HEADER TRANSFERASE 10-MAR-10 3M49
TITLE CRYSTAL STRUCTURE OF TRANSKETOLASE COMPLEXED WITH THIAMINE DIPHOSPHATE
TITLE 2 FROM BACILLUS ANTHRACIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSKETOLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.2.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;
SOURCE 3 ORGANISM_TAXID: 261594;
SOURCE 4 STRAIN: AMES ANCESTOR;
SOURCE 5 GENE: BAS3470, BA_3744, GBAA3744, GBAA_3744, TKT-2, TKT2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS ALPHA-BETA-ALPHA SANDWICH, CSGID, TRANSFERASE, STRUCTURAL GENOMICS,
KEYWDS 2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
EXPDTA X-RAY DIFFRACTION
AUTHOR N.MALTSEVA,Y.KIM,K.KWON,W.F.ANDERSON,A.JOACHIMIAK,CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 3 04-AUG-21 3M49 1 COMPND REMARK SEQADV HET
REVDAT 3 2 1 HETNAM FORMUL LINK SITE
REVDAT 3 3 1 ATOM
REVDAT 2 08-NOV-17 3M49 1 REMARK
REVDAT 1 07-APR-10 3M49 0
SPRSDE 07-APR-10 3M49 3K95
JRNL AUTH N.MALTSEVA,Y.KIM,K.KWON,W.F.ANDERSON,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF TRANSKETOLASE COMPLEXED WITH THIAMINE
JRNL TITL 2 DIPHOSPHATE FROM BACILLUS ANTHRACIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6_289)
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.73
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 102066
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.139
REMARK 3 R VALUE (WORKING SET) : 0.137
REMARK 3 FREE R VALUE : 0.172
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 5095
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 31.7358 - 4.3056 1.00 10224 485 0.1443 0.1736
REMARK 3 2 4.3056 - 3.4188 1.00 9800 547 0.1175 0.1407
REMARK 3 3 3.4188 - 2.9870 1.00 9739 540 0.1382 0.1672
REMARK 3 4 2.9870 - 2.7141 0.99 9706 488 0.1454 0.1932
REMARK 3 5 2.7141 - 2.5196 0.99 9669 496 0.1347 0.1674
REMARK 3 6 2.5196 - 2.3711 0.99 9645 483 0.1305 0.1812
REMARK 3 7 2.3711 - 2.2524 0.99 9568 532 0.1327 0.1802
REMARK 3 8 2.2524 - 2.1544 0.99 9600 510 0.1326 0.1781
REMARK 3 9 2.1544 - 2.0715 0.99 9508 513 0.1345 0.1857
REMARK 3 10 2.0715 - 2.0000 0.99 9512 501 0.1480 0.1969
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 : 0.36
REMARK 3 B_SOL : 40.17
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.54
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.31370
REMARK 3 B22 (A**2) : -2.99110
REMARK 3 B33 (A**2) : 6.30490
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.012 10835
REMARK 3 ANGLE : 1.278 14702
REMARK 3 CHIRALITY : 0.086 1576
REMARK 3 PLANARITY : 0.006 1923
REMARK 3 DIHEDRAL : 16.849 3878
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 37.1926 22.3358 121.1730
REMARK 3 T TENSOR
REMARK 3 T11: 0.0150 T22: 0.0114
REMARK 3 T33: -0.0735 T12: 0.0048
REMARK 3 T13: 0.0138 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.2787 L22: 0.3821
REMARK 3 L33: 0.0711 L12: -0.0200
REMARK 3 L13: -0.0493 L23: -0.0217
REMARK 3 S TENSOR
REMARK 3 S11: -0.0171 S12: 0.0057 S13: 0.0630
REMARK 3 S21: -0.0605 S22: -0.0172 S23: -0.0072
REMARK 3 S31: -0.0114 S32: -0.0311 S33: 0.0167
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 3M49 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058088.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 103149
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.45200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000, MLPHARE, SOLVE, SHELX, DM, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMOMIUM SULFATE, 0.1 M BIS-TRIS
REMARK 280 PH 6.5, 25% PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 41.66650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.65950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 66.04350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.65950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.66650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 66.04350
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 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 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 MSE A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 GLY A -14
REMARK 465 VAL A -13
REMARK 465 ASP A -12
REMARK 465 LEU A -11
REMARK 465 GLY A -10
REMARK 465 THR A -9
REMARK 465 GLU A -8
