HEADER OXIDOREDUCTASE 06-AUG-12 4GGP
TITLE CRYSTAL STRUCTURE OF SELENOMETHIONINE CONTAINING TRANS-2-ENOYL-COA
TITLE 2 REDUCTASE FROM TREPONEMA DENTICOLA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANS-2-ENOYL-COA REDUCTASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 1.1.1.36;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TREPONEMA DENTICOLA;
SOURCE 3 ORGANISM_TAXID: 243275;
SOURCE 4 STRAIN: ATCC 35405;
SOURCE 5 GENE: TDE_0597;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET23A-HIS10-TEV
KEYWDS ROSSMANN FOLD, REDUCTASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.B.BOND-WATTS,A.M.WEEKS,M.C.Y.CHANG
REVDAT 2 10-OCT-12 4GGP 1 JRNL
REVDAT 1 29-AUG-12 4GGP 0
JRNL AUTH B.B.BOND-WATTS,A.M.WEEKS,M.C.CHANG
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF THE
JRNL TITL 2 TRANS-ENOYL-COA REDUCTASE FROM TREPONEMA DENTICOLA.
JRNL REF BIOCHEMISTRY V. 51 6827 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 22906002
JRNL DOI 10.1021/BI300879N
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX AUTOREFINE
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.47
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 103632
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.065
REMARK 3 FREE R VALUE TEST SET COUNT : 5182
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 19.8478 - 6.3033 0.98 3302 175 0.1618 0.1725
REMARK 3 2 6.3033 - 5.0300 0.98 3344 176 0.1851 0.1994
REMARK 3 3 5.0300 - 4.4021 0.98 3287 173 0.1605 0.1890
REMARK 3 4 4.4021 - 4.0032 0.97 3280 172 0.1593 0.1924
REMARK 3 5 4.0032 - 3.7183 0.98 3318 175 0.1627 0.1834
REMARK 3 6 3.7183 - 3.5003 0.98 3300 174 0.1746 0.1982
REMARK 3 7 3.5003 - 3.3258 0.98 3302 173 0.1778 0.2359
REMARK 3 8 3.3258 - 3.1817 0.98 3305 174 0.1872 0.1913
REMARK 3 9 3.1817 - 3.0597 0.98 3293 174 0.1800 0.2030
REMARK 3 10 3.0597 - 2.9544 0.98 3291 173 0.1834 0.2240
REMARK 3 11 2.9544 - 2.8623 0.98 3304 174 0.1778 0.2172
REMARK 3 12 2.8623 - 2.7807 0.97 3281 172 0.1845 0.2343
REMARK 3 13 2.7807 - 2.7077 0.97 3267 173 0.1943 0.2472
REMARK 3 14 2.7077 - 2.6418 0.97 3309 174 0.1930 0.2346
REMARK 3 15 2.6418 - 2.5819 0.97 3301 173 0.1859 0.2307
REMARK 3 16 2.5819 - 2.5270 0.97 3336 176 0.1870 0.2317
REMARK 3 17 2.5270 - 2.4766 0.97 3233 170 0.1870 0.2006
REMARK 3 18 2.4766 - 2.4299 0.97 3295 174 0.1929 0.2496
REMARK 3 19 2.4299 - 2.3866 0.97 3263 171 0.1932 0.2309
REMARK 3 20 2.3866 - 2.3462 0.97 3289 173 0.2061 0.2742
REMARK 3 21 2.3462 - 2.3084 0.97 3212 170 0.2025 0.2361
REMARK 3 22 2.3084 - 2.2730 0.97 3326 175 0.2062 0.2724
REMARK 3 23 2.2730 - 2.2396 0.97 3234 169 0.2121 0.2828
REMARK 3 24 2.2396 - 2.2081 0.96 3278 173 0.2196 0.2585
REMARK 3 25 2.2081 - 2.1783 0.97 3266 171 0.2092 0.2559
REMARK 3 26 2.1783 - 2.1500 0.96 3252 172 0.2140 0.2626
REMARK 3 27 2.1500 - 2.1232 0.97 3263 171 0.2206 0.2380
REMARK 3 28 2.1232 - 2.0976 0.96 3239 171 0.2294 0.2531
REMARK 3 29 2.0976 - 2.0733 0.96 3278 172 0.2388 0.2806
REMARK 3 30 2.0733 - 2.0500 0.96 3202 169 0.2498 0.2869
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.60
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.92
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 : 0.004 12536
REMARK 3 ANGLE : 0.783 16916
REMARK 3 CHIRALITY : 0.057 1872
REMARK 3 PLANARITY : 0.003 2196
REMARK 3 DIHEDRAL : 12.722 4696
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4GGP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-12.
