HEADER ELECTRON TRANSPORT 28-FEB-12 4DY9
TITLE LEISHMANIA MAJOR PEROXIDASE IS A CYTOCHROME C PEROXIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEISHMANIA MAJOR;
SOURCE 3 ORGANISM_TAXID: 5664;
SOURCE 4 GENE: LMJF_16_1310, LMJF_16_1320;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ALPHA HELICAL BUNDLE, ELECTRON TRANSPORT, HEME PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR V.S.JASION,T.L.POULOS
REVDAT 5 03-APR-24 4DY9 1 REMARK
REVDAT 4 28-FEB-24 4DY9 1 REMARK
REVDAT 3 15-NOV-17 4DY9 1 REMARK
REVDAT 2 11-APR-12 4DY9 1 JRNL
REVDAT 1 14-MAR-12 4DY9 0
JRNL AUTH V.S.JASION,T.L.POULOS
JRNL TITL LEISHMANIA MAJOR PEROXIDASE IS A CYTOCHROME C PEROXIDASE.
JRNL REF BIOCHEMISTRY V. 51 2453 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 22372542
JRNL DOI 10.1021/BI300169X
REMARK 2
REMARK 2 RESOLUTION. 2.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 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) : 2.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 6330
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.640
REMARK 3 FREE R VALUE TEST SET COUNT : 294
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 22.0012 - 2.6220 0.99 3100 150 0.1682 0.2064
REMARK 3 2 2.6220 - 2.0820 0.99 2936 144 0.1461 0.2239
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 44.57
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.660
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05270
REMARK 3 B22 (A**2) : -2.34280
REMARK 3 B33 (A**2) : 2.29020
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 : 0.007 890
REMARK 3 ANGLE : 1.214 1215
REMARK 3 CHIRALITY : 0.078 120
REMARK 3 PLANARITY : 0.005 155
REMARK 3 DIHEDRAL : 13.669 328
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 6:13)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.9067 -8.2394 20.9832
REMARK 3 T TENSOR
REMARK 3 T11: 0.0145 T22: 0.2032
REMARK 3 T33: 0.1941 T12: 0.0265
REMARK 3 T13: -0.0765 T23: 0.0571
REMARK 3 L TENSOR
REMARK 3 L11: 0.3009 L22: 0.1684
REMARK 3 L33: 0.7205 L12: 0.2206
REMARK 3 L13: 0.0592 L23: -0.0372
REMARK 3 S TENSOR
REMARK 3 S11: 0.0188 S12: -0.0621 S13: 0.0611
REMARK 3 S21: 0.1402 S22: 0.1539 S23: -0.1110
REMARK 3 S31: 0.0618 S32: 0.1395 S33: 0.0742
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 14:24)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6658 4.1167 11.6471
REMARK 3 T TENSOR
REMARK 3 T11: 0.0645 T22: 0.0868
REMARK 3 T33: 0.1101 T12: 0.0185
REMARK 3 T13: -0.0155 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 0.4346 L22: 0.1619
REMARK 3 L33: 0.0358 L12: 0.2516
REMARK 3 L13: 0.0353 L23: 0.0401
REMARK 3 S TENSOR
REMARK 3 S11: 0.0234 S12: 0.2422 S13: 0.2155
REMARK 3 S21: -0.0308 S22: 0.1351 S23: 0.0267
REMARK 3 S31: 0.0159 S32: 0.0642 S33: 0.0061
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 25:44)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.6919 1.8043 4.4567
REMARK 3 T TENSOR
REMARK 3 T11: 0.0919 T22: 0.0851
REMARK 3 T33: 0.0783 T12: -0.0254
REMARK 3 T13: -0.0166 T23: 0.0483
REMARK 3 L TENSOR
REMARK 3 L11: 0.7068 L22: 0.3454
REMARK 3 L33: 0.1799 L12: -0.4908
REMARK 3 L13: -0.3348 L23: 0.2260
REMARK 3 S TENSOR
