HEADER LYASE 07-JUN-13 4L3V
TITLE CRYSTAL STRUCTURE OF DELTA516-525 HUMAN CYSTATHIONINE BETA-SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTATHIONINE BETA-SYNTHASE;
COMPND 3 CHAIN: B, A, C;
COMPND 4 SYNONYM: BETA-THIONASE, SERINE SULFHYDRASE;
COMPND 5 EC: 4.2.1.22;
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: CBS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) GOLD
KEYWDS CBS DOMAIN, HOMOCYTEINE, CYSTEINE BIOSYNTHESIS, HEME, PYRIDOXAL 5'-
KEYWDS 2 PHOSPHATE, S-ADENOSYLMETHIONINE, TRANSSULFURATION PATHWAY, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ERENO,T.MAJTAN,I.OYENARTE,J.P.KRAUS,L.A.MARTINEZ
REVDAT 4 20-SEP-23 4L3V 1 REMARK LINK
REVDAT 3 16-OCT-13 4L3V 1 JRNL
REVDAT 2 02-OCT-13 4L3V 1 JRNL
REVDAT 1 18-SEP-13 4L3V 0
JRNL AUTH J.ERENO-ORBEA,T.MAJTAN,I.OYENARTE,J.P.KRAUS,
JRNL AUTH 2 L.A.MARTINEZ-CRUZ
JRNL TITL STRUCTURAL BASIS OF REGULATION AND OLIGOMERIZATION OF HUMAN
JRNL TITL 2 CYSTATHIONINE BETA-SYNTHASE, THE CENTRAL ENZYME OF
JRNL TITL 3 TRANSSULFURATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 110 E3790 2013
JRNL REFN ISSN 0027-8424
JRNL PMID 24043838
JRNL DOI 10.1073/PNAS.1313683110
REMARK 2
REMARK 2 RESOLUTION. 3.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
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) : 3.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 46253
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2340
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 48.5203 - 9.3068 0.97 2768 157 0.1748 0.1667
REMARK 3 2 9.3068 - 7.3955 1.00 2752 149 0.1500 0.1660
REMARK 3 3 7.3955 - 6.4631 1.00 2687 147 0.1880 0.2311
REMARK 3 4 6.4631 - 5.8733 1.00 2692 143 0.2002 0.2351
REMARK 3 5 5.8733 - 5.4529 1.00 2645 173 0.2125 0.2251
REMARK 3 6 5.4529 - 5.1318 1.00 2669 130 0.2016 0.2377
REMARK 3 7 5.1318 - 4.8751 1.00 2662 145 0.2015 0.2261
REMARK 3 8 4.8751 - 4.6630 0.99 2625 140 0.2157 0.2326
REMARK 3 9 4.6630 - 4.4836 1.00 2660 138 0.2163 0.2319
REMARK 3 10 4.4836 - 4.3290 0.99 2639 144 0.2296 0.2284
REMARK 3 11 4.3290 - 4.1937 0.99 2613 143 0.2392 0.2939
REMARK 3 12 4.1937 - 4.0739 0.98 2618 123 0.2511 0.2717
REMARK 3 13 4.0739 - 3.9667 0.99 2633 122 0.2585 0.2959
REMARK 3 14 3.9667 - 3.8700 0.99 2596 143 0.2677 0.2894
REMARK 3 15 3.8700 - 3.7820 0.98 2628 129 0.2882 0.3054
REMARK 3 16 3.7820 - 3.7016 0.99 2587 150 0.3153 0.3028
REMARK 3 17 3.7016 - 3.6276 0.54 1439 64 0.4107 0.3970
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) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.540
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 : 0.007 11968
REMARK 3 ANGLE : 1.165 16268
REMARK 3 CHIRALITY : 0.073 1825
REMARK 3 PLANARITY : 0.009 2080
REMARK 3 DIHEDRAL : 13.002 4449
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 4L3V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1000080147.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46253
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.628
REMARK 200 RESOLUTION RANGE LOW (A) : 48.516
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 2.440
REMARK 200 R MERGE (I) : 0.31000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.37
REMARK 200 R MERGE FOR SHELL (I) : 1.51000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.280
