HEADER HYDROLASE 17-JUN-10 3NJ4
TITLE FLUORO-NEPLANOCIN A IN HUMAN S-ADENOSYLHOMOCYSTEINE HYDROLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSYLHOMOCYSTEINASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ADOHCYASE, S-ADENOSYL-L-HOMOCYSTEINE HYDROLASE;
COMPND 5 EC: 3.3.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: AHCY, SAHH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS S-ADENOSYLHOMOCYSTEIN, HYDROLASE, NAD
EXPDTA X-RAY DIFFRACTION
AUTHOR L.S.JEONG,K.M.LEE,K.Y.HWANG,S.CHOI,Y.S.HEO
REVDAT 2 20-MAR-24 3NJ4 1 REMARK SEQADV
REVDAT 1 04-MAY-11 3NJ4 0
JRNL AUTH K.M.LEE,W.J.CHOI,Y.LEE,H.J.LEE,L.X.ZHAO,H.W.LEE,J.G.PARK,
JRNL AUTH 2 H.O.KIM,K.Y.HWANG,Y.S.HEO,S.CHOI,L.S.JEONG
JRNL TITL X-RAY CRYSTAL STRUCTURE AND BINDING MODE ANALYSIS OF HUMAN
JRNL TITL 2 S-ADENOSYLHOMOCYSTEINE HYDROLASE COMPLEXED WITH NOVEL
JRNL TITL 3 MECHANISM-BASED INHIBITORS, HALONEPLANOCIN A ANALOGUES.
JRNL REF J.MED.CHEM. V. 54 930 2011
JRNL REFN ISSN 0022-2623
JRNL PMID 21226494
JRNL DOI 10.1021/JM1010836
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.61
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 766342.260
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.1
REMARK 3 NUMBER OF REFLECTIONS : 55307
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3954
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7461
REMARK 3 BIN R VALUE (WORKING SET) : 0.3010
REMARK 3 BIN FREE R VALUE : 0.3550
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 592
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13332
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 256
REMARK 3 SOLVENT ATOMS : 258
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.39000
REMARK 3 B22 (A**2) : -0.98000
REMARK 3 B33 (A**2) : 2.37000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 5.99000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.37
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.47
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.800
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.200 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.940 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.720 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.500 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 40.31
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ADC.PARAM
REMARK 3 PARAMETER FILE 4 : NAH.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ADC.TOP
REMARK 3 TOPOLOGY FILE 4 : NAH.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3NJ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059893.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 6B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55307
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.1
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) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.6
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 8.0, 22% PEG400, 100MM
REMARK 280 LITHIUM SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 40.96950
