HEADER HYDROLASE 29-APR-14 4PFJ
TITLE THE STRUCTURE OF BI-ACETYLATED SAHH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSYLHOMOCYSTEINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ADOHCYASE, S-ADENOSYL-L-HOMOCYSTEINE HYDROLASE;
COMPND 5 EC: 3.3.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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
KEYWDS ACETYLATION SAHH HYDROLASE SEMI-SYNTHETIC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.KAVRAN,Y.WANG,P.A.COLE,D.J.LEAHY
REVDAT 7 15-NOV-23 4PFJ 1 ATOM
REVDAT 6 27-SEP-23 4PFJ 1 REMARK
REVDAT 5 17-JAN-18 4PFJ 1 REMARK SITE ATOM
REVDAT 4 22-NOV-17 4PFJ 1 SOURCE JRNL REMARK
REVDAT 3 19-NOV-14 4PFJ 1 JRNL
REVDAT 2 08-OCT-14 4PFJ 1 JRNL
REVDAT 1 01-OCT-14 4PFJ 0
JRNL AUTH Y.WANG,J.M.KAVRAN,Z.CHEN,K.R.KARUKURICHI,D.J.LEAHY,P.A.COLE
JRNL TITL REGULATION OF S-ADENOSYLHOMOCYSTEINE HYDROLASE BY LYSINE
JRNL TITL 2 ACETYLATION.
JRNL REF J.BIOL.CHEM. V. 289 31361 2014
JRNL REFN ESSN 1083-351X
JRNL PMID 25248746
JRNL DOI 10.1074/JBC.M114.597153
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 39774
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2008
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 49.1942 - 5.5435 0.99 2858 133 0.1834 0.2337
REMARK 3 2 5.5435 - 4.4009 1.00 2756 145 0.1590 0.1948
REMARK 3 3 4.4009 - 3.8449 1.00 2714 145 0.1545 0.2211
REMARK 3 4 3.8449 - 3.4934 1.00 2724 141 0.1637 0.2085
REMARK 3 5 3.4934 - 3.2431 1.00 2693 146 0.1825 0.2282
REMARK 3 6 3.2431 - 3.0519 1.00 2695 151 0.1995 0.2549
REMARK 3 7 3.0519 - 2.8991 1.00 2685 141 0.2148 0.2897
REMARK 3 8 2.8991 - 2.7729 1.00 2679 161 0.2216 0.2556
REMARK 3 9 2.7729 - 2.6662 1.00 2701 133 0.2258 0.3133
REMARK 3 10 2.6662 - 2.5742 1.00 2666 135 0.2442 0.2892
REMARK 3 11 2.5742 - 2.4937 1.00 2683 146 0.2397 0.2763
REMARK 3 12 2.4937 - 2.4224 1.00 2685 130 0.2613 0.3402
REMARK 3 13 2.4224 - 2.3586 1.00 2621 165 0.2662 0.2924
REMARK 3 14 2.3586 - 2.3011 0.97 2606 136 0.3010 0.3484
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.510
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 6920
REMARK 3 ANGLE : 0.847 9393
REMARK 3 CHIRALITY : 0.030 1058
REMARK 3 PLANARITY : 0.003 1193
REMARK 3 DIHEDRAL : 14.259 2544
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 4PFJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000201295.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JAN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39810
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.240