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.8.1_1168
REMARK 200 STARTING MODEL: PDB ENTRY 4LOD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 78.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% V/V PEG550, 0.1 M SODIUM CITRATE
REMARK 280 TRIBASIC DEHYDRATE, PH 5.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.62650
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 53.62650
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 113.87500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 171.32750
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 113.87500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 171.32750
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 53.62650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 113.87500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 171.32750
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 53.62650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 113.87500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 171.32750
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -455.50000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -160.87950
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 PRO B 2
REMARK 465 SER B 3
REMARK 465 GLU B 4
REMARK 465 THR B 5
REMARK 465 PRO B 6
REMARK 465 GLN B 7
REMARK 465 ALA B 8
REMARK 465 GLU B 9
REMARK 465 VAL B 10
REMARK 465 GLY B 11
REMARK 465 PRO B 12
REMARK 465 THR B 13
REMARK 465 GLY B 14
REMARK 465 CYS B 15
REMARK 465 PRO B 16
REMARK 465 HIS B 17
REMARK 465 ARG B 18
REMARK 465 SER B 19
REMARK 465 GLY B 20
REMARK 465 PRO B 21
REMARK 465 HIS B 22
REMARK 465 SER B 23
REMARK 465 ALA B 24
REMARK 465 LYS B 25
REMARK 465 GLY B 26
REMARK 465 SER B 27
REMARK 465 LEU B 28
REMARK 465 GLU B 29
REMARK 465 LYS B 30
REMARK 465 GLY B 31
REMARK 465 SER B 32
REMARK 465 PRO B 33
REMARK 465 GLU B 34
REMARK 465 ASP B 35
REMARK 465 LYS B 36
REMARK 465 GLU B 37
REMARK 465 ALA B 38
REMARK 465 LYS B 39
REMARK 465 GLU B 40
REMARK 465 GLN B 515
REMARK 465 ILE B 516
REMARK 465 GLN B 517
REMARK 465 TYR B 518
REMARK 465 HIS B 519
REMARK 465 SER B 520
REMARK 465 THR B 521
REMARK 465 GLY B 522
REMARK 465 LYS B 523
REMARK 465 SER B 524
REMARK 465 SER B 525
REMARK 465 GLN B 526
REMARK 465 LYS B 551
REMARK 465 PRO A 2
REMARK 465 SER A 3
REMARK 465 GLU A 4
REMARK 465 THR A 5
REMARK 465 PRO A 6
REMARK 465 GLN A 7
REMARK 465 ALA A 8
REMARK 465 GLU A 9
REMARK 465 VAL A 10
REMARK 465 GLY A 11
REMARK 465 PRO A 12
REMARK 465 THR A 13
REMARK 465 GLY A 14
REMARK 465 CYS A 15
REMARK 465 PRO A 16
REMARK 465 HIS A 17
REMARK 465 ARG A 18
REMARK 465 SER A 19
REMARK 465 GLY A 20
REMARK 465 PRO A 21
REMARK 465 HIS A 22
REMARK 465 SER A 23
REMARK 465 ALA A 24
REMARK 465 LYS A 25
REMARK 465 GLY A 26
REMARK 465 SER A 27
REMARK 465 LEU A 28
REMARK 465 GLU A 29
REMARK 465 LYS A 30
REMARK 465 GLY A 31
REMARK 465 SER A 32
REMARK 465 PRO A 33
REMARK 465 GLU A 34
REMARK 465 ASP A 35
REMARK 465 LYS A 36
REMARK 465 GLU A 37
REMARK 465 ALA A 38
REMARK 465 LYS A 39
REMARK 465 GLU A 40
REMARK 465 GLN A 515
REMARK 465 ILE A 516
REMARK 465 GLN A 517
REMARK 465 TYR A 518
REMARK 465 HIS A 519
REMARK 465 SER A 520
REMARK 465 THR A 521
REMARK 465 GLY A 522
REMARK 465 LYS A 523
REMARK 465 SER A 524
REMARK 465 SER A 525