REMARK 290 SMTRY3 2 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 20820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 54900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -112.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 SER D 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 O THR A 276 OE2 GLU A 305 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 LYS A 4 106.54 -50.81
REMARK 500 TYR A 7 167.99 178.18
REMARK 500 ASP A 11 97.27 -165.82
REMARK 500 HIS A 55 102.04 -25.65
REMARK 500 MET A 56 91.71 -69.34
REMARK 500 PRO A 98 102.52 -54.86
REMARK 500 ALA A 101 146.73 -171.75
REMARK 500 THR A 185 -2.04 -57.69
REMARK 500 LYS A 186 -72.12 -109.69
REMARK 500 PHE A 189 -52.69 -138.70
REMARK 500 LEU A 192 -77.64 -74.80
REMARK 500 THR A 260 -165.21 -128.70
REMARK 500 ASN A 314 -24.31 -151.43
REMARK 500 PRO A 323 132.03 -39.44
REMARK 500 ALA A 350 -148.85 -161.29
REMARK 500 PRO A 380 -167.43 -64.64
REMARK 500 CYS A 421 7.02 -69.26
REMARK 500 ASP A 422 -39.14 -134.79
REMARK 500 TYR B 7 -178.42 174.26
REMARK 500 LYS B 8 110.24 -171.56
REMARK 500 ASP B 11 111.25 -163.60
REMARK 500 HIS B 55 106.07 -22.44
REMARK 500 ASP B 122 50.35 -149.04
REMARK 500 GLU B 155 -175.99 -67.99
REMARK 500 GLU B 156 -43.60 -141.15
REMARK 500 THR B 185 9.21 -59.83
REMARK 500 LYS B 186 -76.99 -119.74
REMARK 500 PHE B 189 -53.89 -128.86
REMARK 500 LEU B 192 -76.32 -76.35
REMARK 500 TYR B 221 59.09 -142.11
REMARK 500 THR B 260 -164.45 -129.69
REMARK 500 PRO B 323 127.58 -37.98
REMARK 500 LEU B 344 106.26 -47.47
REMARK 500 ALA B 350 -138.32 -148.09
REMARK 500 TYR C 7 -174.91 -170.61
REMARK 500 LYS C 8 93.90 -170.27
REMARK 500 ASP C 11 104.48 -163.40
REMARK 500 ASN C 27 20.55 -73.13
REMARK 500 MET C 29 70.08 -112.18
REMARK 500 HIS C 55 113.87 -38.97
REMARK 500 PRO C 98 99.73 -59.89
REMARK 500 THR C 185 10.38 -66.89
REMARK 500 LYS C 186 -75.79 -121.08
REMARK 500 PHE C 189 -62.17 -132.61
REMARK 500 LEU C 192 -82.31 -81.33
REMARK 500 ASP C 280 75.11 47.59
REMARK 500 MET C 290 169.05 -48.25
REMARK 500 ASP C 307 81.90 -69.58
REMARK 500 ASN C 314 -30.58 -151.02
REMARK 500 ASN C 332 4.41 -68.53
REMARK 500
REMARK 500 THIS ENTRY HAS 68 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AFX A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AFX B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AFX C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AFX D 604
DBREF 3NJ4 A 1 432 UNP P23526 SAHH_HUMAN 1 432
DBREF 3NJ4 B 1 432 UNP P23526 SAHH_HUMAN 1 432
DBREF 3NJ4 C 1 432 UNP P23526 SAHH_HUMAN 1 432
DBREF 3NJ4 D 1 432 UNP P23526 SAHH_HUMAN 1 432
SEQADV 3NJ4 GLY A -2 UNP P23526 EXPRESSION TAG
SEQADV 3NJ4 SER A -1 UNP P23526 EXPRESSION TAG
SEQADV 3NJ4 HIS A 0 UNP P23526 EXPRESSION TAG
SEQADV 3NJ4 GLY B -2 UNP P23526 EXPRESSION TAG
SEQADV 3NJ4 SER B -1 UNP P23526 EXPRESSION TAG
SEQADV 3NJ4 HIS B 0 UNP P23526 EXPRESSION TAG
SEQADV 3NJ4 GLY C -2 UNP P23526 EXPRESSION TAG
SEQADV 3NJ4 SER C -1 UNP P23526 EXPRESSION TAG
SEQADV 3NJ4 HIS C 0 UNP P23526 EXPRESSION TAG
SEQADV 3NJ4 GLY D -2 UNP P23526 EXPRESSION TAG
SEQADV 3NJ4 SER D -1 UNP P23526 EXPRESSION TAG
SEQADV 3NJ4 HIS D 0 UNP P23526 EXPRESSION TAG
SEQRES 1 A 435 GLY SER HIS MET SER ASP LYS LEU PRO TYR LYS VAL ALA
SEQRES 2 A 435 ASP ILE GLY LEU ALA ALA TRP GLY ARG LYS ALA LEU ASP