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1LI4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM FORMATE, BIS-TRIS,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 49.18300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.36350
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 88.08000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 49.18300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.36350
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 88.08000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 49.18300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 51.36350
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 88.08000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 49.18300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 51.36350
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 88.08000
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: 28540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -130.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 98.36600
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 603 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ASP B 3
REMARK 465 LYS B 4
REMARK 465 LEU B 5
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ALY A 408 CH
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 HD21 ASN B 179 OD2 ASP B 182 1.53
REMARK 500 HD21 ASN A 179 OD2 ASP A 182 1.57
REMARK 500 O HOH A 749 O HOH A 775 2.09
REMARK 500 ND2 ASN B 179 OD2 ASP B 182 2.09
REMARK 500 OE1 GLU B 26 O HOH B 601 2.17
REMARK 500 O ALA B 72 O HOH B 602 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 11 100.37 -161.19
REMARK 500 HIS A 55 122.90 -34.35
REMARK 500 ALA A 101 141.25 -172.31
REMARK 500 LYS A 186 -72.43 -103.39
REMARK 500 PHE A 189 -64.78 -125.60
REMARK 500 THR A 275 25.45 -140.92
REMARK 500 ALA A 350 -152.43 -146.91
REMARK 500 TYR B 7 -179.81 -172.07
REMARK 500 LYS B 8 116.98 -161.75
REMARK 500 ALA B 101 146.22 -171.84
REMARK 500 PRO B 124 179.99 -58.74
REMARK 500 LYS B 186 -74.99 -87.83
REMARK 500 PHE B 189 -57.73 -121.96
REMARK 500 LEU B 192 -73.47 -81.42
REMARK 500 ASP B 303 49.41 -86.25
REMARK 500 ALA B 350 -149.66 -138.03
REMARK 500 VAL B 381 102.51 -54.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 794 DISTANCE = 6.62 ANGSTROMS
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 ADN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADN B 502
DBREF 4PFJ A 1 432 UNP P23526 SAHH_HUMAN 1 432
DBREF 4PFJ B 1 432 UNP P23526 SAHH_HUMAN 1 432
SEQADV 4PFJ ASN A 86 UNP P23526 ASP 86 VARIANT
SEQADV 4PFJ CYS A 396 UNP P23526 GLU 396 ENGINEERED MUTATION
SEQADV 4PFJ ASN B 86 UNP P23526 ASP 86 VARIANT
SEQADV 4PFJ CYS B 396 UNP P23526 GLU 396 ENGINEERED MUTATION