REMARK 465 ASN A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 PHE A -4
REMARK 465 GLN A -3
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 MSE B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 SER B -16
REMARK 465 SER B -15
REMARK 465 GLY B -14
REMARK 465 VAL B -13
REMARK 465 ASP B -12
REMARK 465 LEU B -11
REMARK 465 GLY B -10
REMARK 465 THR B -9
REMARK 465 GLU B -8
REMARK 465 ASN B -7
REMARK 465 LEU B -6
REMARK 465 TYR B -5
REMARK 465 PHE B -4
REMARK 465 GLN B -3
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MSE B 1
REMARK 465 SER B 2
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 O3B TPP A 701 O HOH A 1039 2.06
REMARK 500 O1 FMT B 707 O HOH B 1028 2.14
REMARK 500 O2 SO4 A 702 C2 TPP B 701 2.18
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 ASP A 142 -118.14 40.62
REMARK 500 ASP A 148 90.73 -163.58
REMARK 500 SER A 198 -7.82 -141.29
REMARK 500 SER A 200 15.94 -148.90
REMARK 500 ILE A 477 -58.30 -131.57
REMARK 500 PHE B 46 -44.87 -130.12
REMARK 500 ASP B 142 -128.91 56.59
REMARK 500 ASP B 148 89.11 -164.12
REMARK 500 SER B 198 -3.87 -146.19
REMARK 500 ILE B 477 -57.80 -130.92
REMARK 500 ASN B 512 12.72 -141.57
REMARK 500 MSE B 586 75.28 -119.92
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 716 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 157 OD2
REMARK 620 2 ASN A 187 OD1 84.8
REMARK 620 3 ILE A 189 O 106.5 92.2
REMARK 620 4 TPP A 701 O2B 159.3 79.6 87.8
REMARK 620 5 TPP A 701 O2A 100.8 173.2 89.8 94.0
REMARK 620 6 HOH A1038 O 81.7 93.3 170.5 85.6 83.9
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 TPP A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 711
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG5 A 712
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 713
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 714
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 715
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 716
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 717
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 718
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 719
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 720
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 721
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 722
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 723
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 724
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 711
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 712
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 713
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 714
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HYL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TRANSKETOLASE FROM BACILLUS ANTHRACIS
REMARK 900 RELATED ID: 3K95 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TRANSKETOLASE COMPLEXED WITH THIAMINE
REMARK 900 DIPHOSPHATE FROM BACILLUS ANTHRACIS
REMARK 900 RELATED ID: IDP02454 RELATED DB: TARGETDB
DBREF 3M49 A 1 666 UNP Q81Y15 Q81Y15_BACAN 1 666
DBREF 3M49 B 1 666 UNP Q81Y15 Q81Y15_BACAN 1 666
SEQADV 3M49 MSE A -23 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 HIS A -22 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 HIS A -21 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 HIS A -20 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 HIS A -19 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 HIS A -18 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 HIS A -17 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 SER A -16 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 SER A -15 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 GLY A -14 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 VAL A -13 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 ASP A -12 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 LEU A -11 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 GLY A -10 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 THR A -9 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 GLU A -8 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 ASN A -7 