 0.1646 0.1983
REMARK 3 18 1.9887 - 1.9512 0.99 6033 348 0.1724 0.2288
REMARK 3 19 1.9512 - 1.9164 0.99 6048 307 0.1727 0.2164
REMARK 3 20 1.9164 - 1.8839 0.99 6033 320 0.1750 0.2264
REMARK 3 21 1.8839 - 1.8535 0.99 6061 297 0.1702 0.1861
REMARK 3 22 1.8535 - 1.8250 0.99 6053 283 0.1787 0.2328
REMARK 3 23 1.8250 - 1.7981 0.99 5997 321 0.1970 0.2206
REMARK 3 24 1.7981 - 1.7728 0.99 5985 321 0.2061 0.2335
REMARK 3 25 1.7728 - 1.7488 0.99 6026 312 0.2180 0.2566
REMARK 3 26 1.7488 - 1.7261 0.99 5952 373 0.2240 0.2506
REMARK 3 27 1.7261 - 1.7045 0.99 6003 300 0.2342 0.2667
REMARK 3 28 1.7045 - 1.6840 0.98 5962 290 0.2523 0.2929
REMARK 3 29 1.6840 - 1.6644 0.98 5980 327 0.2615 0.3072
REMARK 3 30 1.6644 - 1.6457 0.87 5279 262 0.2666 0.2821
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.430
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.006 12905
REMARK 3 ANGLE : 1.070 17555
REMARK 3 CHIRALITY : 0.074 1885
REMARK 3 PLANARITY : 0.006 2264
REMARK 3 DIHEDRAL : 12.930 4750
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9604 30.8785 -11.7862
REMARK 3 T TENSOR
REMARK 3 T11: 0.2261 T22: 0.2460
REMARK 3 T33: 0.1037 T12: -0.0117
REMARK 3 T13: 0.0314 T23: -0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 0.9931 L22: 0.6273
REMARK 3 L33: 0.5672 L12: -0.0035
REMARK 3 L13: 0.2608 L23: -0.1556
REMARK 3 S TENSOR
REMARK 3 S11: -0.0030 S12: -0.2746 S13: -0.0793
REMARK 3 S21: 0.2119 S22: -0.0291 S23: 0.0195
REMARK 3 S31: 0.0597 S32: -0.0534 S33: 0.0334
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0213 16.4480 -29.6524
REMARK 3 T TENSOR
REMARK 3 T11: 0.1453 T22: 0.1522
REMARK 3 T33: 0.1493 T12: 0.0228
REMARK 3 T13: -0.0182 T23: 0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 0.6758 L22: 0.9254
REMARK 3 L33: 0.3994 L12: 0.0803
REMARK 3 L13: -0.0391 L23: -0.0808
REMARK 3 S TENSOR
REMARK 3 S11: 0.0064 S12: -0.1263 S13: -0.1260
REMARK 3 S21: 0.1349 S22: -0.0524 S23: -0.1491
REMARK 3 S31: 0.0526 S32: 0.0574 S33: 0.0420
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3217 72.8226 -26.2650
REMARK 3 T TENSOR
REMARK 3 T11: 0.2289 T22: 0.1672
REMARK 3 T33: 0.3851 T12: 0.0504
REMARK 3 T13: -0.0898 T23: -0.1295
REMARK 3 L TENSOR
REMARK 3 L11: 0.9023 L22: 0.8307
REMARK 3 L33: 0.5286 L12: 0.0374
REMARK 3 L13: 0.0192 L23: -0.0242
REMARK 3 S TENSOR
REMARK 3 S11: -0.0895 S12: -0.2290 S13: 0.4464
REMARK 3 S21: 0.1859 S22: 0.0062 S23: 0.0235
REMARK 3 S31: -0.1478 S32: -0.0646 S33: 0.0594
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8130 58.5405 -15.5994
REMARK 3 T TENSOR
REMARK 3 T11: 0.2335 T22: 0.2564
REMARK 3 T33: 0.2642 T12: -0.0263
REMARK 3 T13: -0.1272 T23: -0.0612
REMARK 3 L TENSOR
REMARK 3 L11: 0.7070 L22: 0.6397
REMARK 3 L33: 0.8311 L12: 0.0607
REMARK 3 L13: -0.0222 L23: -0.0543
REMARK 3 S TENSOR
REMARK 3 S11: -0.0368 S12: -0.2228 S13: 0.2944
REMARK 3 S21: 0.1794 S22: -0.0822 S23: -0.1381
REMARK 3 S31: -0.1820 S32: 0.0846 S33: 0.0734
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 4K1W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078786.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 191348
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.646
REMARK 200 RESOLUTION RANGE LOW (A) : 46.214
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
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 : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: 2QJJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG400, 0.1M HEPES, 0.2M SODIUM
REMARK 280 CHLORIDE, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.59850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.59850
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 58.11150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 82.68150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 58.11150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 82.68150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 83.59850
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 58.11150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 82.68150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 83.59850
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 58.11150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 82.68150