REMARK 100 THE RCSB ID CODE IS RCSB074160.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-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 : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979, 0.957
REMARK 200 MONOCHROMATOR : DOUBLE FLAT CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 114220
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.15000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.6700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.59900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.380
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: PHENIX AUTOSOL AND AUTOBUILD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE, PH 7.5, 25% PEG
REMARK 280 6000, 2.5% GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 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, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLY A -3
REMARK 465 THR A -2
REMARK 465 GLY A -1
REMARK 465 ALA A 0
REMARK 465 GLY B -3
REMARK 465 THR B -2
REMARK 465 GLY B -1
REMARK 465 ALA B 0
REMARK 465 GLY C -3
REMARK 465 THR C -2
REMARK 465 GLY C -1
REMARK 465 ALA C 0
REMARK 465 GLY D -3
REMARK 465 THR D -2
REMARK 465 GLY D -1
REMARK 465 ALA D 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH C 531 O HOH C 556 1.84
REMARK 500 OE1 GLU B 25 O HOH B 463 1.91
REMARK 500 O HOH D 473 O HOH D 474 1.94
REMARK 500 O HOH A 483 O HOH C 483 1.97
REMARK 500 O HOH B 415 O HOH B 436 1.99
REMARK 500 O HOH B 493 O HOH B 500 2.02
REMARK 500 O HOH B 425 O HOH B 504 2.05
REMARK 500 O HOH B 466 O HOH B 471 2.05
REMARK 500 O HOH D 422 O HOH D 493 2.07
REMARK 500 OE2 GLU C 342 O HOH C 482 2.08
REMARK 500 O HOH D 540 O HOH D 542 2.08
REMARK 500 O HOH A 432 O HOH A 530 2.08
REMARK 500 O HOH C 550 O HOH C 551 2.08
REMARK 500 O HOH B 471 O HOH B 480 2.09
REMARK 500 O HOH C 492 O HOH C 494 2.10
REMARK 500 O HOH D 507 O HOH D 523 2.10
REMARK 500 O HOH A 518 O HOH C 493 2.10
REMARK 500 O HOH A 504 O HOH D 510 2.11
REMARK 500 O HOH D 532 O HOH D 533 2.12
REMARK 500 N MSE A 1 O HOH A 468 2.13
REMARK 500 O HOH D 470 O HOH D 526 2.15
REMARK 500 O GLU A 38 NZ LYS A 322 2.15
REMARK 500 O HOH D 470 O HOH D 478 2.16
REMARK 500 ND2 ASN B 303 O HOH B 497 2.17
REMARK 500 N ALA D 361 O HOH D 522 2.17
REMARK 500 O PRO D 46 O HOH D 535 2.17
REMARK 500 O HOH C 455 O HOH C 518 2.18
REMARK 500 O HOH A 518 O HOH C 543 2.18
REMARK 500 O HOH B 486 O HOH B 487 2.18
REMARK 500 N THR A 150 O HOH A 499 2.19
REMARK 500 OD1 ASP A 366 O HOH A 464 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 84 -167.90 -110.18
REMARK 500 VAL A 286 -44.90 75.47
REMARK 500 ARG A 318 -59.05 -129.88
REMARK 500 TYR A 387 -21.94 75.61
REMARK 500 ARG A 396 -169.58 -118.39
REMARK 500 SER B 143 56.03 -142.88
REMARK 500 ALA B 145 78.85 -119.21
REMARK 500 LEU B 162 74.44 -109.18
REMARK 500 VAL B 286 -46.30 78.20
REMARK 500 ARG B 318 -58.95 -130.73
REMARK 500 ALA C 15 135.93 83.69
REMARK 500 SER C 143 42.16 -140.34
REMARK 500 THR C 154 -36.97 -133.35
REMARK 500 VAL C 286 -45.09 76.90
REMARK 500 ARG C 318 -55.18 -129.15
REMARK 500 ASP C 329 -169.17 -79.99