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 LEU A -6 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 TYR A -5 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 PHE A -4 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 GLN A -3 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 SER A -2 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 ASN A -1 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 ALA A 0 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 MSE B -23 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 HIS B -22 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 HIS B -21 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 HIS B -20 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 HIS B -19 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 HIS B -18 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 HIS B -17 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 SER B -16 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 SER B -15 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 GLY B -14 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 VAL B -13 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 ASP B -12 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 LEU B -11 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 GLY B -10 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 THR B -9 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 GLU B -8 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 ASN B -7 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 LEU B -6 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 TYR B -5 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 PHE B -4 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 GLN B -3 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 SER B -2 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 ASN B -1 UNP Q81Y15 EXPRESSION TAG
SEQADV 3M49 ALA B 0 UNP Q81Y15 EXPRESSION TAG
SEQRES 1 A 690 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 690 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MSE SER
SEQRES 3 A 690 HIS SER ILE GLU GLN LEU SER ILE ASN THR ILE ARG THR
SEQRES 4 A 690 LEU SER ILE ASP ALA ILE GLU LYS ALA ASN SER GLY HIS
SEQRES 5 A 690 PRO GLY MSE PRO MSE GLY ALA ALA PRO MSE ALA TYR THR
SEQRES 6 A 690 LEU TRP THR GLN PHE MSE LYS HIS ASN PRO ASN ASN PRO
SEQRES 7 A 690 THR TRP PHE ASN ARG ASP ARG PHE VAL LEU SER ALA GLY
SEQRES 8 A 690 HIS GLY SER MSE LEU LEU TYR SER LEU LEU HIS LEU SER
SEQRES 9 A 690 GLY TYR ASP VAL THR MSE ASP ASP LEU LYS ASN PHE ARG
SEQRES 10 A 690 GLN TRP GLY SER LYS THR PRO GLY HIS PRO GLU TYR GLY
SEQRES 11 A 690 HIS THR ALA GLY VAL ASP ALA THR THR GLY PRO LEU GLY
SEQRES 12 A 690 GLN GLY ILE ALA THR ALA VAL GLY MSE ALA MSE ALA GLU
SEQRES 13 A 690 ARG HIS LEU ALA ALA LYS TYR ASN ARG ASP ALA TYR ASN
SEQRES 14 A 690 ILE VAL ASP HIS TYR THR TYR ALA ILE CYS GLY ASP GLY
SEQRES 15 A 690 ASP LEU MSE GLU GLY VAL SER ALA GLU ALA SER SER LEU
SEQRES 16 A 690 ALA ALA HIS LEU GLN LEU GLY ARG LEU VAL VAL LEU TYR
SEQRES 17 A 690 ASP SER ASN ASP ILE SER LEU ASP GLY ASP LEU ASN ARG
SEQRES 18 A 690 SER PHE SER GLU SER VAL GLU ASP ARG TYR LYS ALA TYR
SEQRES 19 A 690 GLY TRP GLN VAL ILE ARG VAL GLU ASP GLY ASN ASP ILE
SEQRES 20 A 690 GLU ALA ILE ALA LYS ALA ILE GLU GLU ALA LYS ALA ASP
SEQRES 21 A 690 GLU LYS ARG PRO THR LEU ILE GLU VAL ARG THR THR ILE
SEQRES 22 A 690 GLY PHE GLY SER PRO ASN LYS SER GLY LYS SER ALA SER
SEQRES 23 A 690 HIS GLY SER PRO LEU GLY VAL GLU GLU THR LYS LEU THR
SEQRES 24 A 690 LYS GLU ALA TYR ALA TRP THR ALA GLU GLN ASP PHE HIS
SEQRES 25 A 690 VAL ALA GLU GLU VAL TYR GLU ASN PHE ARG LYS THR VAL
SEQRES 26 A 690 GLN ASP VAL GLY GLU THR ALA GLN ALA GLU TRP ASN THR
SEQRES 27 A 690 MSE LEU GLY GLU TYR ALA GLN ALA TYR PRO GLU LEU ALA
SEQRES 28 A 690 ASN GLU LEU GLN ALA ALA MSE ASN GLY LEU LEU PRO GLU
SEQRES 29 A 690 GLY TRP GLU GLN ASN LEU PRO THR TYR GLU LEU GLY SER
SEQRES 30 A 690 LYS ALA ALA THR ARG ASN SER SER GLY ALA VAL ILE ASN
SEQRES 31 A 690 ALA ILE ALA GLU SER VAL PRO SER PHE PHE GLY GLY SER
SEQRES 32 A 690 ALA ASP LEU ALA GLY SER ASN LYS THR TYR MSE ASN ASN
SEQRES 33 A 690 GLU LYS ASP PHE THR ARG ASP ASP TYR SER GLY LYS ASN