REMARK 465 GLN A 526
REMARK 465 LYS A 551
REMARK 465 PRO C 2
REMARK 465 SER C 3
REMARK 465 GLU C 4
REMARK 465 THR C 5
REMARK 465 PRO C 6
REMARK 465 GLN C 7
REMARK 465 ALA C 8
REMARK 465 GLU C 9
REMARK 465 VAL C 10
REMARK 465 GLY C 11
REMARK 465 PRO C 12
REMARK 465 THR C 13
REMARK 465 GLY C 14
REMARK 465 CYS C 15
REMARK 465 PRO C 16
REMARK 465 HIS C 17
REMARK 465 ARG C 18
REMARK 465 SER C 19
REMARK 465 GLY C 20
REMARK 465 PRO C 21
REMARK 465 HIS C 22
REMARK 465 SER C 23
REMARK 465 ALA C 24
REMARK 465 LYS C 25
REMARK 465 GLY C 26
REMARK 465 SER C 27
REMARK 465 LEU C 28
REMARK 465 GLU C 29
REMARK 465 LYS C 30
REMARK 465 GLY C 31
REMARK 465 SER C 32
REMARK 465 PRO C 33
REMARK 465 GLU C 34
REMARK 465 ASP C 35
REMARK 465 LYS C 36
REMARK 465 GLU C 37
REMARK 465 ALA C 38
REMARK 465 LYS C 39
REMARK 465 GLU C 40
REMARK 465 ALA C 60
REMARK 465 GLN C 515
REMARK 465 ILE C 516
REMARK 465 GLN C 517
REMARK 465 TYR C 518
REMARK 465 HIS C 519
REMARK 465 SER C 520
REMARK 465 THR C 521
REMARK 465 GLY C 522
REMARK 465 LYS C 523
REMARK 465 SER C 524
REMARK 465 SER C 525
REMARK 465 GLN C 526
REMARK 465 LYS C 551
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 THR B 403 CB OG1 CG2
REMARK 470 ASP B 444 CG OD1 OD2
REMARK 470 GLU B 514 CG CD OE1 OE2
REMARK 470 ASP A 444 CB CG OD1 OD2
REMARK 470 GLU A 514 CG CD OE1 OE2
REMARK 470 ASP C 444 CB CG OD1 OD2
REMARK 470 GLU C 514 CG CD OE1 OE2
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 B 94 -62.35 -96.76
REMARK 500 ASP B 221 71.12 53.33
REMARK 500 THR B 235 -67.63 -109.64
REMARK 500 GLN B 341 -60.62 -90.22
REMARK 500 LYS B 384 -86.70 -105.21
REMARK 500 LYS A 94 -62.95 -94.91
REMARK 500 ASN A 194 -5.32 66.86
REMARK 500 ASP A 221 71.95 50.39
REMARK 500 THR A 235 -66.45 -109.51
REMARK 500 LYS A 384 -87.47 -105.63
REMARK 500 ASP A 549 -60.50 -134.11
REMARK 500 LYS C 94 -62.95 -96.53
REMARK 500 ASN C 194 -5.40 64.31
REMARK 500 THR C 235 -68.38 -109.25
REMARK 500 LYS C 384 -87.14 -105.45
REMARK 500 ASP C 549 -62.01 -134.54
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 HEM B 602 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 52 SG
REMARK 620 2 HEM B 602 NA 90.0
REMARK 620 3 HEM B 602 NB 90.0 91.7
REMARK 620 4 HEM B 602 NC 90.0 179.2 87.5
REMARK 620 5 HEM B 602 ND 90.0 87.6 179.3 93.2
REMARK 620 6 HIS B 65 NE2 180.0 90.0 90.0 90.0 90.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 602 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 52 SG
REMARK 620 2 HEM A 602 NA 90.0
REMARK 620 3 HEM A 602 NB 90.0 90.8
REMARK 620 4 HEM A 602 NC 90.0 178.7 87.9
REMARK 620 5 HEM A 602 ND 90.0 88.7 179.5 92.6
REMARK 620 6 HIS A 65 NE2 180.0 90.0 90.0 90.0 90.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 602 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 52 SG
REMARK 620 2 HEM C 602 NA 90.0
REMARK 620 3 HEM C 602 NB 90.0 90.4
REMARK 620 4 HEM C 602 NC 90.0 179.4 89.1
REMARK 620 5 HEM C 602 ND 90.0 89.1 179.4 91.5
REMARK 620 6 HIS C 65 NE2 180.0 90.0 90.0 90.0 90.0
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 PLP B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JBQ RELATED DB: PDB
REMARK 900 RELATED ID: 4L0D RELATED DB: PDB
REMARK 900 RELATED ID: 4L27 RELATED DB: PDB
REMARK 900 RELATED ID: 4L28 RELATED DB: PDB
DBREF 4L3V B 2 551 UNP P35520 CBS_HUMAN 2 551