REMARK 500 VAL D 286 -44.51 76.58
REMARK 500 ARG D 318 -56.41 -126.41
REMARK 500 THR D 357 -162.57 -117.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GGO RELATED DB: PDB
DBREF 4GGP A 1 397 UNP Q73Q47 Y597_TREDE 1 397
DBREF 4GGP B 1 397 UNP Q73Q47 Y597_TREDE 1 397
DBREF 4GGP C 1 397 UNP Q73Q47 Y597_TREDE 1 397
DBREF 4GGP D 1 397 UNP Q73Q47 Y597_TREDE 1 397
SEQADV 4GGP GLY A -3 UNP Q73Q47 EXPRESSION TAG
SEQADV 4GGP THR A -2 UNP Q73Q47 EXPRESSION TAG
SEQADV 4GGP GLY A -1 UNP Q73Q47 EXPRESSION TAG
SEQADV 4GGP ALA A 0 UNP Q73Q47 EXPRESSION TAG
SEQADV 4GGP GLY B -3 UNP Q73Q47 EXPRESSION TAG
SEQADV 4GGP THR B -2 UNP Q73Q47 EXPRESSION TAG
SEQADV 4GGP GLY B -1 UNP Q73Q47 EXPRESSION TAG
SEQADV 4GGP ALA B 0 UNP Q73Q47 EXPRESSION TAG
SEQADV 4GGP GLY C -3 UNP Q73Q47 EXPRESSION TAG
SEQADV 4GGP THR C -2 UNP Q73Q47 EXPRESSION TAG
SEQADV 4GGP GLY C -1 UNP Q73Q47 EXPRESSION TAG
SEQADV 4GGP ALA C 0 UNP Q73Q47 EXPRESSION TAG
SEQADV 4GGP GLY D -3 UNP Q73Q47 EXPRESSION TAG
SEQADV 4GGP THR D -2 UNP Q73Q47 EXPRESSION TAG
SEQADV 4GGP GLY D -1 UNP Q73Q47 EXPRESSION TAG
SEQADV 4GGP ALA D 0 UNP Q73Q47 EXPRESSION TAG
SEQRES 1 A 401 GLY THR GLY ALA MSE ILE VAL LYS PRO MSE VAL ARG ASN
SEQRES 2 A 401 ASN ILE CYS LEU ASN ALA HIS PRO GLN GLY CYS LYS LYS
SEQRES 3 A 401 GLY VAL GLU ASP GLN ILE GLU TYR THR LYS LYS ARG ILE
SEQRES 4 A 401 THR ALA GLU VAL LYS ALA GLY ALA LYS ALA PRO LYS ASN
SEQRES 5 A 401 VAL LEU VAL LEU GLY CYS SER ASN GLY TYR GLY LEU ALA
SEQRES 6 A 401 SER ARG ILE THR ALA ALA PHE GLY TYR GLY ALA ALA THR
SEQRES 7 A 401 ILE GLY VAL SER PHE GLU LYS ALA GLY SER GLU THR LYS
SEQRES 8 A 401 TYR GLY THR PRO GLY TRP TYR ASN ASN LEU ALA PHE ASP
SEQRES 9 A 401 GLU ALA ALA LYS ARG GLU GLY LEU TYR SER VAL THR ILE
SEQRES 10 A 401 ASP GLY ASP ALA PHE SER ASP GLU ILE LYS ALA GLN VAL
SEQRES 11 A 401 ILE GLU GLU ALA LYS LYS LYS GLY ILE LYS PHE ASP LEU
SEQRES 12 A 401 ILE VAL TYR SER LEU ALA SER PRO VAL ARG THR ASP PRO
SEQRES 13 A 401 ASP THR GLY ILE MSE HIS LYS SER VAL LEU LYS PRO PHE
SEQRES 14 A 401 GLY LYS THR PHE THR GLY LYS THR VAL ASP PRO PHE THR
SEQRES 15 A 401 GLY GLU LEU LYS GLU ILE SER ALA GLU PRO ALA ASN ASP
SEQRES 16 A 401 GLU GLU ALA ALA ALA THR VAL LYS VAL MSE GLY GLY GLU
SEQRES 17 A 401 ASP TRP GLU ARG TRP ILE LYS GLN LEU SER LYS GLU GLY
SEQRES 18 A 401 LEU LEU GLU GLU GLY CYS ILE THR LEU ALA TYR SER TYR
SEQRES 19 A 401 ILE GLY PRO GLU ALA THR GLN ALA LEU TYR ARG LYS GLY
SEQRES 20 A 401 THR ILE GLY LYS ALA LYS GLU HIS LEU GLU ALA THR ALA
SEQRES 21 A 401 HIS ARG LEU ASN LYS GLU ASN PRO SER ILE ARG ALA PHE
SEQRES 22 A 401 VAL SER VAL ASN LYS GLY LEU VAL THR ARG ALA SER ALA
SEQRES 23 A 401 VAL ILE PRO VAL ILE PRO LEU TYR LEU ALA SER LEU PHE
SEQRES 24 A 401 LYS VAL MSE LYS GLU LYS GLY ASN HIS GLU GLY CYS ILE
SEQRES 25 A 401 GLU GLN ILE THR ARG LEU TYR ALA GLU ARG LEU TYR ARG
SEQRES 26 A 401 LYS ASP GLY THR ILE PRO VAL ASP GLU GLU ASN ARG ILE
SEQRES 27 A 401 ARG ILE ASP ASP TRP GLU LEU GLU GLU ASP VAL GLN LYS
SEQRES 28 A 401 ALA VAL SER ALA LEU MSE GLU LYS VAL THR GLY GLU ASN
SEQRES 29 A 401 ALA GLU SER LEU THR ASP LEU ALA GLY TYR ARG HIS ASP