SEQRES 34 A 690 ILE TRP TYR GLY VAL ARG GLU PHE ALA MSE GLY ALA ALA
SEQRES 35 A 690 MSE ASN GLY ILE ALA LEU HIS GLY GLY LEU LYS THR TYR
SEQRES 36 A 690 GLY GLY THR PHE PHE VAL PHE SER ASP TYR LEU ARG PRO
SEQRES 37 A 690 ALA ILE ARG LEU ALA ALA LEU MSE GLN LEU PRO VAL THR
SEQRES 38 A 690 TYR VAL PHE THR HIS ASP SER ILE ALA VAL GLY GLU ASP
SEQRES 39 A 690 GLY PRO THR HIS GLU PRO ILE GLU GLN LEU ALA ALA LEU
SEQRES 40 A 690 ARG ALA MSE PRO ASN VAL SER VAL ILE ARG PRO ALA ASP
SEQRES 41 A 690 GLY ASN GLU SER VAL ALA ALA TRP ARG LEU ALA LEU GLU
SEQRES 42 A 690 SER THR ASN LYS PRO THR ALA LEU VAL LEU THR ARG GLN
SEQRES 43 A 690 ASP LEU PRO THR LEU GLU GLY ALA LYS ASP ASP THR TYR
SEQRES 44 A 690 GLU LYS VAL ALA LYS GLY ALA TYR VAL VAL SER ALA SER
SEQRES 45 A 690 LYS LYS GLU THR ALA ASP VAL ILE LEU LEU ALA THR GLY
SEQRES 46 A 690 SER GLU VAL SER LEU ALA VAL GLU ALA GLN LYS ALA LEU
SEQRES 47 A 690 ALA VAL ASP GLY VAL ASP ALA SER VAL VAL SER MSE PRO
SEQRES 48 A 690 SER MSE ASP ARG PHE GLU ALA GLN THR ALA GLU TYR LYS
SEQRES 49 A 690 GLU SER VAL LEU PRO LYS ALA VAL THR LYS ARG PHE ALA
SEQRES 50 A 690 ILE GLU MSE GLY ALA THR PHE GLY TRP HIS ARG TYR VAL
SEQRES 51 A 690 GLY LEU GLU GLY ASP VAL LEU GLY ILE ASP THR PHE GLY
SEQRES 52 A 690 ALA SER ALA PRO GLY GLU LYS ILE MSE GLU GLU TYR GLY
SEQRES 53 A 690 PHE THR VAL GLU ASN VAL VAL ARG LYS VAL LYS GLU MSE
SEQRES 54 A 690 LEU
SEQRES 1 B 690 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 690 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MSE SER
SEQRES 3 B 690 HIS SER ILE GLU GLN LEU SER ILE ASN THR ILE ARG THR
SEQRES 4 B 690 LEU SER ILE ASP ALA ILE GLU LYS ALA ASN SER GLY HIS
SEQRES 5 B 690 PRO GLY MSE PRO MSE GLY ALA ALA PRO MSE ALA TYR THR
SEQRES 6 B 690 LEU TRP THR GLN PHE MSE LYS HIS ASN PRO ASN ASN PRO
SEQRES 7 B 690 THR TRP PHE ASN ARG ASP ARG PHE VAL LEU SER ALA GLY
SEQRES 8 B 690 HIS GLY SER MSE LEU LEU TYR SER LEU LEU HIS LEU SER
SEQRES 9 B 690 GLY TYR ASP VAL THR MSE ASP ASP LEU LYS ASN PHE ARG
SEQRES 10 B 690 GLN TRP GLY SER LYS THR PRO GLY HIS PRO GLU TYR GLY
SEQRES 11 B 690 HIS THR ALA GLY VAL ASP ALA THR THR GLY PRO LEU GLY
SEQRES 12 B 690 GLN GLY ILE ALA THR ALA VAL GLY MSE ALA MSE ALA GLU
SEQRES 13 B 690 ARG HIS LEU ALA ALA LYS TYR ASN ARG ASP ALA TYR ASN
SEQRES 14 B 690 ILE VAL ASP HIS TYR THR TYR ALA ILE CYS GLY ASP GLY
SEQRES 15 B 690 ASP LEU MSE GLU GLY VAL SER ALA GLU ALA SER SER LEU
SEQRES 16 B 690 ALA ALA HIS LEU GLN LEU GLY ARG LEU VAL VAL LEU TYR
SEQRES 17 B 690 ASP SER ASN ASP ILE SER LEU ASP GLY ASP LEU ASN ARG
SEQRES 18 B 690 SER PHE SER GLU SER VAL GLU ASP ARG TYR LYS ALA TYR
SEQRES 19 B 690 GLY TRP GLN VAL ILE ARG VAL GLU ASP GLY ASN ASP ILE
SEQRES 20 B 690 GLU ALA ILE ALA LYS ALA ILE GLU GLU ALA LYS ALA ASP
SEQRES 21 B 690 GLU LYS ARG PRO THR LEU ILE GLU VAL ARG THR THR ILE
SEQRES 22 B 690 GLY PHE GLY SER PRO ASN LYS SER GLY LYS SER ALA SER
SEQRES 23 B 690 HIS GLY SER PRO LEU GLY VAL GLU GLU THR LYS LEU THR
SEQRES 24 B 690 LYS GLU ALA TYR ALA TRP THR ALA GLU GLN ASP PHE HIS
SEQRES 25 B 690 VAL ALA GLU GLU VAL TYR GLU ASN PHE ARG LYS THR VAL
SEQRES 26 B 690 GLN ASP VAL GLY GLU THR ALA GLN ALA GLU TRP ASN THR
SEQRES 27 B 690 MSE LEU GLY GLU TYR ALA GLN ALA TYR PRO GLU LEU ALA
SEQRES 28 B 690 ASN GLU LEU GLN ALA ALA MSE ASN GLY LEU LEU PRO GLU
SEQRES 29 B 690 GLY TRP GLU GLN ASN LEU PRO THR TYR GLU LEU GLY SER
SEQRES 30 B 690 LYS ALA ALA THR ARG ASN SER SER GLY ALA VAL ILE ASN
SEQRES 31 B 690 ALA ILE ALA GLU SER VAL PRO SER PHE PHE GLY GLY SER
SEQRES 32 B 690 ALA ASP LEU ALA GLY SER ASN LYS THR TYR MSE ASN ASN
SEQRES 33 B 690 GLU LYS ASP PHE THR ARG ASP ASP TYR SER GLY LYS ASN
SEQRES 34 B 690 ILE TRP TYR GLY VAL ARG GLU PHE ALA MSE GLY ALA ALA
SEQRES 35 B 690 MSE ASN GLY ILE ALA LEU HIS GLY GLY LEU LYS THR TYR
SEQRES 36 B 690 GLY GLY THR PHE PHE VAL PHE SER ASP TYR LEU ARG PRO
SEQRES 37 B 690 ALA ILE ARG LEU ALA ALA LEU MSE GLN LEU PRO VAL THR
SEQRES 38 B 690 TYR VAL PHE THR HIS ASP SER ILE ALA VAL GLY GLU ASP
SEQRES 39 B 690 GLY PRO THR HIS GLU PRO ILE GLU GLN LEU ALA ALA LEU
SEQRES 40 B 690 ARG ALA MSE PRO ASN VAL SER VAL ILE ARG PRO ALA ASP
SEQRES 41 B 690 GLY ASN GLU SER VAL ALA ALA TRP ARG LEU ALA LEU GLU