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 651 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 860 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 659 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 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 ASP A 157
REMARK 465 ALA A 158
REMARK 465 TYR A 159
REMARK 465 GLY A 160
REMARK 465 VAL A 161
REMARK 465 GLY A 162
REMARK 465 ARG A 163
REMARK 465 GLY A 164
REMARK 465 LYS A 165
REMARK 465 LEU A 166
REMARK 465 TYR A 167
REMARK 465 TYR A 168
REMARK 465 GLU A 169
REMARK 465 PRO A 170
REMARK 465 ALA A 171
REMARK 465 ASP A 172
REMARK 465 ALA A 173
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 ASP B 157
REMARK 465 ALA B 158
REMARK 465 TYR B 159
REMARK 465 GLY B 160
REMARK 465 VAL B 161
REMARK 465 GLY B 162
REMARK 465 ARG B 163
REMARK 465 GLY B 164
REMARK 465 LYS B 165
REMARK 465 LEU B 166
REMARK 465 TYR B 167
REMARK 465 TYR B 168
REMARK 465 GLU B 169
REMARK 465 PRO B 170
REMARK 465 ALA B 171
REMARK 465 ASP B 172
REMARK 465 ALA B 173
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 LYS C 156
REMARK 465 ASP C 157
REMARK 465 ALA C 158
REMARK 465 TYR C 159
REMARK 465 GLY C 160
REMARK 465 VAL C 161
REMARK 465 GLY C 162
REMARK 465 ARG C 163
REMARK 465 GLY C 164
REMARK 465 LYS C 165
REMARK 465 LEU C 166
REMARK 465 TYR C 167
REMARK 465 TYR C 168
REMARK 465 GLU C 169
REMARK 465 PRO C 170
REMARK 465 ALA C 171
REMARK 465 ASP C 172
REMARK 465 ALA C 173
REMARK 465 SER C 174
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 LYS D 156
REMARK 465 ASP D 157
REMARK 465 ALA D 158
REMARK 465 TYR D 159
REMARK 465 GLY D 160
REMARK 465 VAL D 161
REMARK 465 GLY D 162
REMARK 465 ARG D 163
REMARK 465 GLY D 164
REMARK 465 LYS D 165
REMARK 465 LEU D 166
REMARK 465 TYR D 167
REMARK 465 TYR D 168
REMARK 465 GLU D 169
REMARK 465 PRO D 170
REMARK 465 ALA D 171
REMARK 465 ASP D 172
REMARK 465 ALA D 173
REMARK 465 SER D 174
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 ARG A 39 32.82 -140.47
REMARK 500 HIS A 50 -59.33 -122.51
REMARK 500 TYR A 75 -55.86 74.13
REMARK 500 ARG A 78 -175.47 70.93
REMARK 500 ASP A 115 -85.30 -89.59
REMARK 500 ASN A 334 40.61 -94.32
REMARK 500 ASP A 354 63.69 -106.52
REMARK 500 ARG B 39 30.51 -140.68
REMARK 500 HIS B 50 -62.47 -130.18
REMARK 500 TYR B 75 -53.11 74.01
REMARK 500 ARG B 78 -176.60 67.70
REMARK 500 ASP B 115 -86.80 -89.50
REMARK 500 ASN B 334 43.49 -92.00
REMARK 500 PHE B 351 76.13 -118.64
REMARK 500 ASP B 354 62.92 -106.18
REMARK 500 ASP B 354 64.91 -107.67
REMARK 500 TRP B 400 -168.76 -124.86
REMARK 500 HIS C 50 -60.61 -129.20
REMARK 500 TYR C 75 -52.92 68.81
REMARK 500 ARG C 78 -177.53 68.75
REMARK 500 ASP C 115 -86.31 -87.52
REMARK 500 ASN C 334 41.77 -88.76
REMARK 500 PHE C 351 75.15 -119.62
REMARK 500 ASP C 354 72.09 -105.73
REMARK 500 ARG D 39 32.73 -141.47
REMARK 500 HIS D 50 -61.03 -128.22
REMARK 500 TYR D 75 -52.51 72.68
REMARK 500 ARG D 78 -176.53 71.63
REMARK 500 ASP D 115 -83.33 -88.07
REMARK 500 ASP D 115 -86.95 -84.67
REMARK 500 ASN D 334 44.18 -92.51
REMARK 500 PHE D 351 74.08 -118.91
REMARK 500 TRP D 400 -167.69 -126.06
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 ASP A 210 OD2
REMARK 620 2 GLU A 236 OE1 87.2
REMARK 620 3 GLU A 262 OE1 168.0 83.6
REMARK 620 4 CS2 A 502 O2 97.7 165.9 93.0
REMARK 620 5 CS2 A 502 O1B 92.6 88.6 94.9 78.1
REMARK 620 6 HOH A 848 O 86.8 95.9 86.4 97.5 175.4
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 ASP B 210 OD2
REMARK 620 2 GLU B 236 OE1 88.4
REMARK 620 3 GLU B 262 OE1 169.4 85.0
REMARK 620 4 CS2 B 502 O1B 92.4 88.5 95.6
REMARK 620 5 CS2 B 502 O2 97.6 165.5 90.8 78.1
REMARK 620 6 HOH B 856 O 84.9 99.9 88.2 171.1 93.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 504 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 874 O
REMARK 620 2 HOH B 882 O 155.4
REMARK 620 3 HOH B 883 O 89.3 87.7
REMARK 620 4 HOH D 812 O 84.0 87.1 151.6
REMARK 620 N 1 2 3
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 ASP C 210 OD2
REMARK 620 2 GLU C 236 OE1 85.9
REMARK 620 3 GLU C 262 OE1 170.6 85.5
REMARK 620 4 CS2 C 502 O2 97.4 163.2 91.9
REMARK 620 5 CS2 C 502 O1B 89.9 87.1 93.4 76.4
REMARK 620 6 HOH C 812 O 87.7 104.7 90.8 92.0 167.8
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 ASP D 210 OD2
REMARK 620 2 GLU D 236 OE1 88.5
REMARK 620 3 GLU D 262 OE1 171.4 84.8
REMARK 620 4 CS2 D 502 O2 97.0 164.9 90.8
REMARK 620 5 CS2 D 502 O1B 91.5 89.6 93.8 76.2