SEQRES 3 A 435 ILE ALA GLU ASN GLU MET PRO GLY LEU MET ARG MET ARG
SEQRES 4 A 435 GLU ARG TYR SER ALA SER LYS PRO LEU LYS GLY ALA ARG
SEQRES 5 A 435 ILE ALA GLY CYS LEU HIS MET THR VAL GLU THR ALA VAL
SEQRES 6 A 435 LEU ILE GLU THR LEU VAL THR LEU GLY ALA GLU VAL GLN
SEQRES 7 A 435 TRP SER SER CYS ASN ILE PHE SER THR GLN ASP HIS ALA
SEQRES 8 A 435 ALA ALA ALA ILE ALA LYS ALA GLY ILE PRO VAL TYR ALA
SEQRES 9 A 435 TRP LYS GLY GLU THR ASP GLU GLU TYR LEU TRP CYS ILE
SEQRES 10 A 435 GLU GLN THR LEU TYR PHE LYS ASP GLY PRO LEU ASN MET
SEQRES 11 A 435 ILE LEU ASP ASP GLY GLY ASP LEU THR ASN LEU ILE HIS
SEQRES 12 A 435 THR LYS TYR PRO GLN LEU LEU PRO GLY ILE ARG GLY ILE
SEQRES 13 A 435 SER GLU GLU THR THR THR GLY VAL HIS ASN LEU TYR LYS
SEQRES 14 A 435 MET MET ALA ASN GLY ILE LEU LYS VAL PRO ALA ILE ASN
SEQRES 15 A 435 VAL ASN ASP SER VAL THR LYS SER LYS PHE ASP ASN LEU
SEQRES 16 A 435 TYR GLY CYS ARG GLU SER LEU ILE ASP GLY ILE LYS ARG
SEQRES 17 A 435 ALA THR ASP VAL MET ILE ALA GLY LYS VAL ALA VAL VAL
SEQRES 18 A 435 ALA GLY TYR GLY ASP VAL GLY LYS GLY CYS ALA GLN ALA
SEQRES 19 A 435 LEU ARG GLY PHE GLY ALA ARG VAL ILE ILE THR GLU ILE
SEQRES 20 A 435 ASP PRO ILE ASN ALA LEU GLN ALA ALA MET GLU GLY TYR
SEQRES 21 A 435 GLU VAL THR THR MET ASP GLU ALA CYS GLN GLU GLY ASN
SEQRES 22 A 435 ILE PHE VAL THR THR THR GLY CYS ILE ASP ILE ILE LEU
SEQRES 23 A 435 GLY ARG HIS PHE GLU GLN MET LYS ASP ASP ALA ILE VAL
SEQRES 24 A 435 CYS ASN ILE GLY HIS PHE ASP VAL GLU ILE ASP VAL LYS
SEQRES 25 A 435 TRP LEU ASN GLU ASN ALA VAL GLU LYS VAL ASN ILE LYS
SEQRES 26 A 435 PRO GLN VAL ASP ARG TYR ARG LEU LYS ASN GLY ARG ARG
SEQRES 27 A 435 ILE ILE LEU LEU ALA GLU GLY ARG LEU VAL ASN LEU GLY
SEQRES 28 A 435 CYS ALA MET GLY HIS PRO SER PHE VAL MET SER ASN SER
SEQRES 29 A 435 PHE THR ASN GLN VAL MET ALA GLN ILE GLU LEU TRP THR
SEQRES 30 A 435 HIS PRO ASP LYS TYR PRO VAL GLY VAL HIS PHE LEU PRO
SEQRES 31 A 435 LYS LYS LEU ASP GLU ALA VAL ALA GLU ALA HIS LEU GLY
SEQRES 32 A 435 LYS LEU ASN VAL LYS LEU THR LYS LEU THR GLU LYS GLN
SEQRES 33 A 435 ALA GLN TYR LEU GLY MET SER CYS ASP GLY PRO PHE LYS
SEQRES 34 A 435 PRO ASP HIS TYR ARG TYR
SEQRES 1 B 435 GLY SER HIS MET SER ASP LYS LEU PRO TYR LYS VAL ALA
SEQRES 2 B 435 ASP ILE GLY LEU ALA ALA TRP GLY ARG LYS ALA LEU ASP
SEQRES 3 B 435 ILE ALA GLU ASN GLU MET PRO GLY LEU MET ARG MET ARG
SEQRES 4 B 435 GLU ARG TYR SER ALA SER LYS PRO LEU LYS GLY ALA ARG
SEQRES 5 B 435 ILE ALA GLY CYS LEU HIS MET THR VAL GLU THR ALA VAL
SEQRES 6 B 435 LEU ILE GLU THR LEU VAL THR LEU GLY ALA GLU VAL GLN
SEQRES 7 B 435 TRP SER SER CYS ASN ILE PHE SER THR GLN ASP HIS ALA
SEQRES 8 B 435 ALA ALA ALA ILE ALA LYS ALA GLY ILE PRO VAL TYR ALA
SEQRES 9 B 435 TRP LYS GLY GLU THR ASP GLU GLU TYR LEU TRP CYS ILE
SEQRES 10 B 435 GLU GLN THR LEU TYR PHE LYS ASP GLY PRO LEU ASN MET
SEQRES 11 B 435 ILE LEU ASP ASP GLY GLY ASP LEU THR ASN LEU ILE HIS
SEQRES 12 B 435 THR LYS TYR PRO GLN LEU LEU PRO GLY ILE ARG GLY ILE
SEQRES 13 B 435 SER GLU GLU THR THR THR GLY VAL HIS ASN LEU TYR LYS
SEQRES 14 B 435 MET MET ALA ASN GLY ILE LEU LYS VAL PRO ALA ILE ASN
SEQRES 15 B 435 VAL ASN ASP SER VAL THR LYS SER LYS PHE ASP ASN LEU