SEQRES 42 B 690 SER THR ASN LYS PRO THR ALA LEU VAL LEU THR ARG GLN
SEQRES 43 B 690 ASP LEU PRO THR LEU GLU GLY ALA LYS ASP ASP THR TYR
SEQRES 44 B 690 GLU LYS VAL ALA LYS GLY ALA TYR VAL VAL SER ALA SER
SEQRES 45 B 690 LYS LYS GLU THR ALA ASP VAL ILE LEU LEU ALA THR GLY
SEQRES 46 B 690 SER GLU VAL SER LEU ALA VAL GLU ALA GLN LYS ALA LEU
SEQRES 47 B 690 ALA VAL ASP GLY VAL ASP ALA SER VAL VAL SER MSE PRO
SEQRES 48 B 690 SER MSE ASP ARG PHE GLU ALA GLN THR ALA GLU TYR LYS
SEQRES 49 B 690 GLU SER VAL LEU PRO LYS ALA VAL THR LYS ARG PHE ALA
SEQRES 50 B 690 ILE GLU MSE GLY ALA THR PHE GLY TRP HIS ARG TYR VAL
SEQRES 51 B 690 GLY LEU GLU GLY ASP VAL LEU GLY ILE ASP THR PHE GLY
SEQRES 52 B 690 ALA SER ALA PRO GLY GLU LYS ILE MSE GLU GLU TYR GLY
SEQRES 53 B 690 PHE THR VAL GLU ASN VAL VAL ARG LYS VAL LYS GLU MSE
SEQRES 54 B 690 LEU
MODRES 3M49 MSE A 31 MET SELENOMETHIONINE
MODRES 3M49 MSE A 33 MET SELENOMETHIONINE
MODRES 3M49 MSE A 38 MET SELENOMETHIONINE
MODRES 3M49 MSE A 47 MET SELENOMETHIONINE
MODRES 3M49 MSE A 71 MET SELENOMETHIONINE
MODRES 3M49 MSE A 86 MET SELENOMETHIONINE
MODRES 3M49 MSE A 128 MET SELENOMETHIONINE
MODRES 3M49 MSE A 130 MET SELENOMETHIONINE
MODRES 3M49 MSE A 161 MET SELENOMETHIONINE
MODRES 3M49 MSE A 315 MET SELENOMETHIONINE
MODRES 3M49 MSE A 334 MET SELENOMETHIONINE
MODRES 3M49 MSE A 390 MET SELENOMETHIONINE
MODRES 3M49 MSE A 415 MET SELENOMETHIONINE
MODRES 3M49 MSE A 419 MET SELENOMETHIONINE
MODRES 3M49 MSE A 452 MET SELENOMETHIONINE
MODRES 3M49 MSE A 486 MET SELENOMETHIONINE
MODRES 3M49 MSE A 586 MET SELENOMETHIONINE
MODRES 3M49 MSE A 589 MET SELENOMETHIONINE
MODRES 3M49 MSE A 616 MET SELENOMETHIONINE
MODRES 3M49 MSE A 648 MET SELENOMETHIONINE
MODRES 3M49 MSE A 665 MET SELENOMETHIONINE
MODRES 3M49 MSE B 31 MET SELENOMETHIONINE
MODRES 3M49 MSE B 33 MET SELENOMETHIONINE
MODRES 3M49 MSE B 38 MET SELENOMETHIONINE
MODRES 3M49 MSE B 47 MET SELENOMETHIONINE
MODRES 3M49 MSE B 71 MET SELENOMETHIONINE
MODRES 3M49 MSE B 86 MET SELENOMETHIONINE
MODRES 3M49 MSE B 128 MET SELENOMETHIONINE
MODRES 3M49 MSE B 130 MET SELENOMETHIONINE
MODRES 3M49 MSE B 161 MET SELENOMETHIONINE
MODRES 3M49 MSE B 315 MET SELENOMETHIONINE
MODRES 3M49 MSE B 334 MET SELENOMETHIONINE
MODRES 3M49 MSE B 390 MET SELENOMETHIONINE
MODRES 3M49 MSE B 415 MET SELENOMETHIONINE
MODRES 3M49 MSE B 419 MET SELENOMETHIONINE
MODRES 3M49 MSE B 452 MET SELENOMETHIONINE
MODRES 3M49 MSE B 486 MET SELENOMETHIONINE
MODRES 3M49 MSE B 586 MET SELENOMETHIONINE
MODRES 3M49 MSE B 589 MET SELENOMETHIONINE
MODRES 3M49 MSE B 616 MET SELENOMETHIONINE
MODRES 3M49 MSE B 648 MET SELENOMETHIONINE
MODRES 3M49 MSE B 665 MET SELENOMETHIONINE
HET MSE A 31 16
HET MSE A 33 8
HET MSE A 38 16
HET MSE A 47 8
HET MSE A 71 8
HET MSE A 86 8
HET MSE A 128 8
HET MSE A 130 8
HET MSE A 161 8
HET MSE A 315 8
HET MSE A 334 8
HET MSE A 390 8
HET MSE A 415 8
HET MSE A 419 8
HET MSE A 452 8
HET MSE A 486 8
HET MSE A 586 8
HET MSE A 589 8
HET MSE A 616 8
HET MSE A 648 8
HET MSE A 665 8
HET MSE B 31 16
HET MSE B 33 8
HET MSE B 38 8
HET MSE B 47 8
HET MSE B 71 8
HET MSE B 86 8
HET MSE B 128 8
HET MSE B 130 8
HET MSE B 161 8
HET MSE B 315 8
HET MSE B 334 8
HET MSE B 390 8
HET MSE B 415 8
HET MSE B 419 8
HET MSE B 452 8
HET MSE B 486 8
HET MSE B 586 8
HET MSE B 589 8
HET MSE B 616 8
HET MSE B 648 8
HET MSE B 665 8
HET TPP A 701 26
HET SO4 A 702 5
HET FMT A 703 3
HET GOL A 704 6
HET GOL A 705 6
HET SO4 A 706 5
HET SO4 A 707 5
HET SO4 A 708 5
HET SO4 A 709 5
HET FMT A 710 3
HET ACY A 711 4
HET PG5 A 712 12
HET PEG A 713 7
HET TRS A 714 16
HET FMT A 715 3
HET MG A 716 1
HET PEG A 717 7
HET FMT A 718 3
HET GOL A 719 6
HET GOL A 720 6
HET FMT A 721 3
HET SO4 A 722 5
HET FMT A 723 3
HET GOL A 724 6
HET TPP B 701 26
HET SO4 B 702 5
HET BTB B 703 14
HET FMT B 704 3
HET GOL B 705 6
HET FMT B 706 3
HET FMT B 707 3
HET SO4 B 708 5
HET FMT B 709 3
HET GOL B 710 6
HET FMT B 711 3
HET GOL B 712 6
HET FMT B 713 3
HET SO4 B 714 5
HETNAM MSE SELENOMETHIONINE
HETNAM TPP THIAMINE DIPHOSPHATE
HETNAM SO4 SULFATE ION
HETNAM FMT FORMIC ACID
HETNAM GOL GLYCEROL
HETNAM ACY ACETIC ACID
HETNAM PG5 1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM MG MAGNESIUM ION
HETNAM BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-