REMARK 620 6 HOH D 801 O 87.1 101.9 89.0 92.5 168.4
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 MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS2 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO2 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO2 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDO A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS2 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDO B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS2 C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO2 C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO2 C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDO C 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS2 D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO2 D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDO D 505
DBREF 4K1W A 1 402 UNP A4XF23 A4XF23_NOVAD 1 402
DBREF 4K1W B 1 402 UNP A4XF23 A4XF23_NOVAD 1 402
DBREF 4K1W C 1 402 UNP A4XF23 A4XF23_NOVAD 1 402
DBREF 4K1W D 1 402 UNP A4XF23 A4XF23_NOVAD 1 402
SEQADV 4K1W HIS A -15 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS A -14 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS A -13 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS A -12 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS A -11 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS A -10 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W SER A -9 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W SER A -8 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W GLY A -7 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W LEU A -6 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W VAL A -5 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W PRO A -4 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W ARG A -3 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W GLY A -2 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W SER A -1 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS A 0 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W PRO A 314 UNP A4XF23 ALA 314 ENGINEERED MUTATION
SEQADV 4K1W HIS B -15 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS B -14 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS B -13 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS B -12 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS B -11 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS B -10 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W SER B -9 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W SER B -8 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W GLY B -7 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W LEU B -6 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W VAL B -5 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W PRO B -4 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W ARG B -3 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W GLY B -2 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W SER B -1 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS B 0 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W PRO B 314 UNP A4XF23 ALA 314 ENGINEERED MUTATION
SEQADV 4K1W HIS C -15 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS C -14 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS C -13 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS C -12 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS C -11 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS C -10 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W SER C -9 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W SER C -8 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W GLY C -7 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W LEU C -6 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W VAL C -5 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W PRO C -4 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W ARG C -3 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W GLY C -2 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W SER C -1 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS C 0 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W PRO C 314 UNP A4XF23 ALA 314 ENGINEERED MUTATION
