HEADER OXYGEN TRANSPORT, OXYGEN STORAGE 15-MAY-11 3S1J
TITLE CRYSTAL STRUCTURE OF ACETATE-BOUND HELL'S GATE GLOBIN I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMOGLOBIN-LIKE FLAVOPROTEIN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: HELL'S GATE GLOBIN I;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHYLACIDIPHILUM INFERNORUM;
SOURCE 3 ORGANISM_COMMON: METHYLOKORUS INFERNORUM;
SOURCE 4 ORGANISM_TAXID: 481448;
SOURCE 5 STRAIN: V4;
SOURCE 6 GENE: HMP, MINF_1095;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2(DE3)PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-3A
KEYWDS GLOBIN, HEME, ACETATE-BOUND, AUTOXIDATION, OXYGEN TRANSPORT, OXYGEN
KEYWDS 2 STORAGE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.H.TEH,J.A.SAITO,A.BAHARUDDIN,J.R.TUCKERMAN,J.S.NEWHOUSE,M.KANBE,
AUTHOR 2 E.I.NEWHOUSE,R.A.RAHIM,F.FAVIER,C.DIDIERJEAN,E.H.S.SOUSA,M.B.STOTT,
AUTHOR 3 P.F.DUNFIELD,G.GONZALEZ,M.A.GILLES-GONZALEZ,N.NAJIMUDIN,M.ALAM
REVDAT 3 20-MAR-24 3S1J 1 REMARK SEQADV
REVDAT 2 13-MAR-13 3S1J 1 JRNL
REVDAT 1 21-SEP-11 3S1J 0
JRNL AUTH A.H.TEH,J.A.SAITO,A.BAHARUDDIN,J.R.TUCKERMAN,J.S.NEWHOUSE,
JRNL AUTH 2 M.KANBE,E.I.NEWHOUSE,R.A.RAHIM,F.FAVIER,C.DIDIERJEAN,
JRNL AUTH 3 E.H.S.SOUSA,M.B.STOTT,P.F.DUNFIELD,G.GONZALEZ,
JRNL AUTH 4 M.A.GILLES-GONZALEZ,N.NAJIMUDIN,M.ALAM
JRNL TITL HELL'S GATE GLOBIN I: AN ACID AND THERMOSTABLE BACTERIAL
JRNL TITL 2 HEMOGLOBIN RESEMBLING MAMMALIAN NEUROGLOBIN
JRNL REF FEBS LETT. V. 585 3250 2011
JRNL REFN ISSN 0014-5793
JRNL PMID 21925500
JRNL DOI 10.1016/J.FEBSLET.2011.09.002
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.1_743
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 59417
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1961
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 38.4889 - 4.3363 0.92 4110 130 0.1920 0.2188
REMARK 3 2 4.3363 - 3.4426 0.94 4039 131 0.1751 0.2078
REMARK 3 3 3.4426 - 3.0076 0.98 4144 145 0.2013 0.2245
REMARK 3 4 3.0076 - 2.7327 0.99 4199 148 0.2132 0.2115
REMARK 3 5 2.7327 - 2.5369 0.99 4193 146 0.2101 0.2469
REMARK 3 6 2.5369 - 2.3873 0.99 4183 142 0.2244 0.2920
REMARK 3 7 2.3873 - 2.2678 1.00 4166 144 0.2120 0.2474
REMARK 3 8 2.2678 - 2.1691 1.00 4222 141 0.2184 0.2378
REMARK 3 9 2.1691 - 2.0856 1.00 4195 149 0.2199 0.2373
REMARK 3 10 2.0856 - 2.0136 1.00 4176 136 0.2381 0.2842
REMARK 3 11 2.0136 - 1.9507 1.00 4155 140 0.2652 0.2558
REMARK 3 12 1.9507 - 1.8949 1.00 4184 144 0.3002 0.3005
REMARK 3 13 1.8949 - 1.8450 0.93 3844 142 0.3501 0.3592
REMARK 3 14 1.8450 - 1.8000 0.87 3646 123 0.3963 0.4043
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.06
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 49.06
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.580
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.930
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.95
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.97030
REMARK 3 B22 (A**2) : -1.72260
REMARK 3 B33 (A**2) : 3.69300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 3436
REMARK 3 ANGLE : 0.989 4699
REMARK 3 CHIRALITY : 0.068 495
REMARK 3 PLANARITY : 0.004 591
REMARK 3 DIHEDRAL : 15.622 1286
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 3S1J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAY-11.