SEQRES 1 A 432 MET SER ASP LYS LEU PRO TYR LYS VAL ALA ASP ILE GLY
SEQRES 2 A 432 LEU ALA ALA TRP GLY ARG LYS ALA LEU ASP ILE ALA GLU
SEQRES 3 A 432 ASN GLU MET PRO GLY LEU MET ARG MET ARG GLU ARG TYR
SEQRES 4 A 432 SER ALA SER LYS PRO LEU LYS GLY ALA ARG ILE ALA GLY
SEQRES 5 A 432 CYS LEU HIS MET THR VAL GLU THR ALA VAL LEU ILE GLU
SEQRES 6 A 432 THR LEU VAL THR LEU GLY ALA GLU VAL GLN TRP SER SER
SEQRES 7 A 432 CYS ASN ILE PHE SER THR GLN ASN HIS ALA ALA ALA ALA
SEQRES 8 A 432 ILE ALA LYS ALA GLY ILE PRO VAL TYR ALA TRP LYS GLY
SEQRES 9 A 432 GLU THR ASP GLU GLU TYR LEU TRP CYS ILE GLU GLN THR
SEQRES 10 A 432 LEU TYR PHE LYS ASP GLY PRO LEU ASN MET ILE LEU ASP
SEQRES 11 A 432 ASP GLY GLY ASP LEU THR ASN LEU ILE HIS THR LYS TYR
SEQRES 12 A 432 PRO GLN LEU LEU PRO GLY ILE ARG GLY ILE SER GLU GLU
SEQRES 13 A 432 THR THR THR GLY VAL HIS ASN LEU TYR LYS MET MET ALA
SEQRES 14 A 432 ASN GLY ILE LEU LYS VAL PRO ALA ILE ASN VAL ASN ASP
SEQRES 15 A 432 SER VAL THR LYS SER LYS PHE ASP ASN LEU TYR GLY CYS
SEQRES 16 A 432 ARG GLU SER LEU ILE ASP GLY ILE LYS ARG ALA THR ASP
SEQRES 17 A 432 VAL MET ILE ALA GLY LYS VAL ALA VAL VAL ALA GLY TYR
SEQRES 18 A 432 GLY ASP VAL GLY LYS GLY CYS ALA GLN ALA LEU ARG GLY
SEQRES 19 A 432 PHE GLY ALA ARG VAL ILE ILE THR GLU ILE ASP PRO ILE
SEQRES 20 A 432 ASN ALA LEU GLN ALA ALA MET GLU GLY TYR GLU VAL THR
SEQRES 21 A 432 THR MET ASP GLU ALA CYS GLN GLU GLY ASN ILE PHE VAL
SEQRES 22 A 432 THR THR THR GLY CYS ILE ASP ILE ILE LEU GLY ARG HIS
SEQRES 23 A 432 PHE GLU GLN MET LYS ASP ASP ALA ILE VAL CYS ASN ILE
SEQRES 24 A 432 GLY HIS PHE ASP VAL GLU ILE ASP VAL LYS TRP LEU ASN
SEQRES 25 A 432 GLU ASN ALA VAL GLU LYS VAL ASN ILE LYS PRO GLN VAL
SEQRES 26 A 432 ASP ARG TYR ARG LEU LYS ASN GLY ARG ARG ILE ILE LEU
SEQRES 27 A 432 LEU ALA GLU GLY ARG LEU VAL ASN LEU GLY CYS ALA MET
SEQRES 28 A 432 GLY HIS PRO SER PHE VAL MET SER ASN SER PHE THR ASN
SEQRES 29 A 432 GLN VAL MET ALA GLN ILE GLU LEU TRP THR HIS PRO ASP
SEQRES 30 A 432 LYS TYR PRO VAL GLY VAL HIS PHE LEU PRO LYS LYS LEU
SEQRES 31 A 432 ASP GLU ALA VAL ALA CYS ALA HIS LEU GLY ALY LEU ASN
SEQRES 32 A 432 VAL LYS LEU THR ALY LEU THR GLU LYS GLN ALA GLN TYR
SEQRES 33 A 432 LEU GLY MET SER CYS ASP GLY PRO PHE LYS PRO ASP HIS
SEQRES 34 A 432 TYR ARG TYR
SEQRES 1 B 432 MET SER ASP LYS LEU PRO TYR LYS VAL ALA ASP ILE GLY
SEQRES 2 B 432 LEU ALA ALA TRP GLY ARG LYS ALA LEU ASP ILE ALA GLU
SEQRES 3 B 432 ASN GLU MET PRO GLY LEU MET ARG MET ARG GLU ARG TYR
SEQRES 4 B 432 SER ALA SER LYS PRO LEU LYS GLY ALA ARG ILE ALA GLY
SEQRES 5 B 432 CYS LEU HIS MET THR VAL GLU THR ALA VAL LEU ILE GLU