HETNAM 2 BTB PROPANE-1,3-DIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN TRS TRIS BUFFER
HETSYN BTB BIS-TRIS BUFFER
FORMUL 1 MSE 42(C5 H11 N O2 SE)
FORMUL 3 TPP 2(C12 H19 N4 O7 P2 S 1+)
FORMUL 4 SO4 9(O4 S 2-)
FORMUL 5 FMT 12(C H2 O2)
FORMUL 6 GOL 8(C3 H8 O3)
FORMUL 13 ACY C2 H4 O2
FORMUL 14 PG5 C8 H18 O4
FORMUL 15 PEG 2(C4 H10 O3)
FORMUL 16 TRS C4 H12 N O3 1+
FORMUL 18 MG MG 2+
FORMUL 29 BTB C8 H19 N O5
FORMUL 41 HOH *1130(H2 O)
HELIX 1 1 SER A 4 ASN A 25 1 22
HELIX 2 2 PRO A 29 PHE A 46 1 18
HELIX 3 3 ALA A 66 HIS A 68 5 3
HELIX 4 4 GLY A 69 SER A 80 1 12
HELIX 5 5 THR A 85 LYS A 90 1 6
HELIX 6 6 GLY A 119 ASN A 140 1 22
HELIX 7 7 GLY A 156 GLU A 162 1 7
HELIX 8 8 GLU A 162 LEU A 175 1 14
HELIX 9 9 ASP A 194 SER A 198 5 5
HELIX 10 10 SER A 202 GLY A 211 1 10
HELIX 11 11 ASP A 222 ASP A 236 1 15
HELIX 12 12 LYS A 259 HIS A 263 5 5
HELIX 13 13 GLY A 268 TYR A 279 1 12
HELIX 14 14 ALA A 290 VAL A 301 1 12
HELIX 15 15 VAL A 301 TYR A 323 1 23
HELIX 16 16 TYR A 323 ASN A 335 1 13
HELIX 17 17 GLY A 341 LEU A 346 5 6
HELIX 18 18 THR A 357 VAL A 372 1 16
HELIX 19 19 LEU A 382 LYS A 387 1 6
HELIX 20 20 ARG A 411 GLY A 426 1 16
HELIX 21 21 VAL A 437 TYR A 441 5 5
HELIX 22 22 LEU A 442 GLN A 453 1 12
HELIX 23 23 SER A 464 GLY A 468 5 5
HELIX 24 24 GLY A 471 GLU A 475 5 5
HELIX 25 25 GLU A 478 ALA A 485 1 8
HELIX 26 26 ASP A 496 SER A 510 1 15
HELIX 27 27 LEU A 527 ASP A 532 1 6
HELIX 28 28 ASP A 533 LYS A 540 1 8
HELIX 29 29 SER A 562 ASP A 577 1 16
HELIX 30 30 SER A 588 ALA A 594 1 7
HELIX 31 31 THR A 596 LEU A 604 1 9
HELIX 32 32 TRP A 622 GLY A 627 1 6
HELIX 33 33 PRO A 643 TYR A 651 1 9
HELIX 34 34 THR A 654 LEU A 666 1 13
HELIX 35 35 SER B 4 ASN B 25 1 22
HELIX 36 36 PRO B 29 PHE B 46 1 18
HELIX 37 37 ALA B 66 HIS B 68 5 3
HELIX 38 38 GLY B 69 GLY B 81 1 13
HELIX 39 39 THR B 85 LYS B 90 1 6
HELIX 40 40 GLY B 119 ASN B 140 1 22
HELIX 41 41 GLY B 156 GLU B 162 1 7
HELIX 42 42 GLU B 162 LEU B 175 1 14
HELIX 43 43 ASN B 196 SER B 198 5 3
HELIX 44 44 SER B 202 GLY B 211 1 10
HELIX 45 45 ASP B 222 ASP B 236 1 15
HELIX 46 46 LYS B 259 HIS B 263 5 5
HELIX 47 47 GLY B 268 TYR B 279 1 12
HELIX 48 48 ALA B 290 VAL B 301 1 12
HELIX 49 49 VAL B 301 TYR B 323 1 23
HELIX 50 50 TYR B 323 ASN B 335 1 13
HELIX 51 51 GLY B 341 LEU B 346 5 6
HELIX 52 52 THR B 357 VAL B 372 1 16
HELIX 53 53 LEU B 382 LYS B 387 1 6
HELIX 54 54 ARG B 411 GLY B 426 1 16
HELIX 55 55 VAL B 437 TYR B 441 5 5
HELIX 56 56 LEU B 442 GLN B 453 1 12
HELIX 57 57 SER B 464 GLY B 468 5 5
HELIX 58 58 GLY B 471 GLU B 475 5 5
HELIX 59 59 GLU B 478 ALA B 485 1 8
HELIX 60 60 ASP B 496 SER B 510 1 15
HELIX 61 61 LEU B 527 LYS B 531 5 5
HELIX 62 62 ASP B 533 LYS B 540 1 8
HELIX 63 63 SER B 562 ASP B 577 1 16
HELIX 64 64 SER B 588 ALA B 594 1 7
HELIX 65 65 THR B 596 LEU B 604 1 9
HELIX 66 66 TRP B 622 GLY B 627 1 6
HELIX 67 67 PRO B 643 TYR B 651 1 9
HELIX 68 68 THR B 654 LEU B 666 1 13
SHEET 1 A 5 ARG A 61 LEU A 64 0
SHEET 2 A 5 THR A 151 CYS A 155 1 O TYR A 152 N ARG A 61
SHEET 3 A 5 LEU A 180 SER A 186 1 O LEU A 183 N ALA A 153
SHEET 4 A 5 THR A 241 ARG A 246 1 O ILE A 243 N VAL A 182
SHEET 5 A 5 GLN A 213 VAL A 217 1 N VAL A 217 O GLU A 244
SHEET 1 B 2 LYS A 354 ALA A 356 0
SHEET 2 B 2 ASP A 523 PRO A 525 -1 O LEU A 524 N ALA A 355
SHEET 1 C 6 ASN A 405 TRP A 407 0
SHEET 2 C 6 PHE A 375 SER A 379 1 N GLY A 377 O ILE A 406
SHEET 3 C 6 LYS A 429 PHE A 435 1 O LYS A 429 N PHE A 376
SHEET 4 C 6 THR A 457 THR A 461 1 O VAL A 459 N GLY A 432
SHEET 5 C 6 THR A 515 VAL A 518 1 O LEU A 517 N TYR A 458
SHEET 6 C 6 SER A 490 ILE A 492 1 N SER A 490 O ALA A 516
SHEET 1 D 5 TYR A 543 SER A 546 0
SHEET 2 D 5 ALA A 581 SER A 585 -1 O VAL A 583 N SER A 546
SHEET 3 D 5 VAL A 555 ALA A 559 1 N LEU A 557 O SER A 582
SHEET 4 D 5 ARG A 611 ILE A 614 1 O PHE A 612 N LEU A 558
SHEET 5 D 5 ASP A 631 LEU A 633 1 O LEU A 633 N ALA A 613
SHEET 1 E 5 ARG B 61 LEU B 64 0
SHEET 2 E 5 THR B 151 CYS B 155 1 O TYR B 152 N ARG B 61
SHEET 3 E 5 LEU B 180 SER B 186 1 O LEU B 183 N ALA B 153
SHEET 4 E 5 THR B 241 ARG B 246 1 O THR B 241 N VAL B 182
SHEET 5 E 5 GLN B 213 VAL B 217 1 N VAL B 217 O GLU B 244
SHEET 1 F 2 ILE B 189 SER B 190 0