SEQRES 16 B 435 TYR GLY CYS ARG GLU SER LEU ILE ASP GLY ILE LYS ARG
SEQRES 17 B 435 ALA THR ASP VAL MET ILE ALA GLY LYS VAL ALA VAL VAL
SEQRES 18 B 435 ALA GLY TYR GLY ASP VAL GLY LYS GLY CYS ALA GLN ALA
SEQRES 19 B 435 LEU ARG GLY PHE GLY ALA ARG VAL ILE ILE THR GLU ILE
SEQRES 20 B 435 ASP PRO ILE ASN ALA LEU GLN ALA ALA MET GLU GLY TYR
SEQRES 21 B 435 GLU VAL THR THR MET ASP GLU ALA CYS GLN GLU GLY ASN
SEQRES 22 B 435 ILE PHE VAL THR THR THR GLY CYS ILE ASP ILE ILE LEU
SEQRES 23 B 435 GLY ARG HIS PHE GLU GLN MET LYS ASP ASP ALA ILE VAL
SEQRES 24 B 435 CYS ASN ILE GLY HIS PHE ASP VAL GLU ILE ASP VAL LYS
SEQRES 25 B 435 TRP LEU ASN GLU ASN ALA VAL GLU LYS VAL ASN ILE LYS
SEQRES 26 B 435 PRO GLN VAL ASP ARG TYR ARG LEU LYS ASN GLY ARG ARG
SEQRES 27 B 435 ILE ILE LEU LEU ALA GLU GLY ARG LEU VAL ASN LEU GLY
SEQRES 28 B 435 CYS ALA MET GLY HIS PRO SER PHE VAL MET SER ASN SER
SEQRES 29 B 435 PHE THR ASN GLN VAL MET ALA GLN ILE GLU LEU TRP THR
SEQRES 30 B 435 HIS PRO ASP LYS TYR PRO VAL GLY VAL HIS PHE LEU PRO
SEQRES 31 B 435 LYS LYS LEU ASP GLU ALA VAL ALA GLU ALA HIS LEU GLY
SEQRES 32 B 435 LYS LEU ASN VAL LYS LEU THR LYS LEU THR GLU LYS GLN
SEQRES 33 B 435 ALA GLN TYR LEU GLY MET SER CYS ASP GLY PRO PHE LYS
SEQRES 34 B 435 PRO ASP HIS TYR ARG TYR
SEQRES 1 C 435 GLY SER HIS MET SER ASP LYS LEU PRO TYR LYS VAL ALA
SEQRES 2 C 435 ASP ILE GLY LEU ALA ALA TRP GLY ARG LYS ALA LEU ASP
SEQRES 3 C 435 ILE ALA GLU ASN GLU MET PRO GLY LEU MET ARG MET ARG
SEQRES 4 C 435 GLU ARG TYR SER ALA SER LYS PRO LEU LYS GLY ALA ARG
SEQRES 5 C 435 ILE ALA GLY CYS LEU HIS MET THR VAL GLU THR ALA VAL
SEQRES 6 C 435 LEU ILE GLU THR LEU VAL THR LEU GLY ALA GLU VAL GLN
SEQRES 7 C 435 TRP SER SER CYS ASN ILE PHE SER THR GLN ASP HIS ALA
SEQRES 8 C 435 ALA ALA ALA ILE ALA LYS ALA GLY ILE PRO VAL TYR ALA
SEQRES 9 C 435 TRP LYS GLY GLU THR ASP GLU GLU TYR LEU TRP CYS ILE
SEQRES 10 C 435 GLU GLN THR LEU TYR PHE LYS ASP GLY PRO LEU ASN MET
SEQRES 11 C 435 ILE LEU ASP ASP GLY GLY ASP LEU THR ASN LEU ILE HIS
SEQRES 12 C 435 THR LYS TYR PRO GLN LEU LEU PRO GLY ILE ARG GLY ILE
SEQRES 13 C 435 SER GLU GLU THR THR THR GLY VAL HIS ASN LEU TYR LYS
SEQRES 14 C 435 MET MET ALA ASN GLY ILE LEU LYS VAL PRO ALA ILE ASN
SEQRES 15 C 435 VAL ASN ASP SER VAL THR LYS SER LYS PHE ASP ASN LEU
SEQRES 16 C 435 TYR GLY CYS ARG GLU SER LEU ILE ASP GLY ILE LYS ARG
SEQRES 17 C 435 ALA THR ASP VAL MET ILE ALA GLY LYS VAL ALA VAL VAL
SEQRES 18 C 435 ALA GLY TYR GLY ASP VAL GLY LYS GLY CYS ALA GLN ALA
SEQRES 19 C 435 LEU ARG GLY PHE GLY ALA ARG VAL ILE ILE THR GLU ILE
SEQRES 20 C 435 ASP PRO ILE ASN ALA LEU GLN ALA ALA MET GLU GLY TYR
SEQRES 21 C 435 GLU VAL THR THR MET ASP GLU ALA CYS GLN GLU GLY ASN
SEQRES 22 C 435 ILE PHE VAL THR THR THR GLY CYS ILE ASP ILE ILE LEU
SEQRES 23 C 435 GLY ARG HIS PHE GLU GLN MET LYS ASP ASP ALA ILE VAL
SEQRES 24 C 435 CYS ASN ILE GLY HIS PHE ASP VAL GLU ILE ASP VAL LYS
SEQRES 25 C 435 TRP LEU ASN GLU ASN ALA VAL GLU LYS VAL ASN ILE LYS
SEQRES 26 C 435 PRO GLN VAL ASP ARG TYR ARG LEU LYS ASN GLY ARG ARG
SEQRES 27 C 435 ILE ILE LEU LEU ALA GLU GLY ARG LEU VAL ASN LEU GLY
SEQRES 28 C 435 CYS ALA MET GLY HIS PRO SER PHE VAL MET SER ASN SER