SEQADV 4K1W HIS D -15 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS D -14 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS D -13 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS D -12 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS D -11 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS D -10 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W SER D -9 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W SER D -8 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W GLY D -7 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W LEU D -6 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W VAL D -5 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W PRO D -4 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W ARG D -3 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W GLY D -2 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W SER D -1 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W HIS D 0 UNP A4XF23 EXPRESSION TAG
SEQADV 4K1W PRO D 314 UNP A4XF23 ALA 314 ENGINEERED MUTATION
SEQRES 1 A 418 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG
SEQRES 2 A 418 GLY SER HIS MET LYS ILE THR ALA ALA ARG VAL ILE ILE
SEQRES 3 A 418 THR CYS PRO GLY ARG ASN PHE VAL THR LEU LYS ILE GLU
SEQRES 4 A 418 THR ASP GLN GLY VAL TYR GLY ILE GLY ASP ALA THR LEU
SEQRES 5 A 418 ASN GLY ARG GLU LEU SER VAL VAL ALA TYR LEU GLN GLU
SEQRES 6 A 418 HIS VAL ALA PRO CYS LEU ILE GLY MET ASP PRO ARG ARG
SEQRES 7 A 418 ILE GLU ASP ILE TRP GLN TYR VAL TYR ARG GLY ALA TYR
SEQRES 8 A 418 TRP ARG ARG GLY PRO VAL THR MET ARG ALA ILE ALA ALA
SEQRES 9 A 418 VAL ASP MET ALA LEU TRP ASP ILE LYS ALA LYS MET ALA
SEQRES 10 A 418 GLY MET PRO LEU TYR GLN LEU LEU GLY GLY ARG SER ARG
SEQRES 11 A 418 ASP GLY ILE MET VAL TYR GLY HIS ALA ASN GLY SER ASP
SEQRES 12 A 418 ILE ALA GLU THR VAL GLU ALA VAL GLY HIS TYR ILE ASP
SEQRES 13 A 418 MET GLY TYR LYS ALA ILE ARG ALA GLN THR GLY VAL PRO
SEQRES 14 A 418 GLY ILE LYS ASP ALA TYR GLY VAL GLY ARG GLY LYS LEU
SEQRES 15 A 418 TYR TYR GLU PRO ALA ASP ALA SER LEU PRO SER VAL THR
SEQRES 16 A 418 GLY TRP ASP THR ARG LYS ALA LEU ASN TYR VAL PRO LYS
SEQRES 17 A 418 LEU PHE GLU GLU LEU ARG LYS THR TYR GLY PHE ASP HIS
SEQRES 18 A 418 HIS LEU LEU HIS ASP GLY HIS HIS ARG TYR THR PRO GLN
SEQRES 19 A 418 GLU ALA ALA ASN LEU GLY LYS MET LEU GLU PRO TYR GLN
SEQRES 20 A 418 LEU PHE TRP LEU GLU ASP CYS THR PRO ALA GLU ASN GLN
SEQRES 21 A 418 GLU ALA PHE ARG LEU VAL ARG GLN HIS THR VAL THR PRO
SEQRES 22 A 418 LEU ALA VAL GLY GLU ILE PHE ASN THR ILE TRP ASP ALA
SEQRES 23 A 418 LYS ASP LEU ILE GLN ASN GLN LEU ILE ASP TYR ILE ARG
SEQRES 24 A 418 ALA THR VAL VAL GLY ALA GLY GLY LEU THR HIS LEU ARG
SEQRES 25 A 418 ARG ILE ALA ASP LEU ALA SER LEU TYR GLN VAL ARG THR
SEQRES 26 A 418 GLY CYS HIS GLY PRO THR ASP LEU SER PRO VAL THR MET
SEQRES 27 A 418 GLY CYS ALA LEU HIS PHE ASP THR TRP VAL PRO ASN PHE
SEQRES 28 A 418 GLY ILE GLN GLU TYR MET ARG HIS THR GLU GLU THR ASP
SEQRES 29 A 418 ALA VAL PHE PRO HIS ASP TYR TRP PHE GLU LYS GLY GLU
SEQRES 30 A 418 LEU PHE VAL GLY GLU THR PRO GLY HIS GLY VAL ASP ILE
SEQRES 31 A 418 ASP GLU GLU LEU ALA ALA LYS TYR PRO TYR LYS PRO ALA
SEQRES 32 A 418 TYR LEU PRO VAL ALA ARG LEU GLU ASP GLY THR MET TRP
SEQRES 33 A 418 ASN TRP
SEQRES 1 B 418 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG
SEQRES 2 B 418 GLY SER HIS MET LYS ILE THR ALA ALA ARG VAL ILE ILE
SEQRES 3 B 418 THR CYS PRO GLY ARG ASN PHE VAL THR LEU LYS ILE GLU
SEQRES 4 B 418 THR ASP GLN GLY VAL TYR GLY ILE GLY ASP ALA THR LEU
SEQRES 5 B 418 ASN GLY ARG GLU LEU SER VAL VAL ALA TYR LEU GLN GLU
SEQRES 6 B 418 HIS VAL ALA PRO CYS LEU ILE GLY MET ASP PRO ARG ARG
SEQRES 7 B 418 ILE GLU ASP ILE TRP GLN TYR VAL TYR ARG GLY ALA TYR
SEQRES 8 B 418 TRP ARG ARG GLY PRO VAL THR MET ARG ALA ILE ALA ALA
SEQRES 9 B 418 VAL ASP MET ALA LEU TRP ASP ILE LYS ALA LYS MET ALA
SEQRES 10 B 418 GLY MET PRO LEU TYR GLN LEU LEU GLY GLY ARG SER ARG
SEQRES 11 B 418 ASP GLY ILE MET VAL TYR GLY HIS ALA ASN GLY SER ASP
SEQRES 12 B 418 ILE ALA GLU THR VAL GLU ALA VAL GLY HIS TYR ILE ASP
SEQRES 13 B 418 MET GLY TYR LYS ALA ILE ARG ALA GLN THR GLY VAL PRO
SEQRES 14 B 418 GLY ILE LYS ASP ALA TYR GLY VAL GLY ARG GLY LYS LEU
SEQRES 15 B 418 TYR TYR GLU PRO ALA ASP ALA SER LEU PRO SER VAL THR
SEQRES 16 B 418 GLY TRP ASP THR ARG LYS ALA LEU ASN TYR VAL PRO LYS