SEQRES 6 B 432 THR LEU VAL THR LEU GLY ALA GLU VAL GLN TRP SER SER
SEQRES 7 B 432 CYS ASN ILE PHE SER THR GLN ASN HIS ALA ALA ALA ALA
SEQRES 8 B 432 ILE ALA LYS ALA GLY ILE PRO VAL TYR ALA TRP LYS GLY
SEQRES 9 B 432 GLU THR ASP GLU GLU TYR LEU TRP CYS ILE GLU GLN THR
SEQRES 10 B 432 LEU TYR PHE LYS ASP GLY PRO LEU ASN MET ILE LEU ASP
SEQRES 11 B 432 ASP GLY GLY ASP LEU THR ASN LEU ILE HIS THR LYS TYR
SEQRES 12 B 432 PRO GLN LEU LEU PRO GLY ILE ARG GLY ILE SER GLU GLU
SEQRES 13 B 432 THR THR THR GLY VAL HIS ASN LEU TYR LYS MET MET ALA
SEQRES 14 B 432 ASN GLY ILE LEU LYS VAL PRO ALA ILE ASN VAL ASN ASP
SEQRES 15 B 432 SER VAL THR LYS SER LYS PHE ASP ASN LEU TYR GLY CYS
SEQRES 16 B 432 ARG GLU SER LEU ILE ASP GLY ILE LYS ARG ALA THR ASP
SEQRES 17 B 432 VAL MET ILE ALA GLY LYS VAL ALA VAL VAL ALA GLY TYR
SEQRES 18 B 432 GLY ASP VAL GLY LYS GLY CYS ALA GLN ALA LEU ARG GLY
SEQRES 19 B 432 PHE GLY ALA ARG VAL ILE ILE THR GLU ILE ASP PRO ILE
SEQRES 20 B 432 ASN ALA LEU GLN ALA ALA MET GLU GLY TYR GLU VAL THR
SEQRES 21 B 432 THR MET ASP GLU ALA CYS GLN GLU GLY ASN ILE PHE VAL
SEQRES 22 B 432 THR THR THR GLY CYS ILE ASP ILE ILE LEU GLY ARG HIS
SEQRES 23 B 432 PHE GLU GLN MET LYS ASP ASP ALA ILE VAL CYS ASN ILE
SEQRES 24 B 432 GLY HIS PHE ASP VAL GLU ILE ASP VAL LYS TRP LEU ASN
SEQRES 25 B 432 GLU ASN ALA VAL GLU LYS VAL ASN ILE LYS PRO GLN VAL
SEQRES 26 B 432 ASP ARG TYR ARG LEU LYS ASN GLY ARG ARG ILE ILE LEU
SEQRES 27 B 432 LEU ALA GLU GLY ARG LEU VAL ASN LEU GLY CYS ALA MET
SEQRES 28 B 432 GLY HIS PRO SER PHE VAL MET SER ASN SER PHE THR ASN
SEQRES 29 B 432 GLN VAL MET ALA GLN ILE GLU LEU TRP THR HIS PRO ASP
SEQRES 30 B 432 LYS TYR PRO VAL GLY VAL HIS PHE LEU PRO LYS LYS LEU
SEQRES 31 B 432 ASP GLU ALA VAL ALA CYS ALA HIS LEU GLY ALY LEU ASN
SEQRES 32 B 432 VAL LYS LEU THR ALY LEU THR GLU LYS GLN ALA GLN TYR
SEQRES 33 B 432 LEU GLY MET SER CYS ASP GLY PRO PHE LYS PRO ASP HIS
SEQRES 34 B 432 TYR ARG TYR
MODRES 4PFJ ALY A 401 LYS MODIFIED RESIDUE
MODRES 4PFJ ALY A 408 LYS MODIFIED RESIDUE
MODRES 4PFJ ALY B 401 LYS MODIFIED RESIDUE
MODRES 4PFJ ALY B 408 LYS MODIFIED RESIDUE
HET ALY A 401 26
HET ALY A 408 25
HET ALY B 401 26
HET ALY B 408 25
HET NAD A 501 70
HET ADN A 502 32
HET NAD B 501 70
HET ADN B 502 32
HETNAM ALY N(6)-ACETYLLYSINE
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM ADN ADENOSINE
FORMUL 1 ALY 4(C8 H16 N2 O3)
FORMUL 3 NAD 2(C21 H27 N7 O14 P2)
FORMUL 4 ADN 2(C10 H13 N5 O4)
FORMUL 7 HOH *326(H2 O)
HELIX 1 AA1 ASP A 11 GLY A 13 5 3
HELIX 2 AA2 LEU A 14 ASN A 27 1 14
HELIX 3 AA3 MET A 29 SER A 40 1 12
HELIX 4 AA4 THR A 57 LEU A 70 1 14
HELIX 5 AA5 GLN A 85 ALA A 95 1 11