SEQRES 29 C 435 PHE THR ASN GLN VAL MET ALA GLN ILE GLU LEU TRP THR
SEQRES 30 C 435 HIS PRO ASP LYS TYR PRO VAL GLY VAL HIS PHE LEU PRO
SEQRES 31 C 435 LYS LYS LEU ASP GLU ALA VAL ALA GLU ALA HIS LEU GLY
SEQRES 32 C 435 LYS LEU ASN VAL LYS LEU THR LYS LEU THR GLU LYS GLN
SEQRES 33 C 435 ALA GLN TYR LEU GLY MET SER CYS ASP GLY PRO PHE LYS
SEQRES 34 C 435 PRO ASP HIS TYR ARG TYR
SEQRES 1 D 435 GLY SER HIS MET SER ASP LYS LEU PRO TYR LYS VAL ALA
SEQRES 2 D 435 ASP ILE GLY LEU ALA ALA TRP GLY ARG LYS ALA LEU ASP
SEQRES 3 D 435 ILE ALA GLU ASN GLU MET PRO GLY LEU MET ARG MET ARG
SEQRES 4 D 435 GLU ARG TYR SER ALA SER LYS PRO LEU LYS GLY ALA ARG
SEQRES 5 D 435 ILE ALA GLY CYS LEU HIS MET THR VAL GLU THR ALA VAL
SEQRES 6 D 435 LEU ILE GLU THR LEU VAL THR LEU GLY ALA GLU VAL GLN
SEQRES 7 D 435 TRP SER SER CYS ASN ILE PHE SER THR GLN ASP HIS ALA
SEQRES 8 D 435 ALA ALA ALA ILE ALA LYS ALA GLY ILE PRO VAL TYR ALA
SEQRES 9 D 435 TRP LYS GLY GLU THR ASP GLU GLU TYR LEU TRP CYS ILE
SEQRES 10 D 435 GLU GLN THR LEU TYR PHE LYS ASP GLY PRO LEU ASN MET
SEQRES 11 D 435 ILE LEU ASP ASP GLY GLY ASP LEU THR ASN LEU ILE HIS
SEQRES 12 D 435 THR LYS TYR PRO GLN LEU LEU PRO GLY ILE ARG GLY ILE
SEQRES 13 D 435 SER GLU GLU THR THR THR GLY VAL HIS ASN LEU TYR LYS
SEQRES 14 D 435 MET MET ALA ASN GLY ILE LEU LYS VAL PRO ALA ILE ASN
SEQRES 15 D 435 VAL ASN ASP SER VAL THR LYS SER LYS PHE ASP ASN LEU
SEQRES 16 D 435 TYR GLY CYS ARG GLU SER LEU ILE ASP GLY ILE LYS ARG
SEQRES 17 D 435 ALA THR ASP VAL MET ILE ALA GLY LYS VAL ALA VAL VAL
SEQRES 18 D 435 ALA GLY TYR GLY ASP VAL GLY LYS GLY CYS ALA GLN ALA
SEQRES 19 D 435 LEU ARG GLY PHE GLY ALA ARG VAL ILE ILE THR GLU ILE
SEQRES 20 D 435 ASP PRO ILE ASN ALA LEU GLN ALA ALA MET GLU GLY TYR
SEQRES 21 D 435 GLU VAL THR THR MET ASP GLU ALA CYS GLN GLU GLY ASN
SEQRES 22 D 435 ILE PHE VAL THR THR THR GLY CYS ILE ASP ILE ILE LEU
SEQRES 23 D 435 GLY ARG HIS PHE GLU GLN MET LYS ASP ASP ALA ILE VAL
SEQRES 24 D 435 CYS ASN ILE GLY HIS PHE ASP VAL GLU ILE ASP VAL LYS
SEQRES 25 D 435 TRP LEU ASN GLU ASN ALA VAL GLU LYS VAL ASN ILE LYS
SEQRES 26 D 435 PRO GLN VAL ASP ARG TYR ARG LEU LYS ASN GLY ARG ARG
SEQRES 27 D 435 ILE ILE LEU LEU ALA GLU GLY ARG LEU VAL ASN LEU GLY
SEQRES 28 D 435 CYS ALA MET GLY HIS PRO SER PHE VAL MET SER ASN SER
SEQRES 29 D 435 PHE THR ASN GLN VAL MET ALA GLN ILE GLU LEU TRP THR
SEQRES 30 D 435 HIS PRO ASP LYS TYR PRO VAL GLY VAL HIS PHE LEU PRO
SEQRES 31 D 435 LYS LYS LEU ASP GLU ALA VAL ALA GLU ALA HIS LEU GLY
SEQRES 32 D 435 LYS LEU ASN VAL LYS LEU THR LYS LEU THR GLU LYS GLN
SEQRES 33 D 435 ALA GLN TYR LEU GLY MET SER CYS ASP GLY PRO PHE LYS
SEQRES 34 D 435 PRO ASP HIS TYR ARG TYR
HET NAD A 501 44
HET AFX A 601 20
HET NAD B 502 44
HET AFX B 602 20
HET NAD C 503 44
HET AFX C 603 20
HET NAD D 504 44
HET AFX D 604 20
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM AFX (4S,5S)-4-(6-AMINO-9H-PURIN-9-YL)-3-FLUORO-5-HYDROXY-2-
HETNAM 2 AFX (HYDROXYMETHYL)CYCLOPENT-2-EN-1-ONE
FORMUL 5 NAD 4(C21 H27 N7 O14 P2)
FORMUL 6 AFX 4(C11 H10 F N5 O3)
FORMUL 13 HOH *258(H2 O)
HELIX 1 1 ASP A 11 GLY A 13 5 3
HELIX 2 2 LEU A 14 ASN A 27 1 14
HELIX 3 3 MET A 29 SER A 40 1 12