DBREF 4L3V A 2 551 UNP P35520 CBS_HUMAN 2 551
DBREF 4L3V C 2 551 UNP P35520 CBS_HUMAN 2 551
SEQRES 1 B 550 PRO SER GLU THR PRO GLN ALA GLU VAL GLY PRO THR GLY
SEQRES 2 B 550 CYS PRO HIS ARG SER GLY PRO HIS SER ALA LYS GLY SER
SEQRES 3 B 550 LEU GLU LYS GLY SER PRO GLU ASP LYS GLU ALA LYS GLU
SEQRES 4 B 550 PRO LEU TRP ILE ARG PRO ASP ALA PRO SER ARG CYS THR
SEQRES 5 B 550 TRP GLN LEU GLY ARG PRO ALA SER GLU SER PRO HIS HIS
SEQRES 6 B 550 HIS THR ALA PRO ALA LYS SER PRO LYS ILE LEU PRO ASP
SEQRES 7 B 550 ILE LEU LYS LYS ILE GLY ASP THR PRO MET VAL ARG ILE
SEQRES 8 B 550 ASN LYS ILE GLY LYS LYS PHE GLY LEU LYS CYS GLU LEU
SEQRES 9 B 550 LEU ALA LYS CYS GLU PHE PHE ASN ALA GLY GLY SER VAL
SEQRES 10 B 550 LYS ASP ARG ILE SER LEU ARG MET ILE GLU ASP ALA GLU
SEQRES 11 B 550 ARG ASP GLY THR LEU LYS PRO GLY ASP THR ILE ILE GLU
SEQRES 12 B 550 PRO THR SER GLY ASN THR GLY ILE GLY LEU ALA LEU ALA
SEQRES 13 B 550 ALA ALA VAL ARG GLY TYR ARG CYS ILE ILE VAL MET PRO
SEQRES 14 B 550 GLU LYS MET SER SER GLU LYS VAL ASP VAL LEU ARG ALA
SEQRES 15 B 550 LEU GLY ALA GLU ILE VAL ARG THR PRO THR ASN ALA ARG
SEQRES 16 B 550 PHE ASP SER PRO GLU SER HIS VAL GLY VAL ALA TRP ARG
SEQRES 17 B 550 LEU LYS ASN GLU ILE PRO ASN SER HIS ILE LEU ASP GLN
SEQRES 18 B 550 TYR ARG ASN ALA SER ASN PRO LEU ALA HIS TYR ASP THR
SEQRES 19 B 550 THR ALA ASP GLU ILE LEU GLN GLN CYS ASP GLY LYS LEU
SEQRES 20 B 550 ASP MET LEU VAL ALA SER VAL GLY THR GLY GLY THR ILE
SEQRES 21 B 550 THR GLY ILE ALA ARG LYS LEU LYS GLU LYS CYS PRO GLY
SEQRES 22 B 550 CYS ARG ILE ILE GLY VAL ASP PRO GLU GLY SER ILE LEU
SEQRES 23 B 550 ALA GLU PRO GLU GLU LEU ASN GLN THR GLU GLN THR THR
SEQRES 24 B 550 TYR GLU VAL GLU GLY ILE GLY TYR ASP PHE ILE PRO THR
SEQRES 25 B 550 VAL LEU ASP ARG THR VAL VAL ASP LYS TRP PHE LYS SER
SEQRES 26 B 550 ASN ASP GLU GLU ALA PHE THR PHE ALA ARG MET LEU ILE
SEQRES 27 B 550 ALA GLN GLU GLY LEU LEU CYS GLY GLY SER ALA GLY SER
SEQRES 28 B 550 THR VAL ALA VAL ALA VAL LYS ALA ALA GLN GLU LEU GLN
SEQRES 29 B 550 GLU GLY GLN ARG CYS VAL VAL ILE LEU PRO ASP SER VAL
SEQRES 30 B 550 ARG ASN TYR MET THR LYS PHE LEU SER ASP ARG TRP MET
SEQRES 31 B 550 LEU GLN LYS GLY PHE LEU LYS GLU GLU ASP LEU THR GLU
SEQRES 32 B 550 LYS LYS PRO TRP TRP TRP HIS LEU ARG VAL GLN GLU LEU
SEQRES 33 B 550 GLY LEU SER ALA PRO LEU THR VAL LEU PRO THR ILE THR
SEQRES 34 B 550 CYS GLY HIS THR ILE GLU ILE LEU ARG GLU LYS GLY PHE
SEQRES 35 B 550 ASP GLN ALA PRO VAL VAL ASP GLU ALA GLY VAL ILE LEU
SEQRES 36 B 550 GLY MET VAL THR LEU GLY ASN MET LEU SER SER LEU LEU
SEQRES 37 B 550 ALA GLY LYS VAL GLN PRO SER ASP GLN VAL GLY LYS VAL
SEQRES 38 B 550 ILE TYR LYS GLN PHE LYS GLN ILE ARG LEU THR ASP THR
SEQRES 39 B 550 LEU GLY ARG LEU SER HIS ILE LEU GLU MET ASP HIS PHE
SEQRES 40 B 550 ALA LEU VAL VAL HIS GLU GLN ILE GLN TYR HIS SER THR
SEQRES 41 B 550 GLY LYS SER SER GLN ARG GLN MET VAL PHE GLY VAL VAL
SEQRES 42 B 550 THR ALA ILE ASP LEU LEU ASN PHE VAL ALA ALA GLN GLU
SEQRES 43 B 550 ARG ASP GLN LYS
SEQRES 1 A 550 PRO SER GLU THR PRO GLN ALA GLU VAL GLY PRO THR GLY
SEQRES 2 A 550 CYS PRO HIS ARG SER GLY PRO HIS SER ALA LYS GLY SER
SEQRES 3 A 550 LEU GLU LYS GLY SER PRO GLU ASP LYS GLU ALA LYS GLU
SEQRES 4 A 550 PRO LEU TRP ILE ARG PRO ASP ALA PRO SER ARG CYS THR