REMARK 100 THE DEPOSITION ID IS D_1000065643.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : VARIMAX HF
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59437
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 38.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 2.930
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.01
REMARK 200 R MERGE FOR SHELL (I) : 0.26300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M AMMONIUM SULPHATE, 0.1M SODIUM
REMARK 280 ACETATE, PH 4.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 74.19750
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 74.19750
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 35.01700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.11250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.01700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.11250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 74.19750
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.01700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.11250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 74.19750
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 35.01700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 63.11250
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: 4780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 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
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: 4850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -74.19750
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 236 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 GLU A 133
REMARK 465 HIS A 134
REMARK 465 HIS A 135
REMARK 465 HIS A 136
REMARK 465 HIS A 137
REMARK 465 HIS A 138
REMARK 465 HIS A 139
REMARK 465 MET B 1
REMARK 465 GLU B 133
REMARK 465 HIS B 134
REMARK 465 HIS B 135
REMARK 465 HIS B 136
REMARK 465 HIS B 137
REMARK 465 HIS B 138
REMARK 465 HIS B 139
REMARK 465 MET C 1
REMARK 465 GLU C 133
REMARK 465 HIS C 134
REMARK 465 HIS C 135
REMARK 465 HIS C 136
REMARK 465 HIS C 137
REMARK 465 HIS C 138
REMARK 465 HIS C 139
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 FE HEM B 140 O ACT B 141 1.95
REMARK 500 FE HEM A 140 O ACT A 141 2.04
REMARK 500 NE2 HIS C 82 FE HEM C 140 2.05
REMARK 500 NE2 HIS B 82 FE HEM B 140 2.06
REMARK 500 FE HEM C 140 O ACT C 141 2.08
REMARK 500 NE2 HIS A 82 FE HEM A 140 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 140
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 141
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 140
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 141
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 142
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 143
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 140
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 141