HELIX 4 4 THR A 57 LEU A 70 1 14
HELIX 5 5 GLN A 85 ALA A 95 1 11
HELIX 6 6 THR A 106 GLN A 116 1 11
HELIX 7 7 GLY A 133 TYR A 143 1 11
HELIX 8 8 LEU A 146 ILE A 150 5 5
HELIX 9 9 THR A 157 ASN A 170 1 14
HELIX 10 10 SER A 183 LYS A 188 1 6
HELIX 11 11 ASN A 191 ASP A 208 1 18
HELIX 12 12 GLY A 222 PHE A 235 1 14
HELIX 13 13 ASP A 245 GLU A 255 1 11
HELIX 14 14 THR A 261 GLY A 269 1 9
HELIX 15 15 LEU A 283 GLU A 288 1 6
HELIX 16 16 ASP A 307 GLU A 313 1 7
HELIX 17 17 GLU A 341 ARG A 343 5 3
HELIX 18 18 LEU A 344 CYS A 349 1 6
HELIX 19 19 PRO A 354 HIS A 375 1 22
HELIX 20 20 PRO A 376 TYR A 379 5 4
HELIX 21 21 PRO A 387 ALA A 397 1 11
HELIX 22 22 HIS A 398 ASN A 403 1 6
HELIX 23 23 THR A 410 GLY A 418 1 9
HELIX 24 24 ASP B 11 GLY B 13 5 3
HELIX 25 25 LEU B 14 ASN B 27 1 14
HELIX 26 26 MET B 29 SER B 40 1 12
HELIX 27 27 THR B 57 LEU B 70 1 14
HELIX 28 28 GLN B 85 ALA B 95 1 11
HELIX 29 29 THR B 106 GLN B 116 1 11
HELIX 30 30 GLY B 133 TYR B 143 1 11
HELIX 31 31 PRO B 144 ILE B 150 5 7
HELIX 32 32 THR B 157 ASN B 170 1 14
HELIX 33 33 SER B 183 LYS B 188 1 6
HELIX 34 34 PHE B 189 ASP B 208 1 20
HELIX 35 35 GLY B 222 PHE B 235 1 14
HELIX 36 36 ASP B 245 GLU B 255 1 11
HELIX 37 37 THR B 261 CYS B 266 1 6
HELIX 38 38 LEU B 283 GLU B 288 1 6
HELIX 39 39 ASP B 307 GLU B 313 1 7
HELIX 40 40 GLU B 341 ARG B 343 5 3
HELIX 41 41 LEU B 344 CYS B 349 1 6
HELIX 42 42 PRO B 354 HIS B 375 1 22
HELIX 43 43 PRO B 387 HIS B 398 1 12
HELIX 44 44 HIS B 398 ASN B 403 1 6
HELIX 45 45 THR B 410 GLY B 418 1 9
HELIX 46 46 ASP C 11 GLY C 13 5 3
HELIX 47 47 LEU C 14 ASN C 27 1 14
HELIX 48 48 MET C 29 SER C 40 1 12
HELIX 49 49 THR C 57 LEU C 70 1 14
HELIX 50 50 GLN C 85 ALA C 95 1 11
HELIX 51 51 THR C 106 GLN C 116 1 11
HELIX 52 52 GLY C 133 TYR C 143 1 11
HELIX 53 53 PRO C 144 ILE C 150 5 7
HELIX 54 54 THR C 157 ASN C 170 1 14
HELIX 55 55 SER C 183 LYS C 188 1 6
HELIX 56 56 GLY C 194 ASP C 208 1 15
HELIX 57 57 GLY C 222 PHE C 235 1 14
HELIX 58 58 ASP C 245 GLU C 255 1 11
HELIX 59 59 THR C 261 CYS C 266 1 6
HELIX 60 60 LEU C 283 MET C 290 1 8
HELIX 61 61 ASP C 307 GLU C 313 1 7
HELIX 62 62 GLU C 341 ARG C 343 5 3
HELIX 63 63 LEU C 344 ALA C 350 1 7
HELIX 64 64 PRO C 354 HIS C 375 1 22
HELIX 65 65 PRO C 387 GLY C 400 1 14
HELIX 66 66 THR C 410 LEU C 417 1 8
HELIX 67 67 ASP D 11 GLY D 13 5 3
HELIX 68 68 LEU D 14 MET D 29 1 16
HELIX 69 69 MET D 29 SER D 40 1 12
HELIX 70 70 THR D 57 LEU D 70 1 14
HELIX 71 71 GLN D 85 ALA D 95 1 11
HELIX 72 72 THR D 106 GLN D 116 1 11
HELIX 73 73 GLY D 133 TYR D 143 1 11
HELIX 74 74 PRO D 144 ILE D 150 5 7
HELIX 75 75 THR D 157 ASN D 170 1 14
HELIX 76 76 SER D 183 LYS D 188 1 6
HELIX 77 77 PHE D 189 ASP D 208 1 20
HELIX 78 78 GLY D 222 PHE D 235 1 14
HELIX 79 79 ASP D 245 GLU D 255 1 11
HELIX 80 80 THR D 261 CYS D 266 1 6
HELIX 81 81 LEU D 283 GLU D 288 1 6
HELIX 82 82 ASP D 307 ALA D 315 1 9
HELIX 83 83 GLU D 341 ARG D 343 5 3
HELIX 84 84 LEU D 344 CYS D 349 1 6
HELIX 85 85 PRO D 354 HIS D 375 1 22
HELIX 86 86 PRO D 376 TYR D 379 5 4
HELIX 87 87 PRO D 387 GLY D 400 1 14
HELIX 88 88 LYS D 401 ASN D 403 5 3
HELIX 89 89 THR D 410 GLY D 418 1 9
SHEET 1 A 4 VAL A 99 TYR A 100 0