SEQRES 5 A 550 TRP GLN LEU GLY ARG PRO ALA SER GLU SER PRO HIS HIS
SEQRES 6 A 550 HIS THR ALA PRO ALA LYS SER PRO LYS ILE LEU PRO ASP
SEQRES 7 A 550 ILE LEU LYS LYS ILE GLY ASP THR PRO MET VAL ARG ILE
SEQRES 8 A 550 ASN LYS ILE GLY LYS LYS PHE GLY LEU LYS CYS GLU LEU
SEQRES 9 A 550 LEU ALA LYS CYS GLU PHE PHE ASN ALA GLY GLY SER VAL
SEQRES 10 A 550 LYS ASP ARG ILE SER LEU ARG MET ILE GLU ASP ALA GLU
SEQRES 11 A 550 ARG ASP GLY THR LEU LYS PRO GLY ASP THR ILE ILE GLU
SEQRES 12 A 550 PRO THR SER GLY ASN THR GLY ILE GLY LEU ALA LEU ALA
SEQRES 13 A 550 ALA ALA VAL ARG GLY TYR ARG CYS ILE ILE VAL MET PRO
SEQRES 14 A 550 GLU LYS MET SER SER GLU LYS VAL ASP VAL LEU ARG ALA
SEQRES 15 A 550 LEU GLY ALA GLU ILE VAL ARG THR PRO THR ASN ALA ARG
SEQRES 16 A 550 PHE ASP SER PRO GLU SER HIS VAL GLY VAL ALA TRP ARG
SEQRES 17 A 550 LEU LYS ASN GLU ILE PRO ASN SER HIS ILE LEU ASP GLN
SEQRES 18 A 550 TYR ARG ASN ALA SER ASN PRO LEU ALA HIS TYR ASP THR
SEQRES 19 A 550 THR ALA ASP GLU ILE LEU GLN GLN CYS ASP GLY LYS LEU
SEQRES 20 A 550 ASP MET LEU VAL ALA SER VAL GLY THR GLY GLY THR ILE
SEQRES 21 A 550 THR GLY ILE ALA ARG LYS LEU LYS GLU LYS CYS PRO GLY
SEQRES 22 A 550 CYS ARG ILE ILE GLY VAL ASP PRO GLU GLY SER ILE LEU
SEQRES 23 A 550 ALA GLU PRO GLU GLU LEU ASN GLN THR GLU GLN THR THR
SEQRES 24 A 550 TYR GLU VAL GLU GLY ILE GLY TYR ASP PHE ILE PRO THR
SEQRES 25 A 550 VAL LEU ASP ARG THR VAL VAL ASP LYS TRP PHE LYS SER
SEQRES 26 A 550 ASN ASP GLU GLU ALA PHE THR PHE ALA ARG MET LEU ILE
SEQRES 27 A 550 ALA GLN GLU GLY LEU LEU CYS GLY GLY SER ALA GLY SER
SEQRES 28 A 550 THR VAL ALA VAL ALA VAL LYS ALA ALA GLN GLU LEU GLN
SEQRES 29 A 550 GLU GLY GLN ARG CYS VAL VAL ILE LEU PRO ASP SER VAL
SEQRES 30 A 550 ARG ASN TYR MET THR LYS PHE LEU SER ASP ARG TRP MET
SEQRES 31 A 550 LEU GLN LYS GLY PHE LEU LYS GLU GLU ASP LEU THR GLU
SEQRES 32 A 550 LYS LYS PRO TRP TRP TRP HIS LEU ARG VAL GLN GLU LEU
SEQRES 33 A 550 GLY LEU SER ALA PRO LEU THR VAL LEU PRO THR ILE THR
SEQRES 34 A 550 CYS GLY HIS THR ILE GLU ILE LEU ARG GLU LYS GLY PHE
SEQRES 35 A 550 ASP GLN ALA PRO VAL VAL ASP GLU ALA GLY VAL ILE LEU
SEQRES 36 A 550 GLY MET VAL THR LEU GLY ASN MET LEU SER SER LEU LEU
SEQRES 37 A 550 ALA GLY LYS VAL GLN PRO SER ASP GLN VAL GLY LYS VAL
SEQRES 38 A 550 ILE TYR LYS GLN PHE LYS GLN ILE ARG LEU THR ASP THR
SEQRES 39 A 550 LEU GLY ARG LEU SER HIS ILE LEU GLU MET ASP HIS PHE
SEQRES 40 A 550 ALA LEU VAL VAL HIS GLU GLN ILE GLN TYR HIS SER THR
SEQRES 41 A 550 GLY LYS SER SER GLN ARG GLN MET VAL PHE GLY VAL VAL
SEQRES 42 A 550 THR ALA ILE ASP LEU LEU ASN PHE VAL ALA ALA GLN GLU
SEQRES 43 A 550 ARG ASP GLN LYS
SEQRES 1 C 550 PRO SER GLU THR PRO GLN ALA GLU VAL GLY PRO THR GLY
SEQRES 2 C 550 CYS PRO HIS ARG SER GLY PRO HIS SER ALA LYS GLY SER
SEQRES 3 C 550 LEU GLU LYS GLY SER PRO GLU ASP LYS GLU ALA LYS GLU
SEQRES 4 C 550 PRO LEU TRP ILE ARG PRO ASP ALA PRO SER ARG CYS THR
SEQRES 5 C 550 TRP GLN LEU GLY ARG PRO ALA SER GLU SER PRO HIS HIS
SEQRES 6 C 550 HIS THR ALA PRO ALA LYS SER PRO LYS ILE LEU PRO ASP
SEQRES 7 C 550 ILE LEU LYS LYS ILE GLY ASP THR PRO MET VAL ARG ILE
SEQRES 8 C 550 ASN LYS ILE GLY LYS LYS PHE GLY LEU LYS CYS GLU LEU
SEQRES 9 C 550 LEU ALA LYS CYS GLU PHE PHE ASN ALA GLY GLY SER VAL