SEQRES 30 A 401 PHE LEU ALA SER ASN GLY PHE ASP VAL GLU GLY ILE ASN
SEQRES 31 A 401 TYR GLU ALA GLU VAL GLU ARG PHE ASP ARG ILE
SEQRES 1 B 401 GLY THR GLY ALA MSE ILE VAL LYS PRO MSE VAL ARG ASN
SEQRES 2 B 401 ASN ILE CYS LEU ASN ALA HIS PRO GLN GLY CYS LYS LYS
SEQRES 3 B 401 GLY VAL GLU ASP GLN ILE GLU TYR THR LYS LYS ARG ILE
SEQRES 4 B 401 THR ALA GLU VAL LYS ALA GLY ALA LYS ALA PRO LYS ASN
SEQRES 5 B 401 VAL LEU VAL LEU GLY CYS SER ASN GLY TYR GLY LEU ALA
SEQRES 6 B 401 SER ARG ILE THR ALA ALA PHE GLY TYR GLY ALA ALA THR
SEQRES 7 B 401 ILE GLY VAL SER PHE GLU LYS ALA GLY SER GLU THR LYS
SEQRES 8 B 401 TYR GLY THR PRO GLY TRP TYR ASN ASN LEU ALA PHE ASP
SEQRES 9 B 401 GLU ALA ALA LYS ARG GLU GLY LEU TYR SER VAL THR ILE
SEQRES 10 B 401 ASP GLY ASP ALA PHE SER ASP GLU ILE LYS ALA GLN VAL
SEQRES 11 B 401 ILE GLU GLU ALA LYS LYS LYS GLY ILE LYS PHE ASP LEU
SEQRES 12 B 401 ILE VAL TYR SER LEU ALA SER PRO VAL ARG THR ASP PRO
SEQRES 13 B 401 ASP THR GLY ILE MSE HIS LYS SER VAL LEU LYS PRO PHE
SEQRES 14 B 401 GLY LYS THR PHE THR GLY LYS THR VAL ASP PRO PHE THR
SEQRES 15 B 401 GLY GLU LEU LYS GLU ILE SER ALA GLU PRO ALA ASN ASP
SEQRES 16 B 401 GLU GLU ALA ALA ALA THR VAL LYS VAL MSE GLY GLY GLU
SEQRES 17 B 401 ASP TRP GLU ARG TRP ILE LYS GLN LEU SER LYS GLU GLY
SEQRES 18 B 401 LEU LEU GLU GLU GLY CYS ILE THR LEU ALA TYR SER TYR
SEQRES 19 B 401 ILE GLY PRO GLU ALA THR GLN ALA LEU TYR ARG LYS GLY
SEQRES 20 B 401 THR ILE GLY LYS ALA LYS GLU HIS LEU GLU ALA THR ALA
SEQRES 21 B 401 HIS ARG LEU ASN LYS GLU ASN PRO SER ILE ARG ALA PHE
SEQRES 22 B 401 VAL SER VAL ASN LYS GLY LEU VAL THR ARG ALA SER ALA
SEQRES 23 B 401 VAL ILE PRO VAL ILE PRO LEU TYR LEU ALA SER LEU PHE
SEQRES 24 B 401 LYS VAL MSE LYS GLU LYS GLY ASN HIS GLU GLY CYS ILE
SEQRES 25 B 401 GLU GLN ILE THR ARG LEU TYR ALA GLU ARG LEU TYR ARG
SEQRES 26 B 401 LYS ASP GLY THR ILE PRO VAL ASP GLU GLU ASN ARG ILE
SEQRES 27 B 401 ARG ILE ASP ASP TRP GLU LEU GLU GLU ASP VAL GLN LYS
SEQRES 28 B 401 ALA VAL SER ALA LEU MSE GLU LYS VAL THR GLY GLU ASN
SEQRES 29 B 401 ALA GLU SER LEU THR ASP LEU ALA GLY TYR ARG HIS ASP
SEQRES 30 B 401 PHE LEU ALA SER ASN GLY PHE ASP VAL GLU GLY ILE ASN
SEQRES 31 B 401 TYR GLU ALA GLU VAL GLU ARG PHE ASP ARG ILE
SEQRES 1 C 401 GLY THR GLY ALA MSE ILE VAL LYS PRO MSE VAL ARG ASN
SEQRES 2 C 401 ASN ILE CYS LEU ASN ALA HIS PRO GLN GLY CYS LYS LYS
SEQRES 3 C 401 GLY VAL GLU ASP GLN ILE GLU TYR THR LYS LYS ARG ILE
SEQRES 4 C 401 THR ALA GLU VAL LYS ALA GLY ALA LYS ALA PRO LYS ASN
SEQRES 5 C 401 VAL LEU VAL LEU GLY CYS SER ASN GLY TYR GLY LEU ALA
SEQRES 6 C 401 SER ARG ILE THR ALA ALA PHE GLY TYR GLY ALA ALA THR
SEQRES 7 C 401 ILE GLY VAL SER PHE GLU LYS ALA GLY SER GLU THR LYS
SEQRES 8 C 401 TYR GLY THR PRO GLY TRP TYR ASN ASN LEU ALA PHE ASP
SEQRES 9 C 401 GLU ALA ALA LYS ARG GLU GLY LEU TYR SER VAL THR ILE
SEQRES 10 C 401 ASP GLY ASP ALA PHE SER ASP GLU ILE LYS ALA GLN VAL
SEQRES 11 C 401 ILE GLU GLU ALA LYS LYS LYS GLY ILE LYS PHE ASP LEU
SEQRES 12 C 401 ILE VAL TYR SER LEU ALA SER PRO VAL ARG THR ASP PRO