SEQRES 17 B 418 LEU PHE GLU GLU LEU ARG LYS THR TYR GLY PHE ASP HIS
SEQRES 18 B 418 HIS LEU LEU HIS ASP GLY HIS HIS ARG TYR THR PRO GLN
SEQRES 19 B 418 GLU ALA ALA ASN LEU GLY LYS MET LEU GLU PRO TYR GLN
SEQRES 20 B 418 LEU PHE TRP LEU GLU ASP CYS THR PRO ALA GLU ASN GLN
SEQRES 21 B 418 GLU ALA PHE ARG LEU VAL ARG GLN HIS THR VAL THR PRO
SEQRES 22 B 418 LEU ALA VAL GLY GLU ILE PHE ASN THR ILE TRP ASP ALA
SEQRES 23 B 418 LYS ASP LEU ILE GLN ASN GLN LEU ILE ASP TYR ILE ARG
SEQRES 24 B 418 ALA THR VAL VAL GLY ALA GLY GLY LEU THR HIS LEU ARG
SEQRES 25 B 418 ARG ILE ALA ASP LEU ALA SER LEU TYR GLN VAL ARG THR
SEQRES 26 B 418 GLY CYS HIS GLY PRO THR ASP LEU SER PRO VAL THR MET
SEQRES 27 B 418 GLY CYS ALA LEU HIS PHE ASP THR TRP VAL PRO ASN PHE
SEQRES 28 B 418 GLY ILE GLN GLU TYR MET ARG HIS THR GLU GLU THR ASP
SEQRES 29 B 418 ALA VAL PHE PRO HIS ASP TYR TRP PHE GLU LYS GLY GLU
SEQRES 30 B 418 LEU PHE VAL GLY GLU THR PRO GLY HIS GLY VAL ASP ILE
SEQRES 31 B 418 ASP GLU GLU LEU ALA ALA LYS TYR PRO TYR LYS PRO ALA
SEQRES 32 B 418 TYR LEU PRO VAL ALA ARG LEU GLU ASP GLY THR MET TRP
SEQRES 33 B 418 ASN TRP
SEQRES 1 C 418 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG
SEQRES 2 C 418 GLY SER HIS MET LYS ILE THR ALA ALA ARG VAL ILE ILE
SEQRES 3 C 418 THR CYS PRO GLY ARG ASN PHE VAL THR LEU LYS ILE GLU
SEQRES 4 C 418 THR ASP GLN GLY VAL TYR GLY ILE GLY ASP ALA THR LEU
SEQRES 5 C 418 ASN GLY ARG GLU LEU SER VAL VAL ALA TYR LEU GLN GLU
SEQRES 6 C 418 HIS VAL ALA PRO CYS LEU ILE GLY MET ASP PRO ARG ARG
SEQRES 7 C 418 ILE GLU ASP ILE TRP GLN TYR VAL TYR ARG GLY ALA TYR
SEQRES 8 C 418 TRP ARG ARG GLY PRO VAL THR MET ARG ALA ILE ALA ALA
SEQRES 9 C 418 VAL ASP MET ALA LEU TRP ASP ILE LYS ALA LYS MET ALA
SEQRES 10 C 418 GLY MET PRO LEU TYR GLN LEU LEU GLY GLY ARG SER ARG
SEQRES 11 C 418 ASP GLY ILE MET VAL TYR GLY HIS ALA ASN GLY SER ASP
SEQRES 12 C 418 ILE ALA GLU THR VAL GLU ALA VAL GLY HIS TYR ILE ASP
SEQRES 13 C 418 MET GLY TYR LYS ALA ILE ARG ALA GLN THR GLY VAL PRO
SEQRES 14 C 418 GLY ILE LYS ASP ALA TYR GLY VAL GLY ARG GLY LYS LEU
SEQRES 15 C 418 TYR TYR GLU PRO ALA ASP ALA SER LEU PRO SER VAL THR
SEQRES 16 C 418 GLY TRP ASP THR ARG LYS ALA LEU ASN TYR VAL PRO LYS
SEQRES 17 C 418 LEU PHE GLU GLU LEU ARG LYS THR TYR GLY PHE ASP HIS
SEQRES 18 C 418 HIS LEU LEU HIS ASP GLY HIS HIS ARG TYR THR PRO GLN
SEQRES 19 C 418 GLU ALA ALA ASN LEU GLY LYS MET LEU GLU PRO TYR GLN
SEQRES 20 C 418 LEU PHE TRP LEU GLU ASP CYS THR PRO ALA GLU ASN GLN
SEQRES 21 C 418 GLU ALA PHE ARG LEU VAL ARG GLN HIS THR VAL THR PRO
SEQRES 22 C 418 LEU ALA VAL GLY GLU ILE PHE ASN THR ILE TRP ASP ALA
SEQRES 23 C 418 LYS ASP LEU ILE GLN ASN GLN LEU ILE ASP TYR ILE ARG
SEQRES 24 C 418 ALA THR VAL VAL GLY ALA GLY GLY LEU THR HIS LEU ARG
SEQRES 25 C 418 ARG ILE ALA ASP LEU ALA SER LEU TYR GLN VAL ARG THR
SEQRES 26 C 418 GLY CYS HIS GLY PRO THR ASP LEU SER PRO VAL THR MET
SEQRES 27 C 418 GLY CYS ALA LEU HIS PHE ASP THR TRP VAL PRO ASN PHE
SEQRES 28 C 418 GLY ILE GLN GLU TYR MET ARG HIS THR GLU GLU THR ASP
SEQRES 29 C 418 ALA VAL PHE PRO HIS ASP TYR TRP PHE GLU LYS GLY GLU
SEQRES 30 C 418 LEU PHE VAL GLY GLU THR PRO GLY HIS GLY VAL ASP ILE
SEQRES 31 C 418 ASP GLU GLU LEU ALA ALA LYS TYR PRO TYR LYS PRO ALA
SEQRES 32 C 418 TYR LEU PRO VAL ALA ARG LEU GLU ASP GLY THR MET TRP
SEQRES 33 C 418 ASN TRP
SEQRES 1 D 418 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG
SEQRES 2 D 418 GLY SER HIS MET LYS ILE THR ALA ALA ARG VAL ILE ILE
SEQRES 3 D 418 THR CYS PRO GLY ARG ASN PHE VAL THR LEU LYS ILE GLU
SEQRES 4 D 418 THR ASP GLN GLY VAL TYR GLY ILE GLY ASP ALA THR LEU
SEQRES 5 D 418 ASN GLY ARG GLU LEU SER VAL VAL ALA TYR LEU GLN GLU
SEQRES 6 D 418 HIS VAL ALA PRO CYS LEU ILE GLY MET ASP PRO ARG ARG
SEQRES 7 D 418 ILE GLU ASP ILE TRP GLN TYR VAL TYR ARG GLY ALA TYR
SEQRES 8 D 418 TRP ARG ARG GLY PRO VAL THR MET ARG ALA ILE ALA ALA
SEQRES 9 D 418 VAL ASP MET ALA LEU TRP ASP ILE LYS ALA LYS MET ALA
SEQRES 10 D 418 GLY MET PRO LEU TYR GLN LEU LEU GLY GLY ARG SER ARG
SEQRES 11 D 418 ASP GLY ILE MET VAL TYR GLY HIS ALA ASN GLY SER ASP
SEQRES 12 D 418 ILE ALA GLU THR VAL GLU ALA VAL GLY HIS TYR ILE ASP
SEQRES 13 D 418 MET GLY TYR LYS ALA ILE ARG ALA GLN THR GLY VAL PRO
SEQRES 14 D 418 GLY ILE LYS ASP ALA TYR GLY VAL GLY ARG GLY LYS LEU
SEQRES 15 D 418 TYR TYR GLU PRO ALA ASP ALA SER LEU PRO SER VAL THR