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 142
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3S1I RELATED DB: PDB
REMARK 900 OXYGEN-BOUND
DBREF 3S1J A 1 133 UNP B3DUZ7 B3DUZ7_METI4 1 133
DBREF 3S1J B 1 133 UNP B3DUZ7 B3DUZ7_METI4 1 133
DBREF 3S1J C 1 133 UNP B3DUZ7 B3DUZ7_METI4 1 133
SEQADV 3S1J HIS A 134 UNP B3DUZ7 EXPRESSION TAG
SEQADV 3S1J HIS A 135 UNP B3DUZ7 EXPRESSION TAG
SEQADV 3S1J HIS A 136 UNP B3DUZ7 EXPRESSION TAG
SEQADV 3S1J HIS A 137 UNP B3DUZ7 EXPRESSION TAG
SEQADV 3S1J HIS A 138 UNP B3DUZ7 EXPRESSION TAG
SEQADV 3S1J HIS A 139 UNP B3DUZ7 EXPRESSION TAG
SEQADV 3S1J HIS B 134 UNP B3DUZ7 EXPRESSION TAG
SEQADV 3S1J HIS B 135 UNP B3DUZ7 EXPRESSION TAG
SEQADV 3S1J HIS B 136 UNP B3DUZ7 EXPRESSION TAG
SEQADV 3S1J HIS B 137 UNP B3DUZ7 EXPRESSION TAG
SEQADV 3S1J HIS B 138 UNP B3DUZ7 EXPRESSION TAG
SEQADV 3S1J HIS B 139 UNP B3DUZ7 EXPRESSION TAG
SEQADV 3S1J HIS C 134 UNP B3DUZ7 EXPRESSION TAG
SEQADV 3S1J HIS C 135 UNP B3DUZ7 EXPRESSION TAG
SEQADV 3S1J HIS C 136 UNP B3DUZ7 EXPRESSION TAG
SEQADV 3S1J HIS C 137 UNP B3DUZ7 EXPRESSION TAG
SEQADV 3S1J HIS C 138 UNP B3DUZ7 EXPRESSION TAG
SEQADV 3S1J HIS C 139 UNP B3DUZ7 EXPRESSION TAG
SEQRES 1 A 139 MET ILE ASP GLN LYS GLU LYS GLU LEU ILE LYS GLU SER
SEQRES 2 A 139 TRP LYS ARG ILE GLU PRO ASN LYS ASN GLU ILE GLY LEU
SEQRES 3 A 139 LEU PHE TYR ALA ASN LEU PHE LYS GLU GLU PRO THR VAL
SEQRES 4 A 139 SER VAL LEU PHE GLN ASN PRO ILE SER SER GLN SER ARG
SEQRES 5 A 139 LYS LEU MET GLN VAL LEU GLY ILE LEU VAL GLN GLY ILE
SEQRES 6 A 139 ASP ASN LEU GLU GLY LEU ILE PRO THR LEU GLN ASP LEU
SEQRES 7 A 139 GLY ARG ARG HIS LYS GLN TYR GLY VAL VAL ASP SER HIS
SEQRES 8 A 139 TYR PRO LEU VAL GLY ASP CYS LEU LEU LYS SER ILE GLN
SEQRES 9 A 139 GLU TYR LEU GLY GLN GLY PHE THR GLU GLU ALA LYS ALA
SEQRES 10 A 139 ALA TRP THR LYS VAL TYR GLY ILE ALA ALA GLN VAL MET
SEQRES 11 A 139 THR ALA GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 139 MET ILE ASP GLN LYS GLU LYS GLU LEU ILE LYS GLU SER
SEQRES 2 B 139 TRP LYS ARG ILE GLU PRO ASN LYS ASN GLU ILE GLY LEU
SEQRES 3 B 139 LEU PHE TYR ALA ASN LEU PHE LYS GLU GLU PRO THR VAL
SEQRES 4 B 139 SER VAL LEU PHE GLN ASN PRO ILE SER SER GLN SER ARG
SEQRES 5 B 139 LYS LEU MET GLN VAL LEU GLY ILE LEU VAL GLN GLY ILE
SEQRES 6 B 139 ASP ASN LEU GLU GLY LEU ILE PRO THR LEU GLN ASP LEU
SEQRES 7 B 139 GLY ARG ARG HIS LYS GLN TYR GLY VAL VAL ASP SER HIS
SEQRES 8 B 139 TYR PRO LEU VAL GLY ASP CYS LEU LEU LYS SER ILE GLN
SEQRES 9 B 139 GLU TYR LEU GLY GLN GLY PHE THR GLU GLU ALA LYS ALA
SEQRES 10 B 139 ALA TRP THR LYS VAL TYR GLY ILE ALA ALA GLN VAL MET
SEQRES 11 B 139 THR ALA GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 139 MET ILE ASP GLN LYS GLU LYS GLU LEU ILE LYS GLU SER
SEQRES 2 C 139 TRP LYS ARG ILE GLU PRO ASN LYS ASN GLU ILE GLY LEU
SEQRES 3 C 139 LEU PHE TYR ALA ASN LEU PHE LYS GLU GLU PRO THR VAL