SEQRES 13 C 401 ASP THR GLY ILE MSE HIS LYS SER VAL LEU LYS PRO PHE
SEQRES 14 C 401 GLY LYS THR PHE THR GLY LYS THR VAL ASP PRO PHE THR
SEQRES 15 C 401 GLY GLU LEU LYS GLU ILE SER ALA GLU PRO ALA ASN ASP
SEQRES 16 C 401 GLU GLU ALA ALA ALA THR VAL LYS VAL MSE GLY GLY GLU
SEQRES 17 C 401 ASP TRP GLU ARG TRP ILE LYS GLN LEU SER LYS GLU GLY
SEQRES 18 C 401 LEU LEU GLU GLU GLY CYS ILE THR LEU ALA TYR SER TYR
SEQRES 19 C 401 ILE GLY PRO GLU ALA THR GLN ALA LEU TYR ARG LYS GLY
SEQRES 20 C 401 THR ILE GLY LYS ALA LYS GLU HIS LEU GLU ALA THR ALA
SEQRES 21 C 401 HIS ARG LEU ASN LYS GLU ASN PRO SER ILE ARG ALA PHE
SEQRES 22 C 401 VAL SER VAL ASN LYS GLY LEU VAL THR ARG ALA SER ALA
SEQRES 23 C 401 VAL ILE PRO VAL ILE PRO LEU TYR LEU ALA SER LEU PHE
SEQRES 24 C 401 LYS VAL MSE LYS GLU LYS GLY ASN HIS GLU GLY CYS ILE
SEQRES 25 C 401 GLU GLN ILE THR ARG LEU TYR ALA GLU ARG LEU TYR ARG
SEQRES 26 C 401 LYS ASP GLY THR ILE PRO VAL ASP GLU GLU ASN ARG ILE
SEQRES 27 C 401 ARG ILE ASP ASP TRP GLU LEU GLU GLU ASP VAL GLN LYS
SEQRES 28 C 401 ALA VAL SER ALA LEU MSE GLU LYS VAL THR GLY GLU ASN
SEQRES 29 C 401 ALA GLU SER LEU THR ASP LEU ALA GLY TYR ARG HIS ASP
SEQRES 30 C 401 PHE LEU ALA SER ASN GLY PHE ASP VAL GLU GLY ILE ASN
SEQRES 31 C 401 TYR GLU ALA GLU VAL GLU ARG PHE ASP ARG ILE
SEQRES 1 D 401 GLY THR GLY ALA MSE ILE VAL LYS PRO MSE VAL ARG ASN
SEQRES 2 D 401 ASN ILE CYS LEU ASN ALA HIS PRO GLN GLY CYS LYS LYS
SEQRES 3 D 401 GLY VAL GLU ASP GLN ILE GLU TYR THR LYS LYS ARG ILE
SEQRES 4 D 401 THR ALA GLU VAL LYS ALA GLY ALA LYS ALA PRO LYS ASN
SEQRES 5 D 401 VAL LEU VAL LEU GLY CYS SER ASN GLY TYR GLY LEU ALA
SEQRES 6 D 401 SER ARG ILE THR ALA ALA PHE GLY TYR GLY ALA ALA THR
SEQRES 7 D 401 ILE GLY VAL SER PHE GLU LYS ALA GLY SER GLU THR LYS
SEQRES 8 D 401 TYR GLY THR PRO GLY TRP TYR ASN ASN LEU ALA PHE ASP
SEQRES 9 D 401 GLU ALA ALA LYS ARG GLU GLY LEU TYR SER VAL THR ILE
SEQRES 10 D 401 ASP GLY ASP ALA PHE SER ASP GLU ILE LYS ALA GLN VAL
SEQRES 11 D 401 ILE GLU GLU ALA LYS LYS LYS GLY ILE LYS PHE ASP LEU
SEQRES 12 D 401 ILE VAL TYR SER LEU ALA SER PRO VAL ARG THR ASP PRO
SEQRES 13 D 401 ASP THR GLY ILE MSE HIS LYS SER VAL LEU LYS PRO PHE
SEQRES 14 D 401 GLY LYS THR PHE THR GLY LYS THR VAL ASP PRO PHE THR
SEQRES 15 D 401 GLY GLU LEU LYS GLU ILE SER ALA GLU PRO ALA ASN ASP
SEQRES 16 D 401 GLU GLU ALA ALA ALA THR VAL LYS VAL MSE GLY GLY GLU
SEQRES 17 D 401 ASP TRP GLU ARG TRP ILE LYS GLN LEU SER LYS GLU GLY
SEQRES 18 D 401 LEU LEU GLU GLU GLY CYS ILE THR LEU ALA TYR SER TYR
SEQRES 19 D 401 ILE GLY PRO GLU ALA THR GLN ALA LEU TYR ARG LYS GLY
SEQRES 20 D 401 THR ILE GLY LYS ALA LYS GLU HIS LEU GLU ALA THR ALA
SEQRES 21 D 401 HIS ARG LEU ASN LYS GLU ASN PRO SER ILE ARG ALA PHE
SEQRES 22 D 401 VAL SER VAL ASN LYS GLY LEU VAL THR ARG ALA SER ALA
SEQRES 23 D 401 VAL ILE PRO VAL ILE PRO LEU TYR LEU ALA SER LEU PHE
SEQRES 24 D 401 LYS VAL MSE LYS GLU LYS GLY ASN HIS GLU GLY CYS ILE
SEQRES 25 D 401 GLU GLN ILE THR ARG LEU TYR ALA GLU ARG LEU TYR ARG
SEQRES 26 D 401 LYS ASP GLY THR ILE PRO VAL ASP GLU GLU ASN ARG ILE