SEQRES 16 D 418 GLY TRP ASP THR ARG LYS ALA LEU ASN TYR VAL PRO LYS
SEQRES 17 D 418 LEU PHE GLU GLU LEU ARG LYS THR TYR GLY PHE ASP HIS
SEQRES 18 D 418 HIS LEU LEU HIS ASP GLY HIS HIS ARG TYR THR PRO GLN
SEQRES 19 D 418 GLU ALA ALA ASN LEU GLY LYS MET LEU GLU PRO TYR GLN
SEQRES 20 D 418 LEU PHE TRP LEU GLU ASP CYS THR PRO ALA GLU ASN GLN
SEQRES 21 D 418 GLU ALA PHE ARG LEU VAL ARG GLN HIS THR VAL THR PRO
SEQRES 22 D 418 LEU ALA VAL GLY GLU ILE PHE ASN THR ILE TRP ASP ALA
SEQRES 23 D 418 LYS ASP LEU ILE GLN ASN GLN LEU ILE ASP TYR ILE ARG
SEQRES 24 D 418 ALA THR VAL VAL GLY ALA GLY GLY LEU THR HIS LEU ARG
SEQRES 25 D 418 ARG ILE ALA ASP LEU ALA SER LEU TYR GLN VAL ARG THR
SEQRES 26 D 418 GLY CYS HIS GLY PRO THR ASP LEU SER PRO VAL THR MET
SEQRES 27 D 418 GLY CYS ALA LEU HIS PHE ASP THR TRP VAL PRO ASN PHE
SEQRES 28 D 418 GLY ILE GLN GLU TYR MET ARG HIS THR GLU GLU THR ASP
SEQRES 29 D 418 ALA VAL PHE PRO HIS ASP TYR TRP PHE GLU LYS GLY GLU
SEQRES 30 D 418 LEU PHE VAL GLY GLU THR PRO GLY HIS GLY VAL ASP ILE
SEQRES 31 D 418 ASP GLU GLU LEU ALA ALA LYS TYR PRO TYR LYS PRO ALA
SEQRES 32 D 418 TYR LEU PRO VAL ALA ARG LEU GLU ASP GLY THR MET TRP
SEQRES 33 D 418 ASN TRP
HET MG A 501 1
HET CS2 A 502 13
HET PGE A 503 10
HET CO2 A 504 3
HET CO2 A 505 3
HET PDO A 506 5
HET MG B 501 1
HET CS2 B 502 13
HET PGE B 503 10
HET MG B 504 1
HET PDO B 505 5
HET MG C 501 1
HET CS2 C 502 13
HET PGE C 503 10
HET CO2 C 504 3
HET CO2 C 505 3
HET CO3 C 506 4
HET PDO C 507 5
HET MG D 501 1
HET CS2 D 502 13
HET PGE D 503 10
HET CO2 D 504 3
HET PDO D 505 5
HETNAM MG MAGNESIUM ION
HETNAM CS2 D-MANNONIC ACID
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM CO2 CARBON DIOXIDE
HETNAM PDO 1,3-PROPANDIOL
HETNAM CO3 CARBONATE ION
HETSYN CS2 D-MANNONATE
FORMUL 5 MG 5(MG 2+)
FORMUL 6 CS2 4(C6 H12 O7)
FORMUL 7 PGE 4(C6 H14 O4)
FORMUL 8 CO2 5(C O2)
FORMUL 10 PDO 4(C3 H8 O2)
FORMUL 21 CO3 C O3 2-
FORMUL 28 HOH *1003(H2 O)
HELIX 1 1 ARG A 39 HIS A 50 1 12
HELIX 2 2 HIS A 50 ILE A 56 1 7
HELIX 3 3 ARG A 62 ALA A 74 1 13
HELIX 4 4 GLY A 79 GLY A 102 1 24
HELIX 5 5 PRO A 104 GLY A 110 1 7
HELIX 6 6 ASP A 127 MET A 141 1 15
HELIX 7 7 ASP A 182 GLY A 202 1 21
HELIX 8 8 THR A 216 GLU A 228 1 13
HELIX 9 9 PRO A 229 GLN A 231 5 3
HELIX 10 10 ASN A 243 ALA A 246 5 4
HELIX 11 11 PHE A 247 THR A 254 1 8
HELIX 12 12 THR A 266 ASP A 269 5 4
HELIX 13 13 ALA A 270 ASN A 276 1 7
HELIX 14 14 GLY A 290 TYR A 305 1 16
HELIX 15 15 SER A 318 VAL A 332 1 15
HELIX 16 16 THR A 344 PHE A 351 1 8
HELIX 17 17 ASP A 375 ALA A 380 1 6
HELIX 18 18 ARG B 39 HIS B 50 1 12
HELIX 19 19 HIS B 50 ILE B 56 1 7
HELIX 20 20 ARG B 62 ALA B 74 1 13
HELIX 21 21 GLY B 79 GLY B 102 1 24
HELIX 22 22 PRO B 104 GLY B 110 1 7
HELIX 23 23 ASP B 127 MET B 141 1 15
HELIX 24 24 ASP B 182 GLY B 202 1 21
HELIX 25 25 THR B 216 GLU B 228 1 13
HELIX 26 26 PRO B 229 GLN B 231 5 3
HELIX 27 27 ASN B 243 ALA B 246 5 4
HELIX 28 28 PHE B 247 THR B 254 1 8
HELIX 29 29 THR B 266 ASP B 269 5 4
HELIX 30 30 ALA B 270 ASN B 276 1 7
HELIX 31 31 GLY B 290 TYR B 305 1 16
HELIX 32 32 SER B 318 VAL B 332 1 15
HELIX 33 33 THR B 344 PHE B 351 1 8
HELIX 34 34 ASP B 375 ALA B 380 1 6
HELIX 35 35 ARG C 39 HIS C 50 1 12
HELIX 36 36 HIS C 50 ILE C 56 1 7
HELIX 37 37 ARG C 62 ALA C 74 1 13
HELIX 38 38 GLY C 79 GLY C 102 1 24
HELIX 39 39 PRO C 104 GLY C 110 1 7
HELIX 40 40 ASP C 127 MET C 141 1 15
HELIX 41 41 ASP C 182 GLY C 202 1 21
HELIX 42 42 THR C 216 GLU C 228 1 13
HELIX 43 43 PRO C 229 GLN C 231 5 3
HELIX 44 44 ASN C 243 ALA C 246 5 4
HELIX 45 45 PHE C 247 THR C 254 1 8
HELIX 46 46 THR C 266 ASP C 269 5 4
HELIX 47 47 ALA C 270 ASN C 276 1 7
HELIX 48 48 GLY C 290 TYR C 305 1 16
HELIX 49 49 SER C 318 VAL C 332 1 15
HELIX 50 50 THR C 344 PHE C 351 1 8
HELIX 51 51 ASP C 375 ALA C 380 1 6
HELIX 52 52 ARG D 39 HIS D 50 1 12
HELIX 53 53 HIS D 50 ILE D 56 1 7
HELIX 54 54 ARG D 62 ALA D 74 1 13
HELIX 55 55 GLY D 79 GLY D 102 1 24
HELIX 56 56 PRO D 104 GLY D 110 1 7
HELIX 57 57 ASP D 127 MET D 141 1 15
HELIX 58 58 ASP D 182 ASN D 188 1 7
HELIX 59 59 TYR D 189 GLY D 202 1 14
HELIX 60 60 THR D 216 GLU D 228 1 13
HELIX 61 61 PRO D 229 GLN D 231 5 3
HELIX 62 62 ASN D 243 ALA D 246 5 4
HELIX 63 63 PHE D 247 THR D 254 1 8
HELIX 64 64 THR D 266 ASP D 269 5 4
HELIX 65 65 ALA D 270 ASN D 276 1 7
HELIX 66 66 GLY D 290 TYR D 305 1 16