SHEET 2 A 4 GLU A 73 SER A 77 1 N TRP A 76 O TYR A 100
SHEET 3 A 4 ARG A 49 CYS A 53 1 N GLY A 52 O SER A 77
SHEET 4 A 4 MET A 127 LEU A 129 1 O LEU A 129 N CYS A 53
SHEET 1 B 2 TYR A 119 PHE A 120 0
SHEET 2 B 2 GLY A 123 PRO A 124 -1 O GLY A 123 N PHE A 120
SHEET 1 C 3 ILE A 153 GLU A 155 0
SHEET 2 C 3 ALA A 177 ASN A 179 1 O ILE A 178 N ILE A 153
SHEET 3 C 3 VAL A 383 HIS A 384 1 O HIS A 384 N ASN A 179
SHEET 1 D 8 GLU A 258 VAL A 259 0
SHEET 2 D 8 ARG A 238 THR A 242 1 N ILE A 241 O GLU A 258
SHEET 3 D 8 VAL A 215 ALA A 219 1 N ALA A 216 O ILE A 240
SHEET 4 D 8 ILE A 271 THR A 274 1 O ILE A 271 N VAL A 217
SHEET 5 D 8 ALA A 294 ASN A 298 1 O ILE A 295 N PHE A 272
SHEET 6 D 8 ARG A 335 LEU A 339 1 O ILE A 337 N VAL A 296
SHEET 7 D 8 VAL A 325 ARG A 329 -1 N TYR A 328 O ILE A 336
SHEET 8 D 8 GLU A 317 LYS A 322 -1 N VAL A 319 O ARG A 327
SHEET 1 E 7 VAL B 99 TYR B 100 0
SHEET 2 E 7 GLU B 73 SER B 77 1 N TRP B 76 O TYR B 100
SHEET 3 E 7 ARG B 49 CYS B 53 1 N GLY B 52 O GLN B 75
SHEET 4 E 7 MET B 127 ASP B 130 1 O LEU B 129 N CYS B 53
SHEET 5 E 7 GLY B 152 SER B 154 1 O SER B 154 N ILE B 128
SHEET 6 E 7 ALA B 177 ILE B 178 1 O ILE B 178 N ILE B 153
SHEET 7 E 7 VAL B 383 HIS B 384 1 O HIS B 384 N ALA B 177
SHEET 1 F 2 TYR B 119 PHE B 120 0
SHEET 2 F 2 GLY B 123 PRO B 124 -1 O GLY B 123 N PHE B 120
SHEET 1 G 8 GLU B 258 VAL B 259 0
SHEET 2 G 8 ARG B 238 THR B 242 1 N ILE B 241 O GLU B 258
SHEET 3 G 8 VAL B 215 ALA B 219 1 N ALA B 216 O ARG B 238
SHEET 4 G 8 ILE B 271 THR B 274 1 O ILE B 271 N VAL B 217
SHEET 5 G 8 ALA B 294 ASN B 298 1 O ILE B 295 N PHE B 272
SHEET 6 G 8 ARG B 335 LEU B 339 1 O ILE B 337 N VAL B 296
SHEET 7 G 8 VAL B 325 ARG B 329 -1 N TYR B 328 O ILE B 336
SHEET 8 G 8 GLU B 317 LYS B 322 -1 N VAL B 319 O ARG B 327
SHEET 1 H 7 VAL C 99 TYR C 100 0
SHEET 2 H 7 GLU C 73 SER C 77 1 N TRP C 76 O TYR C 100
SHEET 3 H 7 ARG C 49 CYS C 53 1 N ILE C 50 O GLU C 73
SHEET 4 H 7 MET C 127 ASP C 130 1 O LEU C 129 N CYS C 53
SHEET 5 H 7 GLY C 152 GLU C 155 1 O SER C 154 N ILE C 128
SHEET 6 H 7 ALA C 177 ASN C 179 1 O ILE C 178 N ILE C 153
SHEET 7 H 7 VAL C 383 HIS C 384 1 O HIS C 384 N ASN C 179
SHEET 1 I 2 TYR C 119 PHE C 120 0
SHEET 2 I 2 GLY C 123 PRO C 124 -1 O GLY C 123 N PHE C 120
SHEET 1 J 8 GLU C 258 VAL C 259 0
SHEET 2 J 8 ARG C 238 THR C 242 1 N ILE C 241 O GLU C 258
SHEET 3 J 8 VAL C 215 ALA C 219 1 N ALA C 216 O ILE C 240
SHEET 4 J 8 ILE C 271 THR C 274 1 O ILE C 271 N VAL C 217
SHEET 5 J 8 ALA C 294 ASN C 298 1 O ILE C 295 N PHE C 272
SHEET 6 J 8 ARG C 335 LEU C 339 1 O ILE C 337 N VAL C 296
SHEET 7 J 8 VAL C 325 ARG C 329 -1 N TYR C 328 O ILE C 336
SHEET 8 J 8 GLU C 317 LYS C 322 -1 N VAL C 319 O ARG C 327
SHEET 1 K 7 VAL D 99 TYR D 100 0
SHEET 2 K 7 GLU D 73 SER D 77 1 N TRP D 76 O TYR D 100
SHEET 3 K 7 ARG D 49 CYS D 53 1 N ILE D 50 O GLU D 73
SHEET 4 K 7 MET D 127 ASP D 130 1 O LEU D 129 N CYS D 53
SHEET 5 K 7 GLY D 152 GLU D 155 1 O GLY D 152 N ILE D 128
SHEET 6 K 7 ALA D 177 ASN D 179 1 O ILE D 178 N ILE D 153
SHEET 7 K 7 VAL D 383 HIS D 384 1 O HIS D 384 N ASN D 179
SHEET 1 L 2 TYR D 119 PHE D 120 0
SHEET 2 L 2 GLY D 123 PRO D 124 -1 O GLY D 123 N PHE D 120
SHEET 1 M 8 GLU D 258 VAL D 259 0