SEQRES 27 D 401 ARG ILE ASP ASP TRP GLU LEU GLU GLU ASP VAL GLN LYS
SEQRES 28 D 401 ALA VAL SER ALA LEU MSE GLU LYS VAL THR GLY GLU ASN
SEQRES 29 D 401 ALA GLU SER LEU THR ASP LEU ALA GLY TYR ARG HIS ASP
SEQRES 30 D 401 PHE LEU ALA SER ASN GLY PHE ASP VAL GLU GLY ILE ASN
SEQRES 31 D 401 TYR GLU ALA GLU VAL GLU ARG PHE ASP ARG ILE
MODRES 4GGP MSE A 1 MET SELENOMETHIONINE
MODRES 4GGP MSE A 6 MET SELENOMETHIONINE
MODRES 4GGP MSE A 157 MET SELENOMETHIONINE
MODRES 4GGP MSE A 201 MET SELENOMETHIONINE
MODRES 4GGP MSE A 298 MET SELENOMETHIONINE
MODRES 4GGP MSE A 353 MET SELENOMETHIONINE
MODRES 4GGP MSE B 1 MET SELENOMETHIONINE
MODRES 4GGP MSE B 6 MET SELENOMETHIONINE
MODRES 4GGP MSE B 157 MET SELENOMETHIONINE
MODRES 4GGP MSE B 201 MET SELENOMETHIONINE
MODRES 4GGP MSE B 298 MET SELENOMETHIONINE
MODRES 4GGP MSE B 353 MET SELENOMETHIONINE
MODRES 4GGP MSE C 1 MET SELENOMETHIONINE
MODRES 4GGP MSE C 6 MET SELENOMETHIONINE
MODRES 4GGP MSE C 157 MET SELENOMETHIONINE
MODRES 4GGP MSE C 201 MET SELENOMETHIONINE
MODRES 4GGP MSE C 298 MET SELENOMETHIONINE
MODRES 4GGP MSE C 353 MET SELENOMETHIONINE
MODRES 4GGP MSE D 1 MET SELENOMETHIONINE
MODRES 4GGP MSE D 6 MET SELENOMETHIONINE
MODRES 4GGP MSE D 157 MET SELENOMETHIONINE
MODRES 4GGP MSE D 201 MET SELENOMETHIONINE
MODRES 4GGP MSE D 298 MET SELENOMETHIONINE
MODRES 4GGP MSE D 353 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 6 8
HET MSE A 157 8
HET MSE A 201 8
HET MSE A 298 8
HET MSE A 353 8
HET MSE B 1 8
HET MSE B 6 8
HET MSE B 157 8
HET MSE B 201 8
HET MSE B 298 8
HET MSE B 353 8
HET MSE C 1 8
HET MSE C 6 8
HET MSE C 157 8
HET MSE C 201 8
HET MSE C 298 8
HET MSE C 353 8
HET MSE D 1 8
HET MSE D 6 8
HET MSE D 157 8
HET MSE D 201 8
HET MSE D 298 8
HET MSE D 353 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 24(C5 H11 N O2 SE)
FORMUL 5 HOH *545(H2 O)
HELIX 1 1 HIS A 16 ILE A 35 1 20
HELIX 2 2 THR A 36 ALA A 41 1 6
HELIX 3 3 ASN A 56 GLY A 71 1 16
HELIX 4 4 THR A 90 GLY A 107 1 18
HELIX 5 5 SER A 119 GLY A 134 1 16
HELIX 6 6 ASN A 190 GLY A 202 1 13
HELIX 7 7 GLY A 203 GLU A 216 1 14
HELIX 8 8 PRO A 233 ALA A 235 5 3
HELIX 9 9 THR A 236 ARG A 241 1 6
HELIX 10 10 GLY A 243 ASN A 263 1 21
HELIX 11 11 ALA A 280 ILE A 284 5 5
HELIX 12 12 VAL A 286 GLY A 302 1 17
HELIX 13 13 GLY A 306 ARG A 318 1 13
HELIX 14 14 GLU A 342 VAL A 356 1 15
HELIX 15 15 ASN A 360 THR A 365 1 6
HELIX 16 16 ASP A 366 SER A 377 1 12
HELIX 17 17 HIS B 16 ILE B 35 1 20
HELIX 18 18 THR B 36 ALA B 41 1 6
HELIX 19 19 ASN B 56 GLY B 71 1 16
HELIX 20 20 THR B 90 GLU B 106 1 17
HELIX 21 21 SER B 119 GLY B 134 1 16
HELIX 22 22 ASN B 190 GLY B 202 1 13
HELIX 23 23 GLY B 203 GLU B 216 1 14
HELIX 24 24 THR B 236 ARG B 241 1 6
HELIX 25 25 GLY B 243 ASN B 263 1 21
HELIX 26 26 VAL B 286 GLY B 302 1 17
HELIX 27 27 GLY B 306 ARG B 318 1 13
HELIX 28 28 GLU B 342 GLU B 354 1 13
HELIX 29 29 ASN B 360 THR B 365 1 6
HELIX 30 30 ASP B 366 SER B 377 1 12
HELIX 31 31 HIS C 16 ILE C 35 1 20
HELIX 32 32 THR C 36 ALA C 41 1 6
HELIX 33 33 ASN C 56 GLY C 71 1 16
HELIX 34 34 THR C 90 GLU C 106 1 17
HELIX 35 35 SER C 119 GLY C 134 1 16
HELIX 36 36 ASN C 190 GLY C 202 1 13