HELIX 6 AA6 THR A 106 THR A 117 1 12
HELIX 7 AA7 GLY A 133 TYR A 143 1 11
HELIX 8 AA8 PRO A 144 ILE A 150 5 7
HELIX 9 AA9 THR A 157 ASN A 170 1 14
HELIX 10 AB1 SER A 183 LYS A 188 1 6
HELIX 11 AB2 PHE A 189 ASP A 208 1 20
HELIX 12 AB3 GLY A 222 PHE A 235 1 14
HELIX 13 AB4 ASP A 245 GLU A 255 1 11
HELIX 14 AB5 THR A 261 CYS A 266 1 6
HELIX 15 AB6 LEU A 283 GLU A 288 1 6
HELIX 16 AB7 ASP A 307 ALA A 315 1 9
HELIX 17 AB8 GLU A 341 ARG A 343 5 3
HELIX 18 AB9 LEU A 344 CYS A 349 1 6
HELIX 19 AC1 PRO A 354 HIS A 375 1 22
HELIX 20 AC2 PRO A 376 TYR A 379 5 4
HELIX 21 AC3 PRO A 387 GLY A 400 1 14
HELIX 22 AC4 THR A 410 GLY A 418 1 9
HELIX 23 AC5 ASP B 11 GLY B 13 5 3
HELIX 24 AC6 LEU B 14 GLU B 28 1 15
HELIX 25 AC7 MET B 29 SER B 40 1 12
HELIX 26 AC8 THR B 57 LEU B 70 1 14
HELIX 27 AC9 GLN B 85 ALA B 95 1 11
HELIX 28 AD1 THR B 106 THR B 117 1 12
HELIX 29 AD2 GLY B 133 LYS B 142 1 10
HELIX 30 AD3 LEU B 146 ILE B 150 5 5
HELIX 31 AD4 THR B 157 ASN B 170 1 14
HELIX 32 AD5 SER B 183 LYS B 188 1 6
HELIX 33 AD6 PHE B 189 ASP B 208 1 20
HELIX 34 AD7 GLY B 222 PHE B 235 1 14
HELIX 35 AD8 ASP B 245 MET B 254 1 10
HELIX 36 AD9 THR B 261 CYS B 266 1 6
HELIX 37 AE1 LEU B 283 GLU B 288 1 6
HELIX 38 AE2 ASP B 307 ALA B 315 1 9
HELIX 39 AE3 GLU B 341 ARG B 343 5 3
HELIX 40 AE4 LEU B 344 CYS B 349 1 6
HELIX 41 AE5 PRO B 354 HIS B 375 1 22
HELIX 42 AE6 PRO B 387 GLY B 400 1 14
HELIX 43 AE7 THR B 410 GLY B 418 1 9
SHEET 1 AA1 7 VAL A 99 TYR A 100 0
SHEET 2 AA1 7 GLU A 73 SER A 77 1 N TRP A 76 O TYR A 100
SHEET 3 AA1 7 ARG A 49 CYS A 53 1 N ILE A 50 O GLU A 73
SHEET 4 AA1 7 MET A 127 ASP A 130 1 O LEU A 129 N CYS A 53
SHEET 5 AA1 7 GLY A 152 GLU A 155 1 O SER A 154 N ASP A 130
SHEET 6 AA1 7 ALA A 177 ASN A 179 1 O ILE A 178 N ILE A 153
SHEET 7 AA1 7 VAL A 383 HIS A 384 1 O HIS A 384 N ALA A 177
SHEET 1 AA2 2 TYR A 119 PHE A 120 0
SHEET 2 AA2 2 GLY A 123 PRO A 124 -1 O GLY A 123 N PHE A 120
SHEET 1 AA3 8 GLU A 258 VAL A 259 0
SHEET 2 AA3 8 ARG A 238 THR A 242 1 N ILE A 241 O GLU A 258
SHEET 3 AA3 8 VAL A 215 ALA A 219 1 N ALA A 216 O ILE A 240
SHEET 4 AA3 8 ILE A 271 THR A 274 1 O ILE A 271 N VAL A 217
SHEET 5 AA3 8 ALA A 294 ASN A 298 1 O ILE A 295 N PHE A 272
SHEET 6 AA3 8 ARG A 335 LEU A 339 1 O ILE A 337 N VAL A 296
SHEET 7 AA3 8 VAL A 325 ARG A 329 -1 N ASP A 326 O LEU A 338
SHEET 8 AA3 8 GLU A 317 LYS A 322 -1 N VAL A 319 O ARG A 327
SHEET 1 AA4 7 VAL B 99 TYR B 100 0
SHEET 2 AA4 7 GLU B 73 SER B 77 1 N TRP B 76 O TYR B 100
SHEET 3 AA4 7 ARG B 49 CYS B 53 1 N GLY B 52 O GLN B 75
SHEET 4 AA4 7 MET B 127 ASP B 130 1 O MET B 127 N ALA B 51
SHEET 5 AA4 7 GLY B 152 GLU B 155 1 O SER B 154 N ASP B 130