HELIX 67 67 SER D 318 VAL D 332 1 15
HELIX 68 68 THR D 344 PHE D 351 1 8
HELIX 69 69 ASP D 375 ALA D 380 1 6
SHEET 1 A 3 ILE A 3 THR A 11 0
SHEET 2 A 3 PHE A 17 THR A 24 -1 O THR A 19 N ILE A 9
SHEET 3 A 3 TYR A 29 ASP A 33 -1 O GLY A 32 N LEU A 20
SHEET 1 B11 TYR A 355 GLU A 358 0
SHEET 2 B11 GLU A 361 VAL A 364 -1 O GLU A 361 N GLU A 358
SHEET 3 B11 ILE A 117 GLY A 125 -1 N ILE A 117 O LEU A 362
SHEET 4 B11 PHE A 335 GLU A 339 1 O GLN A 338 N MET A 118
SHEET 5 B11 ARG A 308 CYS A 311 1 N CYS A 311 O GLU A 339
SHEET 6 B11 TYR A 281 ILE A 282 1 N ILE A 282 O GLY A 310
SHEET 7 B11 LEU A 258 VAL A 260 1 N VAL A 260 O TYR A 281
SHEET 8 B11 TRP A 234 GLU A 236 1 N LEU A 235 O ALA A 259
SHEET 9 B11 HIS A 206 ASP A 210 1 N HIS A 209 O GLU A 236
SHEET 10 B11 ALA A 145 THR A 150 1 N ILE A 146 O LEU A 208
SHEET 11 B11 ILE A 117 GLY A 125 1 N GLY A 121 O ARG A 147
SHEET 1 C 2 VAL A 178 TRP A 181 0
SHEET 2 C 2 VAL A 391 LEU A 394 1 O VAL A 391 N THR A 179
SHEET 1 D 3 ILE B 3 THR B 11 0
SHEET 2 D 3 PHE B 17 THR B 24 -1 O THR B 19 N ILE B 9
SHEET 3 D 3 TYR B 29 ASP B 33 -1 O GLY B 32 N LEU B 20
SHEET 1 E 8 ARG B 308 THR B 309 0
SHEET 2 E 8 TYR B 281 ILE B 282 1 N ILE B 282 O ARG B 308
SHEET 3 E 8 LEU B 258 VAL B 260 1 N VAL B 260 O TYR B 281
SHEET 4 E 8 TRP B 234 GLU B 236 1 N LEU B 235 O ALA B 259
SHEET 5 E 8 HIS B 206 ASP B 210 1 N HIS B 209 O GLU B 236
SHEET 6 E 8 ALA B 145 THR B 150 1 N ALA B 148 O LEU B 208
SHEET 7 E 8 ILE B 117 GLY B 125 1 N GLY B 121 O ARG B 147
SHEET 8 E 8 GLN B 338 GLU B 339 1 O GLN B 338 N MET B 118
SHEET 1 F 9 ARG B 308 THR B 309 0
SHEET 2 F 9 TYR B 281 ILE B 282 1 N ILE B 282 O ARG B 308
SHEET 3 F 9 LEU B 258 VAL B 260 1 N VAL B 260 O TYR B 281
SHEET 4 F 9 TRP B 234 GLU B 236 1 N LEU B 235 O ALA B 259
SHEET 5 F 9 HIS B 206 ASP B 210 1 N HIS B 209 O GLU B 236
SHEET 6 F 9 ALA B 145 THR B 150 1 N ALA B 148 O LEU B 208
SHEET 7 F 9 ILE B 117 GLY B 125 1 N GLY B 121 O ARG B 147
SHEET 8 F 9 GLU B 361 VAL B 364 -1 O LEU B 362 N ILE B 117
SHEET 9 F 9 TYR B 355 GLU B 358 -1 N GLU B 358 O GLU B 361
SHEET 1 G 3 VAL B 178 TRP B 181 0
SHEET 2 G 3 VAL B 391 LEU B 394 1 O VAL B 391 N THR B 179
SHEET 3 G 3 MET B 399 TRP B 400 -1 O TRP B 400 N ALA B 392
SHEET 1 H 3 ILE C 3 THR C 11 0
SHEET 2 H 3 PHE C 17 THR C 24 -1 O THR C 19 N ILE C 9
SHEET 3 H 3 TYR C 29 ASP C 33 -1 O GLY C 32 N LEU C 20
SHEET 1 I 8 ARG C 308 THR C 309 0
SHEET 2 I 8 TYR C 281 ILE C 282 1 N ILE C 282 O ARG C 308
SHEET 3 I 8 LEU C 258 VAL C 260 1 O LEU C 258 N TYR C 281
SHEET 4 I 8 TRP C 234 GLU C 236 1 N LEU C 235 O ALA C 259
SHEET 5 I 8 HIS C 206 ASP C 210 1 N HIS C 209 O GLU C 236
SHEET 6 I 8 ALA C 145 THR C 150 1 N ILE C 146 O HIS C 206
SHEET 7 I 8 ILE C 117 GLY C 125 1 N GLY C 121 O ARG C 147
SHEET 8 I 8 GLN C 338 GLU C 339 1 O GLN C 338 N MET C 118
SHEET 1 J 9 ARG C 308 THR C 309 0
SHEET 2 J 9 TYR C 281 ILE C 282 1 N ILE C 282 O ARG C 308
SHEET 3 J 9 LEU C 258 VAL C 260 1 O LEU C 258 N TYR C 281
SHEET 4 J 9 TRP C 234 GLU C 236 1 N LEU C 235 O ALA C 259
SHEET 5 J 9 HIS C 206 ASP C 210 1 N HIS C 209 O GLU C 236
SHEET 6 J 9 ALA C 145 THR C 150 1 N ILE C 146 O HIS C 206
SHEET 7 J 9 ILE C 117 GLY C 125 1 N GLY C 121 O ARG C 147
SHEET 8 J 9 GLU C 361 VAL C 364 -1 O LEU C 362 N ILE C 117
SHEET 9 J 9 TYR C 355 GLU C 358 -1 N GLU C 358 O GLU C 361
SHEET 1 K 3 VAL C 178 TRP C 181 0
SHEET 2 K 3 VAL C 391 LEU C 394 1 O ARG C 393 N THR C 179
SHEET 3 K 3 MET C 399 TRP C 400 -1 O TRP C 400 N ALA C 392
SHEET 1 L 3 ILE D 3 THR D 11 0
SHEET 2 L 3 PHE D 17 THR D 24 -1 O THR D 19 N ILE D 9
SHEET 3 L 3 TYR D 29 ASP D 33 -1 O GLY D 30 N ILE D 22
SHEET 1 M 8 ARG D 308 THR D 309 0
SHEET 2 M 8 TYR D 281 ILE D 282 1 N ILE D 282 O ARG D 308
SHEET 3 M 8 LEU D 258 VAL D 260 1 O LEU D 258 N TYR D 281
SHEET 4 M 8 TRP D 234 GLU D 236 1 N LEU D 235 O ALA D 259
SHEET 5 M 8 HIS D 206 ASP D 210 1 N HIS D 209 O GLU D 236
SHEET 6 M 8 ALA D 145 THR D 150 1 N ALA D 148 O LEU D 208
SHEET 7 M 8 ILE D 117 GLY D 125 1 N GLY D 121 O ARG D 147
SHEET 8 M 8 GLN D 338 GLU D 339 1 O GLN D 338 N MET D 118
SHEET 1 N 9 ARG D 308 THR D 309 0
SHEET 2 N 9 TYR D 281 ILE D 282 1 N ILE D 282 O ARG D 308
SHEET 3 N 9 LEU D 258 VAL D 260 1 O LEU D 258 N TYR D 281
SHEET 4 N 9 TRP D 234 GLU D 236 1 N LEU D 235 O ALA D 259
SHEET 5 N 9 HIS D 206 ASP D 210 1 N HIS D 209 O GLU D 236
SHEET 6 N 9 ALA D 145 THR D 150 1 N ALA D 148 O LEU D 208