REMARK 3 S11: 0.0137 S12: 0.1060 S13: 0.3469
REMARK 3 S21: -0.0098 S22: 0.1020 S23: 0.0605
REMARK 3 S31: 0.0341 S32: 0.0860 S33: 0.1382
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 45:49)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3794 -11.0635 6.0226
REMARK 3 T TENSOR
REMARK 3 T11: 0.2146 T22: 0.1178
REMARK 3 T33: 0.0897 T12: 0.0242
REMARK 3 T13: -0.0635 T23: -0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 0.1346 L22: 0.1650
REMARK 3 L33: 0.0007 L12: -0.1491
REMARK 3 L13: -0.0087 L23: 0.0100
REMARK 3 S TENSOR
REMARK 3 S11: 0.0933 S12: 0.2183 S13: 0.0979
REMARK 3 S21: -0.0825 S22: 0.0310 S23: -0.0610
REMARK 3 S31: 0.0489 S32: 0.0334 S33: 0.0055
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 50:71)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3501 -8.7586 8.6896
REMARK 3 T TENSOR
REMARK 3 T11: 0.1004 T22: 0.0795
REMARK 3 T33: 0.1180 T12: 0.0177
REMARK 3 T13: 0.0234 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.2173 L22: 0.0854
REMARK 3 L33: 0.2151 L12: 0.1331
REMARK 3 L13: 0.1181 L23: 0.0775
REMARK 3 S TENSOR
REMARK 3 S11: 0.0275 S12: -0.0480 S13: -0.2331
REMARK 3 S21: -0.1257 S22: 0.0091 S23: -0.2128
REMARK 3 S31: 0.1140 S32: 0.1117 S33: 0.0233
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 72:80)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.7462 -8.4438 18.3502
REMARK 3 T TENSOR
REMARK 3 T11: 0.0910 T22: 0.1099
REMARK 3 T33: 0.1147 T12: 0.0259
REMARK 3 T13: 0.0233 T23: 0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 0.0006 L22: 0.0154
REMARK 3 L33: 0.0046 L12: 0.0008
REMARK 3 L13: -0.0011 L23: -0.0082
REMARK 3 S TENSOR
REMARK 3 S11: -0.0309 S12: -0.1851 S13: -0.0829
REMARK 3 S21: 0.0193 S22: -0.0338 S23: 0.0638
REMARK 3 S31: -0.0225 S32: 0.0334 S33: -0.0028
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 81:85)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.8974 -5.4583 22.8776
REMARK 3 T TENSOR
REMARK 3 T11: 0.0855 T22: 0.1029
REMARK 3 T33: 0.1347 T12: -0.0065
REMARK 3 T13: -0.0321 T23: 0.0390
REMARK 3 L TENSOR
REMARK 3 L11: 0.1564 L22: 0.1470
REMARK 3 L33: 0.0961 L12: 0.1146
REMARK 3 L13: -0.0459 L23: -0.1049
REMARK 3 S TENSOR
REMARK 3 S11: 0.0361 S12: -0.0535 S13: 0.0896
REMARK 3 S21: -0.0013 S22: 0.0241 S23: -0.0461
REMARK 3 S31: -0.1913 S32: 0.0919 S33: 0.0177
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 86:113)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.8238 -2.4136 15.6188
REMARK 3 T TENSOR
REMARK 3 T11: 0.0678 T22: 0.0942
REMARK 3 T33: 0.0752 T12: -0.0153
REMARK 3 T13: 0.0081 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 0.2044 L22: 0.1257
REMARK 3 L33: 0.1398 L12: 0.0417
REMARK 3 L13: -0.0305 L23: -0.1419
REMARK 3 S TENSOR
REMARK 3 S11: -0.0544 S12: -0.1691 S13: -0.1121
REMARK 3 S21: -0.0274 S22: 0.0130 S23: 0.0752
REMARK 3 S31: -0.0058 S32: 0.0050 S33: -0.0007
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 4DY9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000070933.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.4
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) : 1.54
REMARK 200 MONOCHROMATOR : VARIMAX OPTIC