SHEET 6 AA4 7 ALA B 177 ASN B 179 1 O ILE B 178 N ILE B 153
SHEET 7 AA4 7 VAL B 383 HIS B 384 1 O HIS B 384 N ASN B 179
SHEET 1 AA5 2 TYR B 119 PHE B 120 0
SHEET 2 AA5 2 GLY B 123 PRO B 124 -1 O GLY B 123 N PHE B 120
SHEET 1 AA6 8 GLU B 258 VAL B 259 0
SHEET 2 AA6 8 ARG B 238 THR B 242 1 N ILE B 241 O GLU B 258
SHEET 3 AA6 8 VAL B 215 ALA B 219 1 N ALA B 216 O ILE B 240
SHEET 4 AA6 8 ILE B 271 THR B 274 1 O ILE B 271 N VAL B 217
SHEET 5 AA6 8 ALA B 294 ASN B 298 1 O ILE B 295 N PHE B 272
SHEET 6 AA6 8 ARG B 335 LEU B 339 1 O ILE B 337 N VAL B 296
SHEET 7 AA6 8 VAL B 325 ARG B 329 -1 N TYR B 328 O ILE B 336
SHEET 8 AA6 8 GLU B 317 LYS B 322 -1 N VAL B 319 O ARG B 327
LINK C GLY A 400 N ALY A 401 1555 1555 1.33
LINK C ALY A 401 N LEU A 402 1555 1555 1.33
LINK C THR A 407 N ALY A 408 1555 1555 1.33
LINK C ALY A 408 N LEU A 409 1555 1555 1.33
LINK C GLY B 400 N ALY B 401 1555 1555 1.33
LINK C ALY B 401 N LEU B 402 1555 1555 1.33
LINK C THR B 407 N ALY B 408 1555 1555 1.33
LINK C ALY B 408 N LEU B 409 1555 1555 1.33
CISPEP 1 GLY A 423 PRO A 424 0 0.62
CISPEP 2 GLY B 423 PRO B 424 0 -1.37
SITE 1 AC1 31 THR A 157 THR A 158 THR A 159 ASN A 191
SITE 2 AC1 31 GLY A 220 GLY A 222 ASP A 223 VAL A 224
SITE 3 AC1 31 THR A 242 GLU A 243 ILE A 244 ASP A 245
SITE 4 AC1 31 ASN A 248 THR A 275 THR A 276 GLY A 277
SITE 5 AC1 31 CYS A 278 ILE A 281 ILE A 299 GLY A 300
SITE 6 AC1 31 HIS A 301 ASN A 346 HIS A 353 GLN A 413
SITE 7 AC1 31 LYS A 426 TYR A 430 ADN A 502 HOH A 658
SITE 8 AC1 31 HOH A 681 HOH A 685 HOH A 699
SITE 1 AC2 15 HIS A 55 THR A 57 GLU A 59 THR A 60
SITE 2 AC2 15 ASP A 131 GLU A 156 THR A 157 LYS A 186
SITE 3 AC2 15 ASP A 190 HIS A 301 MET A 351 HIS A 353
SITE 4 AC2 15 MET A 358 PHE A 362 NAD A 501
SITE 1 AC3 29 THR B 157 THR B 158 THR B 159 ASN B 191
SITE 2 AC3 29 GLY B 222 ASP B 223 VAL B 224 THR B 242
SITE 3 AC3 29 GLU B 243 ILE B 244 ASP B 245 ASN B 248
SITE 4 AC3 29 THR B 275 THR B 276 GLY B 277 CYS B 278
SITE 5 AC3 29 ILE B 281 ILE B 299 GLY B 300 HIS B 301
SITE 6 AC3 29 ASN B 346 HIS B 353 GLN B 413 LYS B 426
SITE 7 AC3 29 TYR B 430 ADN B 502 HOH B 657 HOH B 674
SITE 8 AC3 29 HOH B 682
SITE 1 AC4 15 HIS B 55 THR B 57 GLU B 59 THR B 60
SITE 2 AC4 15 ASP B 131 GLU B 156 THR B 157 LYS B 186
SITE 3 AC4 15 ASP B 190 HIS B 301 MET B 351 HIS B 353
SITE 4 AC4 15 MET B 358 PHE B 362 NAD B 501
CRYST1 98.366 102.727 176.160 90.00 90.00 90.00 I 2 2 2 16
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 0.010166 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009735 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005677 0.00000
(ATOM LINES ARE NOT SHOWN.)
END