SEQRES 10 C 550 LYS ASP ARG ILE SER LEU ARG MET ILE GLU ASP ALA GLU
SEQRES 11 C 550 ARG ASP GLY THR LEU LYS PRO GLY ASP THR ILE ILE GLU
SEQRES 12 C 550 PRO THR SER GLY ASN THR GLY ILE GLY LEU ALA LEU ALA
SEQRES 13 C 550 ALA ALA VAL ARG GLY TYR ARG CYS ILE ILE VAL MET PRO
SEQRES 14 C 550 GLU LYS MET SER SER GLU LYS VAL ASP VAL LEU ARG ALA
SEQRES 15 C 550 LEU GLY ALA GLU ILE VAL ARG THR PRO THR ASN ALA ARG
SEQRES 16 C 550 PHE ASP SER PRO GLU SER HIS VAL GLY VAL ALA TRP ARG
SEQRES 17 C 550 LEU LYS ASN GLU ILE PRO ASN SER HIS ILE LEU ASP GLN
SEQRES 18 C 550 TYR ARG ASN ALA SER ASN PRO LEU ALA HIS TYR ASP THR
SEQRES 19 C 550 THR ALA ASP GLU ILE LEU GLN GLN CYS ASP GLY LYS LEU
SEQRES 20 C 550 ASP MET LEU VAL ALA SER VAL GLY THR GLY GLY THR ILE
SEQRES 21 C 550 THR GLY ILE ALA ARG LYS LEU LYS GLU LYS CYS PRO GLY
SEQRES 22 C 550 CYS ARG ILE ILE GLY VAL ASP PRO GLU GLY SER ILE LEU
SEQRES 23 C 550 ALA GLU PRO GLU GLU LEU ASN GLN THR GLU GLN THR THR
SEQRES 24 C 550 TYR GLU VAL GLU GLY ILE GLY TYR ASP PHE ILE PRO THR
SEQRES 25 C 550 VAL LEU ASP ARG THR VAL VAL ASP LYS TRP PHE LYS SER
SEQRES 26 C 550 ASN ASP GLU GLU ALA PHE THR PHE ALA ARG MET LEU ILE
SEQRES 27 C 550 ALA GLN GLU GLY LEU LEU CYS GLY GLY SER ALA GLY SER
SEQRES 28 C 550 THR VAL ALA VAL ALA VAL LYS ALA ALA GLN GLU LEU GLN
SEQRES 29 C 550 GLU GLY GLN ARG CYS VAL VAL ILE LEU PRO ASP SER VAL
SEQRES 30 C 550 ARG ASN TYR MET THR LYS PHE LEU SER ASP ARG TRP MET
SEQRES 31 C 550 LEU GLN LYS GLY PHE LEU LYS GLU GLU ASP LEU THR GLU
SEQRES 32 C 550 LYS LYS PRO TRP TRP TRP HIS LEU ARG VAL GLN GLU LEU
SEQRES 33 C 550 GLY LEU SER ALA PRO LEU THR VAL LEU PRO THR ILE THR
SEQRES 34 C 550 CYS GLY HIS THR ILE GLU ILE LEU ARG GLU LYS GLY PHE
SEQRES 35 C 550 ASP GLN ALA PRO VAL VAL ASP GLU ALA GLY VAL ILE LEU
SEQRES 36 C 550 GLY MET VAL THR LEU GLY ASN MET LEU SER SER LEU LEU
SEQRES 37 C 550 ALA GLY LYS VAL GLN PRO SER ASP GLN VAL GLY LYS VAL
SEQRES 38 C 550 ILE TYR LYS GLN PHE LYS GLN ILE ARG LEU THR ASP THR
SEQRES 39 C 550 LEU GLY ARG LEU SER HIS ILE LEU GLU MET ASP HIS PHE
SEQRES 40 C 550 ALA LEU VAL VAL HIS GLU GLN ILE GLN TYR HIS SER THR
SEQRES 41 C 550 GLY LYS SER SER GLN ARG GLN MET VAL PHE GLY VAL VAL
SEQRES 42 C 550 THR ALA ILE ASP LEU LEU ASN PHE VAL ALA ALA GLN GLU
SEQRES 43 C 550 ARG ASP GLN LYS
HET PLP B 601 15
HET HEM B 602 43
HET PLP A 601 15
HET HEM A 602 43
HET PLP C 601 15
HET HEM C 602 43
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN PLP VITAMIN B6 PHOSPHATE
HETSYN HEM HEME
FORMUL 4 PLP 3(C8 H10 N O6 P)
FORMUL 5 HEM 3(C34 H32 FE N4 O4)
HELIX 1 1 PRO B 59 SER B 63 5 5
HELIX 2 2 ASP B 79 ILE B 84 5 6
HELIX 3 3 LYS B 94 PHE B 99 1 6
HELIX 4 4 PHE B 111 ASN B 113 5 3
HELIX 5 5 VAL B 118 ASP B 133 1 16
HELIX 6 6 GLY B 148 GLY B 162 1 15
HELIX 7 7 SER B 174 GLY B 185 1 12
HELIX 8 8 SER B 202 ILE B 214 1 13
HELIX 9 9 ALA B 226 THR B 235 1 10
HELIX 10 10 THR B 235 CYS B 244 1 10
HELIX 11 11 GLY B 258 CYS B 272 1 15
HELIX 12 12 PRO B 290 GLN B 295 5 6
HELIX 13 13 ASN B 327 GLN B 341 1 15
HELIX 14 14 GLY B 347 ALA B 361 1 15
HELIX 15 15 GLN B 362 LEU B 364 5 3
HELIX 16 16 SER B 377 MET B 382 5 6
HELIX 17 17 SER B 387 LYS B 394 1 8
HELIX 18 18 LYS B 398 LYS B 406 1 9
HELIX 19 19 PRO B 407 HIS B 411 5 5
HELIX 20 20 ARG B 413 GLY B 418 5 6
HELIX 21 21 THR B 430 GLY B 442 1 13