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6330
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080
REMARK 200 RESOLUTION RANGE LOW (A) : 36.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : 0.04300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 64.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.06800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 38.60
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: YEAST CYTOCHROME C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2K MME, POTASSIUM BROMIDE, PH 6.4,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 17.64000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.18950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 32.18950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.64000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 22.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 MET A 1
REMARK 465 PRO A 2
REMARK 465 PRO A 3
REMARK 465 LYS A 4
REMARK 465 ALA A 5
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 NE ARG A 49 O HOH A 347 1.97
REMARK 500 O HOH A 353 O HOH A 369 2.13
REMARK 500 O HOH A 359 O HOH A 376 2.13
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 ASN A 81 85.56 -162.57
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 A 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 29 NE2
REMARK 620 2 HEM A 201 NA 91.8
REMARK 620 3 HEM A 201 NB 91.0 91.1
REMARK 620 4 HEM A 201 NC 86.4 177.7 87.5
REMARK 620 5 HEM A 201 ND 88.1 89.3 179.0 91.9
REMARK 620 6 MET A 91 SD 173.1 82.7 93.3 99.2 87.6
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 HEM A 201
DBREF 4DY9 A 1 113 UNP Q4QEN5 Q4QEN5_LEIMA 1 113
SEQRES 1 A 113 MET PRO PRO LYS ALA ARG ALA PRO LEU PRO PRO GLY ASP
SEQRES 2 A 113 VAL GLU ARG GLY GLU LYS LEU PHE LYS GLY ARG ALA ALA
SEQRES 3 A 113 GLN CYS HIS THR ALA THR LYS GLY GLY SER ASN GLY VAL
SEQRES 4 A 113 GLY PRO ASN LEU PHE GLY ILE VAL ASN ARG PRO SER GLY
SEQRES 5 A 113 LYS VAL GLU GLY PHE THR TYR SER LYS ALA ASN ALA GLU
SEQRES 6 A 113 SER GLY VAL ILE TRP THR PRO GLU VAL LEU ASP VAL TYR
SEQRES 7 A 113 LEU GLU ASN PRO LYS LYS PHE MET PRO GLY THR LYS MET
SEQRES 8 A 113 SER PHE ALA GLY ILE LYS LYS PRO GLN GLU ARG ALA ASP
SEQRES 9 A 113 VAL ILE ALA TYR LEU GLU THR LEU LYS
HET HEM A 201 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 HOH *95(H2 O)
HELIX 1 1 ASP A 13 ALA A 25 1 13
HELIX 2 2 SER A 60 GLU A 65 1 6
HELIX 3 3 THR A 71 ASN A 81 1 11
HELIX 4 4 ASN A 81 MET A 86 1 6
HELIX 5 5 LYS A 98 THR A 111 1 14
LINK NE2 HIS A 29 FE HEM A 201 1555 1555 2.03
LINK SD MET A 91 FE HEM A 201 1555 1555 2.40
SITE 1 AC1 22 ARG A 24 ALA A 25 GLN A 27 CYS A 28
SITE 2 AC1 22 HIS A 29 VAL A 39 ILE A 46 SER A 51
SITE 3 AC1 22 GLY A 52 PHE A 57 TYR A 59 SER A 60
SITE 4 AC1 22 ASN A 63 VAL A 68 TRP A 70 LEU A 79
SITE 5 AC1 22 THR A 89 LYS A 90 MET A 91 SER A 92
SITE 6 AC1 22 PHE A 93 HOH A 303
CRYST1 35.280 44.000 64.379 90.00 90.00 90.00 P 21 21 21 4
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 0.028345 0.000000 0.000000 0.00000
SCALE2 0.000000 0.022727 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015533 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