HELIX 37 37 GLY C 203 GLU C 216 1 14
HELIX 38 38 PRO C 233 ALA C 235 5 3
HELIX 39 39 THR C 236 ARG C 241 1 6
HELIX 40 40 GLY C 243 GLU C 262 1 20
HELIX 41 41 ALA C 280 ILE C 284 5 5
HELIX 42 42 VAL C 286 GLY C 302 1 17
HELIX 43 43 GLY C 306 ARG C 318 1 13
HELIX 44 44 GLU C 342 VAL C 356 1 15
HELIX 45 45 ASN C 360 THR C 365 1 6
HELIX 46 46 ASP C 366 SER C 377 1 12
HELIX 47 47 HIS D 16 ILE D 35 1 20
HELIX 48 48 THR D 36 ALA D 41 1 6
HELIX 49 49 ASN D 56 GLY D 71 1 16
HELIX 50 50 THR D 90 GLY D 107 1 18
HELIX 51 51 SER D 119 GLY D 134 1 16
HELIX 52 52 ASN D 190 GLY D 202 1 13
HELIX 53 53 GLY D 203 GLU D 216 1 14
HELIX 54 54 PRO D 233 ALA D 235 5 3
HELIX 55 55 THR D 236 ARG D 241 1 6
HELIX 56 56 GLY D 243 ASN D 263 1 21
HELIX 57 57 ALA D 280 ILE D 284 5 5
HELIX 58 58 VAL D 286 GLY D 302 1 17
HELIX 59 59 GLY D 306 ARG D 318 1 13
HELIX 60 60 GLU D 342 GLU D 354 1 13
HELIX 61 61 ASN D 360 THR D 365 1 6
HELIX 62 62 ASP D 366 SER D 377 1 12
SHEET 1 A 2 VAL A 7 ARG A 8 0
SHEET 2 A 2 ILE A 11 CYS A 12 -1 O ILE A 11 N ARG A 8
SHEET 1 B 7 SER A 110 ASP A 114 0
SHEET 2 B 7 ALA A 73 SER A 78 1 N GLY A 76 O ILE A 113
SHEET 3 B 7 ASN A 48 LEU A 52 1 N VAL A 49 O ALA A 73
SHEET 4 B 7 PHE A 137 TYR A 142 1 O VAL A 141 N LEU A 50
SHEET 5 B 7 LEU A 219 SER A 229 1 O LEU A 226 N TYR A 142
SHEET 6 B 7 ILE A 266 VAL A 272 1 O SER A 271 N ALA A 227
SHEET 7 B 7 ILE A 334 ARG A 335 1 O ILE A 334 N VAL A 272
SHEET 1 C 2 VAL A 148 THR A 150 0
SHEET 2 C 2 MSE A 157 LYS A 159 -1 O HIS A 158 N ARG A 149
SHEET 1 D 2 PHE A 169 VAL A 174 0
SHEET 2 D 2 LEU A 181 ALA A 186 -1 O ALA A 186 N PHE A 169
SHEET 1 E 2 VAL B 7 ARG B 8 0
SHEET 2 E 2 ILE B 11 CYS B 12 -1 O ILE B 11 N ARG B 8
SHEET 1 F 7 SER B 110 ASP B 114 0
SHEET 2 F 7 ALA B 73 SER B 78 1 N GLY B 76 O ILE B 113
SHEET 3 F 7 ASN B 48 LEU B 52 1 N VAL B 49 O ALA B 73
SHEET 4 F 7 PHE B 137 TYR B 142 1 O VAL B 141 N LEU B 52
SHEET 5 F 7 LEU B 219 SER B 229 1 O LEU B 226 N TYR B 142
SHEET 6 F 7 ILE B 266 VAL B 272 1 O SER B 271 N ALA B 227
SHEET 7 F 7 ILE B 334 ARG B 335 1 O ILE B 334 N VAL B 272
SHEET 1 G 2 VAL B 148 THR B 150 0
SHEET 2 G 2 MSE B 157 LYS B 159 -1 O HIS B 158 N ARG B 149
SHEET 1 H 2 PHE B 169 VAL B 174 0
SHEET 2 H 2 LEU B 181 ALA B 186 -1 O ALA B 186 N PHE B 169
SHEET 1 I 2 VAL C 7 ARG C 8 0
SHEET 2 I 2 ILE C 11 CYS C 12 -1 O ILE C 11 N ARG C 8
SHEET 1 J 7 SER C 110 ASP C 114 0
SHEET 2 J 7 ALA C 73 SER C 78 1 N GLY C 76 O ILE C 113
SHEET 3 J 7 ASN C 48 LEU C 52 1 N VAL C 49 O ALA C 73
SHEET 4 J 7 PHE C 137 TYR C 142 1 O VAL C 141 N LEU C 52
SHEET 5 J 7 LEU C 219 SER C 229 1 O LEU C 226 N TYR C 142
SHEET 6 J 7 ARG C 267 VAL C 272 1 O ARG C 267 N CYS C 223
SHEET 7 J 7 ILE C 334 ARG C 335 1 O ILE C 334 N VAL C 272
SHEET 1 K 2 VAL C 148 THR C 150 0
SHEET 2 K 2 MSE C 157 LYS C 159 -1 O HIS C 158 N ARG C 149
SHEET 1 L 2 PHE C 169 VAL C 174 0
SHEET 2 L 2 LEU C 181 ALA C 186 -1 O LYS C 182 N THR C 173
SHEET 1 M 2 VAL D 7 ARG D 8 0
SHEET 2 M 2 ILE D 11 CYS D 12 -1 O ILE D 11 N ARG D 8
SHEET 1 N 7 SER D 110 ASP D 114 0
SHEET 2 N 7 ALA D 73 SER D 78 1 N GLY D 76 O ILE D 113