SHEET 2 F 2 GLY B 193 ASP B 194 -1 O GLY B 193 N SER B 190
SHEET 1 G 2 LYS B 354 ALA B 356 0
SHEET 2 G 2 ASP B 523 PRO B 525 -1 O LEU B 524 N ALA B 355
SHEET 1 H 6 ASN B 405 TRP B 407 0
SHEET 2 H 6 PHE B 375 SER B 379 1 N GLY B 377 O ILE B 406
SHEET 3 H 6 LYS B 429 PHE B 435 1 O GLY B 433 N GLY B 378
SHEET 4 H 6 THR B 457 THR B 461 1 O VAL B 459 N GLY B 432
SHEET 5 H 6 THR B 515 VAL B 518 1 O LEU B 517 N TYR B 458
SHEET 6 H 6 SER B 490 ILE B 492 1 N SER B 490 O ALA B 516
SHEET 1 I 5 TYR B 543 SER B 546 0
SHEET 2 I 5 ALA B 581 SER B 585 -1 O VAL B 583 N SER B 546
SHEET 3 I 5 VAL B 555 ALA B 559 1 N LEU B 557 O SER B 582
SHEET 4 I 5 ARG B 611 ILE B 614 1 O PHE B 612 N ILE B 556
SHEET 5 I 5 ASP B 631 LEU B 633 1 O LEU B 633 N ALA B 613
LINK C GLY A 30 N AMSE A 31 1555 1555 1.33
LINK C GLY A 30 N BMSE A 31 1555 1555 1.33
LINK C AMSE A 31 N PRO A 32 1555 1555 1.34
LINK C BMSE A 31 N PRO A 32 1555 1555 1.34
LINK C PRO A 32 N MSE A 33 1555 1555 1.32
LINK C MSE A 33 N GLY A 34 1555 1555 1.33
LINK C PRO A 37 N AMSE A 38 1555 1555 1.33
LINK C PRO A 37 N BMSE A 38 1555 1555 1.33
LINK C AMSE A 38 N ALA A 39 1555 1555 1.33
LINK C BMSE A 38 N ALA A 39 1555 1555 1.33
LINK C PHE A 46 N MSE A 47 1555 1555 1.33
LINK C MSE A 47 N LYS A 48 1555 1555 1.32
LINK C SER A 70 N MSE A 71 1555 1555 1.33
LINK C MSE A 71 N LEU A 72 1555 1555 1.33
LINK C THR A 85 N MSE A 86 1555 1555 1.33
LINK C MSE A 86 N AASP A 87 1555 1555 1.33
LINK C MSE A 86 N BASP A 87 1555 1555 1.33
LINK C GLY A 127 N MSE A 128 1555 1555 1.33
LINK C MSE A 128 N ALA A 129 1555 1555 1.34
LINK C ALA A 129 N MSE A 130 1555 1555 1.33
LINK C MSE A 130 N ALA A 131 1555 1555 1.33
LINK C LEU A 160 N MSE A 161 1555 1555 1.33
LINK C MSE A 161 N GLU A 162 1555 1555 1.34
LINK C THR A 314 N MSE A 315 1555 1555 1.32
LINK C MSE A 315 N LEU A 316 1555 1555 1.33
LINK C ALA A 333 N MSE A 334 1555 1555 1.34
LINK C MSE A 334 N ASN A 335 1555 1555 1.33
LINK C TYR A 389 N MSE A 390 1555 1555 1.33
LINK C MSE A 390 N ASN A 391 1555 1555 1.33
LINK C ALA A 414 N MSE A 415 1555 1555 1.33
LINK C MSE A 415 N GLY A 416 1555 1555 1.33
LINK C ALA A 418 N MSE A 419 1555 1555 1.33
LINK C MSE A 419 N ASN A 420 1555 1555 1.33
LINK C LEU A 451 N MSE A 452 1555 1555 1.33
LINK C MSE A 452 N GLN A 453 1555 1555 1.33
LINK C ALA A 485 N MSE A 486 1555 1555 1.33
LINK C MSE A 486 N PRO A 487 1555 1555 1.35
LINK C SER A 585 N MSE A 586 1555 1555 1.34
LINK C MSE A 586 N PRO A 587 1555 1555 1.33
LINK C SER A 588 N MSE A 589 1555 1555 1.34
LINK C MSE A 589 N ASP A 590 1555 1555 1.33
LINK C GLU A 615 N MSE A 616 1555 1555 1.33
LINK C MSE A 616 N GLY A 617 1555 1555 1.33
LINK C ILE A 647 N MSE A 648 1555 1555 1.33
LINK C MSE A 648 N GLU A 649 1555 1555 1.33
LINK C GLU A 664 N MSE A 665 1555 1555 1.32
LINK C MSE A 665 N LEU A 666 1555 1555 1.33
LINK C GLY B 30 N AMSE B 31 1555 1555 1.32
LINK C GLY B 30 N BMSE B 31 1555 1555 1.33
LINK C AMSE B 31 N PRO B 32 1555 1555 1.34
LINK C BMSE B 31 N PRO B 32 1555 1555 1.34
LINK C PRO B 32 N MSE B 33 1555 1555 1.33
LINK C MSE B 33 N GLY B 34 1555 1555 1.33
LINK C PRO B 37 N MSE B 38 1555 1555 1.33
LINK C MSE B 38 N ALA B 39 1555 1555 1.33
LINK C PHE B 46 N MSE B 47 1555 1555 1.33
LINK C MSE B 47 N LYS B 48 1555 1555 1.33
LINK C SER B 70 N MSE B 71 1555 1555 1.34
LINK C MSE B 71 N LEU B 72 1555 1555 1.32
LINK C THR B 85 N MSE B 86 1555 1555 1.33
LINK C MSE B 86 N AASP B 87 1555 1555 1.33
LINK C MSE B 86 N BASP B 87 1555 1555 1.33
LINK C GLY B 127 N MSE B 128 1555 1555 1.33
LINK C MSE B 128 N ALA B 129 1555 1555 1.34
LINK C ALA B 129 N MSE B 130 1555 1555 1.33
LINK C MSE B 130 N ALA B 131 1555 1555 1.33
LINK C LEU B 160 N MSE B 161 1555 1555 1.33
LINK C MSE B 161 N GLU B 162 1555 1555 1.34
LINK C THR B 314 N MSE B 315 1555 1555 1.33
LINK C MSE B 315 N LEU B 316 1555 1555 1.33
LINK C ALA B 333 N MSE B 334 1555 1555 1.33
LINK C MSE B 334 N ASN B 335 1555 1555 1.33
LINK C TYR B 389 N MSE B 390 1555 1555 1.33
LINK C MSE B 390 N ASN B 391 1555 1555 1.33
LINK C ALA B 414 N MSE B 415 1555 1555 1.32
LINK C MSE B 415 N GLY B 416 1555 1555 1.33
LINK C ALA B 418 N MSE B 419 1555 1555 1.33
LINK C MSE B 419 N ASN B 420 1555 1555 1.33
LINK C LEU B 451 N MSE B 452 1555 1555 1.33