SHEET 7 N 9 ILE D 117 GLY D 125 1 N GLY D 121 O ARG D 147
SHEET 8 N 9 GLU D 361 PHE D 363 -1 O LEU D 362 N ILE D 117
SHEET 9 N 9 TRP D 356 GLU D 358 -1 N GLU D 358 O GLU D 361
SHEET 1 O 3 VAL D 178 TRP D 181 0
SHEET 2 O 3 VAL D 391 LEU D 394 1 O VAL D 391 N THR D 179
SHEET 3 O 3 MET D 399 TRP D 400 -1 O TRP D 400 N ALA D 392
LINK OD2 ASP A 210 MG MG A 501 1555 1555 2.12
LINK OE1 GLU A 236 MG MG A 501 1555 1555 2.09
LINK OE1 GLU A 262 MG MG A 501 1555 1555 2.13
LINK MG MG A 501 O2 CS2 A 502 1555 1555 2.05
LINK MG MG A 501 O1B CS2 A 502 1555 1555 2.23
LINK MG MG A 501 O HOH A 848 1555 1555 1.98
LINK OD2 ASP B 210 MG MG B 501 1555 1555 2.12
LINK OE1 GLU B 236 MG MG B 501 1555 1555 2.04
LINK OE1 GLU B 262 MG MG B 501 1555 1555 2.15
LINK MG MG B 501 O1B CS2 B 502 1555 1555 2.12
LINK MG MG B 501 O2 CS2 B 502 1555 1555 2.12
LINK MG MG B 501 O HOH B 856 1555 1555 1.84
LINK MG MG B 504 O HOH B 874 1555 1555 1.98
LINK MG MG B 504 O HOH B 882 1555 1555 2.10
LINK MG MG B 504 O HOH B 883 1555 1555 1.98
LINK MG MG B 504 O HOH D 812 1555 1555 2.14
LINK OD2 ASP C 210 MG MG C 501 1555 1555 2.10
LINK OE1 GLU C 236 MG MG C 501 1555 1555 2.08
LINK OE1 GLU C 262 MG MG C 501 1555 1555 2.11
LINK MG MG C 501 O2 CS2 C 502 1555 1555 2.10
LINK MG MG C 501 O1B CS2 C 502 1555 1555 2.21
LINK MG MG C 501 O HOH C 812 1555 1555 1.98
LINK OD2 ASP D 210 MG MG D 501 1555 1555 2.08
LINK OE1 GLU D 236 MG MG D 501 1555 1555 2.07
LINK OE1 GLU D 262 MG MG D 501 1555 1555 2.20
LINK MG MG D 501 O2 CS2 D 502 1555 1555 2.11
LINK MG MG D 501 O1B CS2 D 502 1555 1555 2.22
LINK MG MG D 501 O HOH D 801 1555 1555 2.02
SITE 1 AC1 5 ASP A 210 GLU A 236 GLU A 262 CS2 A 502
SITE 2 AC1 5 HOH A 848
SITE 1 AC2 19 ASN A 37 HIS A 122 ARG A 147 ASP A 210
SITE 2 AC2 19 HIS A 212 GLU A 236 GLU A 262 ARG A 283
SITE 3 AC2 19 HIS A 312 PRO A 314 ASP A 316 GLU A 339
SITE 4 AC2 19 LEU A 389 TRP A 402 MG A 501 HOH A 634
SITE 5 AC2 19 HOH A 848 TYR B 75 TRP B 76
SITE 1 AC3 4 LYS A 192 GLU A 195 MET A 226 TYR A 230
SITE 1 AC4 9 ARG A 78 GLY A 79 PRO A 80 VAL A 81
SITE 2 AC4 9 THR A 82 GLY B 79 PRO B 80 VAL B 81
SITE 3 AC4 9 THR B 82
SITE 1 AC5 5 GLU A 228 PRO A 229 GLN A 231 HOH A 859
SITE 2 AC5 5 HOH C 718
SITE 1 AC6 4 HIS A 209 ASP A 210 TYR A 215 HOH A 758
SITE 1 AC7 5 ASP B 210 GLU B 236 GLU B 262 CS2 B 502
SITE 2 AC7 5 HOH B 856
SITE 1 AC8 19 TYR A 75 TRP A 76 ASN B 37 HIS B 122
SITE 2 AC8 19 ARG B 147 ASP B 210 HIS B 212 GLU B 236
SITE 3 AC8 19 GLU B 262 ARG B 283 HIS B 312 PRO B 314
SITE 4 AC8 19 ASP B 316 GLU B 339 LEU B 389 TRP B 402
SITE 5 AC8 19 MG B 501 HOH B 625 HOH B 856
SITE 1 AC9 5 PRO B 191 LYS B 192 GLU B 195 TYR B 230
SITE 2 AC9 5 PHE D 203
SITE 1 BC1 4 HOH B 874 HOH B 882 HOH B 883 HOH D 812
SITE 1 BC2 5 HIS B 209 ASP B 210 GLY B 211 TYR B 215
SITE 2 BC2 5 HOH B 745
SITE 1 BC3 5 ASP C 210 GLU C 236 GLU C 262 CS2 C 502
SITE 2 BC3 5 HOH C 812
SITE 1 BC4 19 ASN C 37 HIS C 122 ARG C 147 ASP C 210
SITE 2 BC4 19 HIS C 212 GLU C 236 GLU C 262 ARG C 283
SITE 3 BC4 19 HIS C 312 PRO C 314 ASP C 316 GLU C 339
SITE 4 BC4 19 LEU C 389 TRP C 402 MG C 501 HOH C 613
SITE 5 BC4 19 HOH C 812 TYR D 75 TRP D 76
SITE 1 BC5 4 PRO C 191 LYS C 192 GLU C 195 TYR C 230
SITE 1 BC6 9 ARG C 78 GLY C 79 PRO C 80 VAL C 81
SITE 2 BC6 9 THR C 82 GLY D 79 PRO D 80 VAL D 81
SITE 3 BC6 9 THR D 82
SITE 1 BC7 6 ARG C 297 ALA C 299 ASP C 300 SER C 303
SITE 2 BC7 6 PRO C 333 ASN C 334
SITE 1 BC8 4 ARG C 61 MET C 103 HOH C 682 HOH C 776
SITE 1 BC9 4 TRP C 181 HIS C 209 ASP C 210 TYR C 215
SITE 1 CC1 5 ASP D 210 GLU D 236 GLU D 262 CS2 D 502
SITE 2 CC1 5 HOH D 801
SITE 1 CC2 18 TYR C 75 ASN D 37 HIS D 122 ARG D 147
SITE 2 CC2 18 ASP D 210 HIS D 212 GLU D 236 GLU D 262
SITE 3 CC2 18 ARG D 283 HIS D 312 PRO D 314 ASP D 316
SITE 4 CC2 18 GLU D 339 LEU D 389 TRP D 402 MG D 501
SITE 5 CC2 18 HOH D 621 HOH D 801
SITE 1 CC3 4 ASN D 188 LYS D 192 GLU D 195 TYR D 230
SITE 1 CC4 7 GLU C 245 HOH C 612 LYS D 271 ASP D 272
SITE 2 CC4 7 HOH D 637 HOH D 707 HOH D 820
SITE 1 CC5 3 HIS D 209 GLY D 211 TYR D 215
CRYST1 116.223 165.363 167.197 90.00 90.00 90.00 C 2 2 21 32
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 0.008604 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006047 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005981 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