SEQRES 4 C 139 SER VAL LEU PHE GLN ASN PRO ILE SER SER GLN SER ARG
SEQRES 5 C 139 LYS LEU MET GLN VAL LEU GLY ILE LEU VAL GLN GLY ILE
SEQRES 6 C 139 ASP ASN LEU GLU GLY LEU ILE PRO THR LEU GLN ASP LEU
SEQRES 7 C 139 GLY ARG ARG HIS LYS GLN TYR GLY VAL VAL ASP SER HIS
SEQRES 8 C 139 TYR PRO LEU VAL GLY ASP CYS LEU LEU LYS SER ILE GLN
SEQRES 9 C 139 GLU TYR LEU GLY GLN GLY PHE THR GLU GLU ALA LYS ALA
SEQRES 10 C 139 ALA TRP THR LYS VAL TYR GLY ILE ALA ALA GLN VAL MET
SEQRES 11 C 139 THR ALA GLU HIS HIS HIS HIS HIS HIS
HET HEM A 140 43
HET ACT A 141 4
HET HEM B 140 43
HET ACT B 141 4
HET SO4 B 142 5
HET SO4 B 143 5
HET HEM C 140 43
HET ACT C 141 4
HET SO4 C 142 5
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM ACT ACETATE ION
HETNAM SO4 SULFATE ION
HETSYN HEM HEME
FORMUL 4 HEM 3(C34 H32 FE N4 O4)
FORMUL 5 ACT 3(C2 H3 O2 1-)
FORMUL 8 SO4 3(O4 S 2-)
FORMUL 13 HOH *258(H2 O)
HELIX 1 1 ASP A 3 GLU A 18 1 16
HELIX 2 2 ASN A 20 GLU A 36 1 17
HELIX 3 3 THR A 38 PHE A 43 5 6
HELIX 4 4 PRO A 46 GLY A 64 1 19
HELIX 5 5 LEU A 71 TYR A 85 1 15
HELIX 6 6 SER A 90 GLY A 108 1 19
HELIX 7 7 THR A 112 ALA A 132 1 21
HELIX 8 8 ASP B 3 GLU B 18 1 16
HELIX 9 9 ASN B 20 GLU B 36 1 17
HELIX 10 10 PRO B 37 PHE B 43 5 7
HELIX 11 11 PRO B 46 GLY B 64 1 19
HELIX 12 12 LEU B 71 GLY B 86 1 16
HELIX 13 13 SER B 90 GLY B 108 1 19
HELIX 14 14 THR B 112 ALA B 132 1 21
HELIX 15 15 ASP C 3 GLU C 18 1 16
HELIX 16 16 ASN C 20 GLU C 36 1 17
HELIX 17 17 THR C 38 PHE C 43 5 6
HELIX 18 18 PRO C 46 GLY C 64 1 19
HELIX 19 19 LEU C 71 TYR C 85 1 15
HELIX 20 20 SER C 90 GLY C 108 1 19
HELIX 21 21 THR C 112 ALA C 132 1 21
SITE 1 AC1 20 ARG A 16 LEU A 42 PHE A 43 GLN A 44
SITE 2 AC1 20 ASN A 45 GLN A 50 LYS A 53 VAL A 57
SITE 3 AC1 20 LEU A 78 ARG A 81 HIS A 82 TYR A 85
SITE 4 AC1 20 VAL A 87 HIS A 91 TYR A 92 VAL A 95
SITE 5 AC1 20 TYR A 123 ACT A 141 HOH A 164 HOH A 171
SITE 1 AC2 3 TYR A 29 GLN A 50 HEM A 140
SITE 1 AC3 16 LEU B 42 PHE B 43 GLN B 44 ASN B 45
SITE 2 AC3 16 GLN B 50 LYS B 53 VAL B 57 LEU B 78
SITE 3 AC3 16 ARG B 81 HIS B 82 TYR B 85 VAL B 87
SITE 4 AC3 16 HIS B 91 VAL B 95 TYR B 123 ACT B 141
SITE 1 AC4 4 TYR B 29 PHE B 43 GLN B 50 HEM B 140
SITE 1 AC5 4 ASP B 89 TYR B 92 THR B 131 HOH B 199
SITE 1 AC6 2 GLY B 108 GLN B 109
SITE 1 AC7 17 LEU C 42 PHE C 43 GLN C 44 ASN C 45
SITE 2 AC7 17 GLN C 50 LYS C 53 VAL C 57 LEU C 78
SITE 3 AC7 17 ARG C 81 HIS C 82 TYR C 85 VAL C 87
SITE 4 AC7 17 HIS C 91 VAL C 95 TYR C 123 ACT C 141
SITE 5 AC7 17 HOH C 199
SITE 1 AC8 4 TYR C 29 PHE C 43 GLN C 50 HEM C 140
SITE 1 AC9 5 ARG B 16 VAL C 87 VAL C 88 ASP C 89
SITE 2 AC9 5 HOH C 230
CRYST1 70.034 126.225 148.395 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 0.014279 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007922 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006739 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