HELIX 22 22 LEU B 461 ALA B 470 1 10
HELIX 23 23 GLN B 478 ILE B 483 5 6
HELIX 24 24 THR B 495 GLU B 504 1 10
HELIX 25 25 THR B 535 ARG B 548 1 14
HELIX 26 26 PRO A 59 SER A 63 5 5
HELIX 27 27 ASP A 79 ILE A 84 5 6
HELIX 28 28 ASN A 93 PHE A 99 1 7
HELIX 29 29 PHE A 111 ASN A 113 5 3
HELIX 30 30 VAL A 118 ASP A 133 1 16
HELIX 31 31 GLY A 148 GLY A 162 1 15
HELIX 32 32 SER A 174 GLY A 185 1 12
HELIX 33 33 SER A 202 ILE A 214 1 13
HELIX 34 34 ALA A 226 THR A 235 1 10
HELIX 35 35 THR A 235 CYS A 244 1 10
HELIX 36 36 GLY A 258 CYS A 272 1 15
HELIX 37 37 PRO A 290 GLN A 295 5 6
HELIX 38 38 ASN A 327 GLY A 343 1 17
HELIX 39 39 GLY A 347 ALA A 361 1 15
HELIX 40 40 GLN A 362 LEU A 364 5 3
HELIX 41 41 SER A 377 MET A 382 5 6
HELIX 42 42 SER A 387 LYS A 394 1 8
HELIX 43 43 LYS A 398 LYS A 406 1 9
HELIX 44 44 PRO A 407 HIS A 411 5 5
HELIX 45 45 ARG A 413 GLY A 418 5 6
HELIX 46 46 THR A 430 GLY A 442 1 13
HELIX 47 47 LEU A 461 ALA A 470 1 10
HELIX 48 48 GLN A 478 ILE A 483 5 6
HELIX 49 49 THR A 495 LEU A 503 1 9
HELIX 50 50 THR A 535 ARG A 548 1 14
HELIX 51 51 ASP C 79 ILE C 84 5 6
HELIX 52 52 LYS C 94 PHE C 99 1 6
HELIX 53 53 PHE C 111 ASN C 113 5 3
HELIX 54 54 VAL C 118 ASP C 133 1 16
HELIX 55 55 GLY C 148 GLY C 162 1 15
HELIX 56 56 SER C 174 GLY C 185 1 12
HELIX 57 57 SER C 202 ILE C 214 1 13
HELIX 58 58 ALA C 226 THR C 235 1 10
HELIX 59 59 THR C 235 CYS C 244 1 10
HELIX 60 60 GLY C 258 CYS C 272 1 15
HELIX 61 61 PRO C 290 GLN C 295 5 6
HELIX 62 62 ASN C 327 GLY C 343 1 17
HELIX 63 63 GLY C 347 ALA C 361 1 15
HELIX 64 64 GLN C 362 LEU C 364 5 3
HELIX 65 65 SER C 377 MET C 382 5 6
HELIX 66 66 SER C 387 LYS C 394 1 8
HELIX 67 67 LYS C 398 LYS C 406 1 9
HELIX 68 68 PRO C 407 HIS C 411 5 5
HELIX 69 69 ARG C 413 GLY C 418 5 6
HELIX 70 70 THR C 430 GLY C 442 1 13
HELIX 71 71 LEU C 461 ALA C 470 1 10
HELIX 72 72 GLN C 478 ILE C 483 5 6
HELIX 73 73 THR C 495 GLU C 504 1 10
HELIX 74 74 THR C 535 ARG C 548 1 14
SHEET 1 A 6 MET B 89 ARG B 91 0
SHEET 2 A 6 GLU B 104 CYS B 109 -1 O ALA B 107 N VAL B 90
SHEET 3 A 6 ARG B 369 LEU B 374 1 O CYS B 370 N GLU B 104
SHEET 4 A 6 MET B 250 SER B 254 1 N MET B 250 O VAL B 371
SHEET 5 A 6 ARG B 276 PRO B 282 1 O ILE B 278 N LEU B 251
SHEET 6 A 6 LYS B 322 SER B 326 1 O PHE B 324 N ASP B 281
SHEET 1 B 4 GLU B 187 THR B 191 0
SHEET 2 B 4 ARG B 164 PRO B 170 1 N ILE B 167 O GLU B 187
SHEET 3 B 4 THR B 141 PRO B 145 1 N ILE B 142 O ILE B 166
SHEET 4 B 4 SER B 217 ILE B 219 1 O HIS B 218 N ILE B 143
SHEET 1 C 2 GLN B 445 VAL B 449 0
SHEET 2 C 2 ILE B 455 THR B 460 -1 O VAL B 459 N ALA B 446
SHEET 1 D 3 LYS B 488 ILE B 490 0
SHEET 2 D 3 ALA B 509 VAL B 512 1 O LEU B 510 N LYS B 488
SHEET 3 D 3 VAL B 530 VAL B 534 -1 O VAL B 534 N ALA B 509
SHEET 1 E 7 ILE A 76 LEU A 77 0
SHEET 2 E 7 MET C 89 ARG C 91 1 O MET C 89 N LEU A 77
SHEET 3 E 7 GLU C 104 CYS C 109 -1 O ALA C 107 N VAL C 90
SHEET 4 E 7 ARG C 369 LEU C 374 1 O CYS C 370 N LEU C 106
SHEET 5 E 7 MET C 250 SER C 254 1 N MET C 250 O VAL C 371
SHEET 6 E 7 ARG C 276 PRO C 282 1 O ARG C 276 N LEU C 251
SHEET 7 E 7 LYS C 322 SER C 326 1 O PHE C 324 N ASP C 281
SHEET 1 F 7 LYS A 322 SER A 326 0
SHEET 2 F 7 ARG A 276 PRO A 282 1 N ASP A 281 O PHE A 324
SHEET 3 F 7 MET A 250 SER A 254 1 N LEU A 251 O ILE A 278