LINK C MSE B 452 N GLN B 453 1555 1555 1.33
LINK C ALA B 485 N MSE B 486 1555 1555 1.33
LINK C MSE B 486 N PRO B 487 1555 1555 1.35
LINK C SER B 585 N MSE B 586 1555 1555 1.33
LINK C MSE B 586 N PRO B 587 1555 1555 1.34
LINK C SER B 588 N MSE B 589 1555 1555 1.34
LINK C MSE B 589 N ASP B 590 1555 1555 1.33
LINK C GLU B 615 N MSE B 616 1555 1555 1.33
LINK C MSE B 616 N GLY B 617 1555 1555 1.33
LINK C ILE B 647 N MSE B 648 1555 1555 1.33
LINK C MSE B 648 N AGLU B 649 1555 1555 1.33
LINK C MSE B 648 N BGLU B 649 1555 1555 1.33
LINK C GLU B 664 N MSE B 665 1555 1555 1.33
LINK C MSE B 665 N LEU B 666 1555 1555 1.32
LINK OD2 ASP A 157 MG MG A 716 1555 1555 2.38
LINK OD1 ASN A 187 MG MG A 716 1555 1555 2.34
LINK O ILE A 189 MG MG A 716 1555 1555 2.32
LINK O2B TPP A 701 MG MG A 716 1555 1555 2.42
LINK O2A TPP A 701 MG MG A 716 1555 1555 2.47
LINK MG MG A 716 O HOH A1038 1555 1555 2.43
SITE 1 AC1 21 HIS A 68 GLY A 116 LEU A 118 ASP A 157
SITE 2 AC1 21 GLY A 158 GLU A 162 ASN A 187 ILE A 189
SITE 3 AC1 21 LEU A 191 ILE A 249 HIS A 263 MG A 716
SITE 4 AC1 21 GOL A 719 HOH A 946 HOH A 953 HOH A1039
SITE 5 AC1 21 ASP B 381 GLU B 412 PHE B 438 TYR B 441
SITE 6 AC1 21 HIS B 474
SITE 1 AC2 8 HIS A 474 HOH A1061 HOH A1062 HIS B 28
SITE 2 AC2 8 HIS B 68 HIS B 102 GLY B 116 TPP B 701
SITE 1 AC3 1 GLY A 96
SITE 1 AC4 9 SER A 2 LEU A 8 ASN A 11 TYR A 279
SITE 2 AC4 9 ALA A 280 TRP A 281 SO4 A 709 GOL A 720
SITE 3 AC4 9 HOH A1135
SITE 1 AC5 5 ASN A 345 PRO A 347 THR B 348 GLU B 350
SITE 2 AC5 5 LYS B 531
SITE 1 AC6 5 ARG A 358 SER A 385 HIS A 462 ARG A 521
SITE 2 AC6 5 HOH A1056
SITE 1 AC7 3 ARG A 591 HOH A 792 HOH A 996
SITE 1 AC8 3 ARG A 239 HOH A 849 ARG B 298
SITE 1 AC9 4 GLN A 7 ASN A 11 TYR A 279 GOL A 704
SITE 1 BC1 2 TYR A 535 GLU A 536
SITE 1 BC2 2 ARG A 660 LYS A 661
SITE 1 BC3 5 TYR A 105 GLY A 106 MSE A 452 PEG A 713
SITE 2 BC3 5 HOH A 911
SITE 1 BC4 6 TYR A 105 GLN A 453 THR A 511 PG5 A 712
SITE 2 BC4 6 HOH A 999 HOH A1227
SITE 1 BC5 3 GLU A 291 TYR A 294 ARG A 298
SITE 1 BC6 5 VAL A 544 SER A 582 SER A 602 VAL A 603
SITE 2 BC6 5 HOH A1104
SITE 1 BC7 5 ASP A 157 ASN A 187 ILE A 189 TPP A 701
SITE 2 BC7 5 HOH A1038
SITE 1 BC8 7 GLU A 218 ASP A 219 ASN A 221 ARG A 246
SITE 2 BC8 7 THR A 248 FMT A 721 HOH A 981
SITE 1 BC9 2 HIS A 3 GLU A 292
SITE 1 CC1 9 HIS A 28 LEU A 191 HIS A 263 TPP A 701
SITE 2 CC1 9 HOH A 930 HOH A 983 ASP B 470 HIS B 474
SITE 3 CC1 9 HOH B1197
SITE 1 CC2 7 LEU A 8 ALA A 280 TRP A 281 THR A 282
SITE 2 CC2 7 ALA A 283 GOL A 704 HOH A1100
SITE 1 CC3 5 GLY A 34 ASN A 221 THR A 247 THR A 248
SITE 2 CC3 5 PEG A 717
SITE 1 CC4 6 ASN A 488 VAL A 489 HOH A 833 HOH A 835
SITE 2 CC4 6 HOH A 924 HOH A1224
SITE 1 CC5 3 ARG A 505 HOH A 969 HOH A1080
SITE 1 CC6 7 LYS A 23 LYS A 90 GLN A 94 HOH A 725
SITE 2 CC6 7 HOH A 826 HOH A 844 HOH A1047
SITE 1 CC7 23 ASP A 381 LEU A 382 GLU A 412 PHE A 438
SITE 2 CC7 23 TYR A 441 HIS A 474 SO4 A 702 MSE B 31
SITE 3 CC7 23 HIS B 68 GLY B 116 LEU B 118 ASP B 157
SITE 4 CC7 23 GLY B 158 GLU B 162 ASN B 187 ILE B 189
SITE 5 CC7 23 LEU B 191 ILE B 249 HIS B 263 HOH B 953
SITE 6 CC7 23 HOH B 954 HOH B 979 HOH B1060
SITE 1 CC8 7 ASN B 488 VAL B 489 LYS B 513 ASP B 590
SITE 2 CC8 7 HOH B1047 HOH B1125 HOH B1178
SITE 1 CC9 10 THR A 348 GLU A 350 LYS A 531 HOH A1171
SITE 2 CC9 10 ASN B 345 PRO B 347 ALA B 367 GLU B 370
SITE 3 CC9 10 HOH B 873 HOH B1024
SITE 1 DC1 5 SER A 26 GLU B 469 ARG B 521 HOH B 812
SITE 2 DC1 5 HOH B1197
SITE 1 DC2 4 ARG B 505 TYR B 535 HOH B 811 HOH B 876
SITE 1 DC3 3 TYR B 535 GLU B 536 HOH B1028
SITE 1 DC4 5 ARG B 358 SER B 385 HIS B 462 ARG B 521
SITE 2 DC4 5 HOH B 999
SITE 1 DC5 4 THR B 85 MSE B 86 GOL B 710 HOH B1152
SITE 1 DC6 3 GLU B 291 TYR B 294 FMT B 709
SITE 1 DC7 5 THR B 55 PHE B 57 ARG B 59 HIS B 425
SITE 2 DC7 5 HOH B1158
SITE 1 DC8 3 ALA B 383 GLY B 384 HOH B1053
SITE 1 DC9 3 ALA B 280 TRP B 281 THR B 282
SITE 1 EC1 4 ARG B 591 HOH B 840 HOH B1015 HOH B1028
CRYST1 83.333 132.087 137.319 90.00 90.00 90.00 P 21 21 21 8
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 0.012000 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007571 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007282 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