SHEET 3 N 7 ASN D 48 LEU D 52 1 N VAL D 49 O ILE D 75
SHEET 4 N 7 PHE D 137 TYR D 142 1 O VAL D 141 N LEU D 52
SHEET 5 N 7 LEU D 219 SER D 229 1 O LEU D 226 N TYR D 142
SHEET 6 N 7 ILE D 266 VAL D 272 1 O SER D 271 N ALA D 227
SHEET 7 N 7 ILE D 334 ARG D 335 1 O ILE D 334 N VAL D 272
SHEET 1 O 2 VAL D 148 THR D 150 0
SHEET 2 O 2 MSE D 157 LYS D 159 -1 O HIS D 158 N ARG D 149
SHEET 1 P 2 PHE D 169 VAL D 174 0
SHEET 2 P 2 LEU D 181 ALA D 186 -1 O ALA D 186 N PHE D 169
LINK C MSE A 1 N ILE A 2 1555 1555 1.33
LINK C PRO A 5 N MSE A 6 1555 1555 1.33
LINK C MSE A 6 N VAL A 7 1555 1555 1.33
LINK C ILE A 156 N MSE A 157 1555 1555 1.33
LINK C MSE A 157 N HIS A 158 1555 1555 1.33
LINK C VAL A 200 N MSE A 201 1555 1555 1.33
LINK C MSE A 201 N GLY A 202 1555 1555 1.33
LINK C VAL A 297 N MSE A 298 1555 1555 1.33
LINK C MSE A 298 N LYS A 299 1555 1555 1.33
LINK C LEU A 352 N MSE A 353 1555 1555 1.33
LINK C MSE A 353 N GLU A 354 1555 1555 1.33
LINK C MSE B 1 N ILE B 2 1555 1555 1.33
LINK C PRO B 5 N MSE B 6 1555 1555 1.33
LINK C MSE B 6 N VAL B 7 1555 1555 1.33
LINK C ILE B 156 N MSE B 157 1555 1555 1.33
LINK C MSE B 157 N HIS B 158 1555 1555 1.33
LINK C VAL B 200 N MSE B 201 1555 1555 1.33
LINK C MSE B 201 N GLY B 202 1555 1555 1.33
LINK C VAL B 297 N MSE B 298 1555 1555 1.33
LINK C MSE B 298 N LYS B 299 1555 1555 1.33
LINK C LEU B 352 N MSE B 353 1555 1555 1.33
LINK C MSE B 353 N GLU B 354 1555 1555 1.33
LINK C MSE C 1 N ILE C 2 1555 1555 1.33
LINK C PRO C 5 N MSE C 6 1555 1555 1.33
LINK C MSE C 6 N VAL C 7 1555 1555 1.33
LINK C ILE C 156 N MSE C 157 1555 1555 1.33
LINK C MSE C 157 N HIS C 158 1555 1555 1.33
LINK C VAL C 200 N MSE C 201 1555 1555 1.33
LINK C MSE C 201 N GLY C 202 1555 1555 1.33
LINK C VAL C 297 N MSE C 298 1555 1555 1.33
LINK C MSE C 298 N LYS C 299 1555 1555 1.33
LINK C LEU C 352 N MSE C 353 1555 1555 1.33
LINK C MSE C 353 N GLU C 354 1555 1555 1.33
LINK C MSE D 1 N ILE D 2 1555 1555 1.33
LINK C PRO D 5 N MSE D 6 1555 1555 1.33
LINK C MSE D 6 N VAL D 7 1555 1555 1.33
LINK C ILE D 156 N MSE D 157 1555 1555 1.33
LINK C MSE D 157 N HIS D 158 1555 1555 1.33
LINK C VAL D 200 N MSE D 201 1555 1555 1.33
LINK C MSE D 201 N GLY D 202 1555 1555 1.33
LINK C VAL D 297 N MSE D 298 1555 1555 1.33
LINK C MSE D 298 N LYS D 299 1555 1555 1.33
LINK C LEU D 352 N MSE D 353 1555 1555 1.33
LINK C MSE D 353 N GLU D 354 1555 1555 1.33
CRYST1 62.580 87.680 91.990 106.25 109.85 98.34 P 1 4
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 0.015974 0.002330 0.007068 0.00000
SCALE2 0.000000 0.011523 0.004368 0.00000
SCALE3 0.000000 0.000000 0.012363 0.00000
HETATM 1 N MSE A 1 -16.039 0.394 -31.451 1.00 62.12 N
HETATM 2 CA MSE A 1 -17.360 -0.100 -31.080 1.00 62.52 C
HETATM 3 C MSE A 1 -17.593 -0.058 -29.573 1.00 57.16 C
HETATM 4 O MSE A 1 -17.027 -0.852 -28.821 1.00 45.00 O
HETATM 5 CB MSE A 1 -17.562 -1.521 -31.600 1.00 50.37 C
HETATM 6 CG MSE A 1 -17.575 -1.621 -33.112 1.00 80.03 C
HETATM 7 SE MSE A 1 -17.573 -3.467 -33.727 1.00127.19 SE
HETATM 8 CE MSE A 1 -15.865 -4.021 -32.975 1.00 56.90 C
(ATOM LINES ARE NOT SHOWN.)
END