SHEET 4 F 7 ARG A 369 LEU A 374 1 O VAL A 371 N MET A 250
SHEET 5 F 7 GLU A 104 CYS A 109 1 N LYS A 108 O VAL A 372
SHEET 6 F 7 MET A 89 ARG A 91 -1 N VAL A 90 O ALA A 107
SHEET 7 F 7 ILE C 76 LEU C 77 1 O LEU C 77 N MET A 89
SHEET 1 G 4 GLU A 187 THR A 191 0
SHEET 2 G 4 ARG A 164 PRO A 170 1 N ILE A 167 O GLU A 187
SHEET 3 G 4 THR A 141 PRO A 145 1 N GLU A 144 O VAL A 168
SHEET 4 G 4 SER A 217 ILE A 219 1 O HIS A 218 N ILE A 143
SHEET 1 H 2 GLN A 445 VAL A 449 0
SHEET 2 H 2 ILE A 455 THR A 460 -1 O VAL A 459 N ALA A 446
SHEET 1 I 3 LYS A 488 ILE A 490 0
SHEET 2 I 3 ALA A 509 VAL A 512 1 O LEU A 510 N LYS A 488
SHEET 3 I 3 VAL A 530 VAL A 534 -1 O PHE A 531 N VAL A 511
SHEET 1 J 4 GLU C 187 THR C 191 0
SHEET 2 J 4 ARG C 164 PRO C 170 1 N CYS C 165 O GLU C 187
SHEET 3 J 4 THR C 141 PRO C 145 1 N ILE C 142 O ILE C 166
SHEET 4 J 4 SER C 217 ILE C 219 1 O HIS C 218 N ILE C 143
SHEET 1 K 2 GLN C 445 VAL C 449 0
SHEET 2 K 2 ILE C 455 THR C 460 -1 O VAL C 459 N ALA C 446
SHEET 1 L 3 LYS C 488 ILE C 490 0
SHEET 2 L 3 ALA C 509 VAL C 512 1 O LEU C 510 N LYS C 488
SHEET 3 L 3 VAL C 530 VAL C 534 -1 O VAL C 534 N ALA C 509
LINK NZ LYS B 119 C4A PLP B 601 1555 1555 1.36
LINK NZ LYS A 119 C4A PLP A 601 1555 1555 1.35
LINK NZ LYS C 119 C4A PLP C 601 1555 1555 1.36
LINK SG CYS B 52 FE HEM B 602 1555 1555 2.23
LINK NE2 HIS B 65 FE HEM B 602 1555 1555 2.05
LINK SG CYS A 52 FE HEM A 602 1555 1555 2.27
LINK NE2 HIS A 65 FE HEM A 602 1555 1555 2.06
LINK SG CYS C 52 FE HEM C 602 1555 1555 2.27
LINK NE2 HIS C 65 FE HEM C 602 1555 1555 2.10
CISPEP 1 GLU B 289 PRO B 290 0 -1.86
CISPEP 2 GLU A 289 PRO A 290 0 -0.75
CISPEP 3 GLU C 289 PRO C 290 0 -1.79
SITE 1 AC1 15 LYS B 119 ASN B 149 SER B 254 VAL B 255
SITE 2 AC1 15 GLY B 256 THR B 257 GLY B 258 GLY B 259
SITE 3 AC1 15 THR B 260 GLY B 305 ILE B 306 SER B 349
SITE 4 AC1 15 PRO B 375 ASP B 376 TYR B 381
SITE 1 AC2 20 THR A 53 ARG A 58 HEM A 602 SER B 50
SITE 2 AC2 20 ARG B 51 CYS B 52 THR B 53 TRP B 54
SITE 3 AC2 20 ARG B 58 PRO B 59 GLU B 62 SER B 63
SITE 4 AC2 20 PRO B 64 HIS B 65 ARG B 224 ALA B 226
SITE 5 AC2 20 PRO B 229 TYR B 233 ARG B 266 THR B 313
SITE 1 AC3 14 LYS A 119 ASN A 149 SER A 254 VAL A 255
SITE 2 AC3 14 GLY A 256 THR A 257 GLY A 258 GLY A 259
SITE 3 AC3 14 THR A 260 GLY A 305 ILE A 306 SER A 349
SITE 4 AC3 14 PRO A 375 ASP A 376
SITE 1 AC4 20 SER A 50 ARG A 51 CYS A 52 THR A 53
SITE 2 AC4 20 TRP A 54 ARG A 58 PRO A 59 GLU A 62
SITE 3 AC4 20 SER A 63 PRO A 64 HIS A 65 ALA A 226
SITE 4 AC4 20 LEU A 230 TYR A 233 GLY A 263 ARG A 266
SITE 5 AC4 20 VAL A 314 THR B 53 ARG B 58 HEM B 602
SITE 1 AC5 15 LYS C 119 ASN C 149 SER C 254 VAL C 255
SITE 2 AC5 15 GLY C 256 THR C 257 GLY C 258 GLY C 259
SITE 3 AC5 15 THR C 260 GLY C 305 ILE C 306 SER C 349
SITE 4 AC5 15 PRO C 375 ASP C 376 TYR C 381
SITE 1 AC6 16 PRO C 49 ARG C 51 CYS C 52 THR C 53
SITE 2 AC6 16 TRP C 54 PRO C 59 GLU C 62 SER C 63
SITE 3 AC6 16 PRO C 64 HIS C 65 ARG C 224 ALA C 226
SITE 4 AC6 16 LEU C 230 GLY C 263 ARG C 266 VAL C 314
CRYST1 227.750 342.655 107.253 90.00 90.00 90.00 C 2 2 21 24
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 0.004391 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002918 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009324 0.00000
(ATOM LINES ARE NOT SHOWN.)
END