SHEET 2 M 8 ARG D 238 THR D 242 1 N ILE D 241 O GLU D 258
SHEET 3 M 8 VAL D 215 ALA D 219 1 N VAL D 218 O ILE D 240
SHEET 4 M 8 ILE D 271 THR D 274 1 O VAL D 273 N ALA D 219
SHEET 5 M 8 ALA D 294 ASN D 298 1 O ILE D 295 N PHE D 272
SHEET 6 M 8 ARG D 335 LEU D 339 1 O ILE D 337 N VAL D 296
SHEET 7 M 8 VAL D 325 ARG D 329 -1 N TYR D 328 O ILE D 336
SHEET 8 M 8 GLU D 317 LYS D 322 -1 N VAL D 319 O ARG D 327
SITE 1 AC1 33 THR A 157 THR A 158 THR A 159 ASP A 190
SITE 2 AC1 33 ASN A 191 GLY A 220 GLY A 222 ASP A 223
SITE 3 AC1 33 VAL A 224 THR A 242 GLU A 243 ILE A 244
SITE 4 AC1 33 ASP A 245 ASN A 248 THR A 275 THR A 276
SITE 5 AC1 33 CYS A 278 ILE A 281 ILE A 299 GLY A 300
SITE 6 AC1 33 HIS A 301 LEU A 344 ASN A 346 HIS A 353
SITE 7 AC1 33 HOH A 451 HOH A 478 HOH A 486 AFX A 601
SITE 8 AC1 33 LEU B 409 GLN B 413 LYS B 426 TYR B 430
SITE 9 AC1 33 HOH B 457
SITE 1 AC2 17 HIS A 55 THR A 57 GLU A 59 THR A 60
SITE 2 AC2 17 ASP A 131 GLU A 156 THR A 157 LYS A 186
SITE 3 AC2 17 ASP A 190 HIS A 301 LEU A 344 LEU A 347
SITE 4 AC2 17 MET A 351 GLY A 352 HIS A 353 MET A 358
SITE 5 AC2 17 NAD A 501
SITE 1 AC3 28 GLN A 413 LYS A 426 TYR A 430 THR B 157
SITE 2 AC3 28 THR B 158 THR B 159 ASP B 190 ASN B 191
SITE 3 AC3 28 GLY B 220 GLY B 222 ASP B 223 VAL B 224
SITE 4 AC3 28 THR B 242 GLU B 243 ILE B 244 ASP B 245
SITE 5 AC3 28 ASN B 248 THR B 275 THR B 276 ILE B 281
SITE 6 AC3 28 ILE B 299 GLY B 300 HIS B 301 LEU B 344
SITE 7 AC3 28 ASN B 346 HIS B 353 HOH B 512 AFX B 602
SITE 1 AC4 17 LEU B 54 HIS B 55 THR B 57 GLU B 59
SITE 2 AC4 17 THR B 60 ASP B 131 GLU B 156 THR B 157
SITE 3 AC4 17 LYS B 186 ASP B 190 HIS B 301 LEU B 347
SITE 4 AC4 17 MET B 351 GLY B 352 HIS B 353 MET B 358
SITE 5 AC4 17 NAD B 502
SITE 1 AC5 27 THR C 157 THR C 158 THR C 159 ASP C 190
SITE 2 AC5 27 ASN C 191 GLY C 220 GLY C 222 ASP C 223
SITE 3 AC5 27 VAL C 224 THR C 242 GLU C 243 ILE C 244
SITE 4 AC5 27 ASP C 245 ASN C 248 THR C 275 THR C 276
SITE 5 AC5 27 ILE C 281 ILE C 299 GLY C 300 HIS C 301
SITE 6 AC5 27 LEU C 344 ASN C 346 HIS C 353 AFX C 603
SITE 7 AC5 27 LEU D 409 LYS D 426 TYR D 430
SITE 1 AC6 15 HIS C 55 THR C 57 GLU C 59 ASP C 131
SITE 2 AC6 15 GLU C 156 THR C 157 LYS C 186 ASP C 190
SITE 3 AC6 15 HIS C 301 LEU C 347 MET C 351 GLY C 352
SITE 4 AC6 15 HIS C 353 MET C 358 NAD C 503
SITE 1 AC7 28 GLN C 413 LYS C 426 TYR C 430 THR D 157
SITE 2 AC7 28 THR D 158 THR D 159 ASP D 190 ASN D 191
SITE 3 AC7 28 GLY D 220 GLY D 222 ASP D 223 VAL D 224
SITE 4 AC7 28 THR D 242 GLU D 243 ILE D 244 ASP D 245
SITE 5 AC7 28 ASN D 248 THR D 275 THR D 276 ILE D 281
SITE 6 AC7 28 ILE D 299 HIS D 301 LEU D 344 ASN D 346
SITE 7 AC7 28 HIS D 353 HOH D 442 HOH D 454 AFX D 604
SITE 1 AC8 16 HIS D 55 THR D 57 GLU D 59 THR D 60
SITE 2 AC8 16 ASP D 131 GLU D 156 THR D 157 LYS D 186
SITE 3 AC8 16 ASP D 190 HIS D 301 LEU D 347 MET D 351
SITE 4 AC8 16 GLY D 352 HIS D 353 MET D 358 NAD D 504
CRYST1 91.201 81.939 129.599 90.00 107.01 90.00 P 1 21 1 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 0.010965 0.000000 0.003354 0.00000
SCALE2 0.000000 0.012204 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008069 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
