HEADER OXIDOREDUCTASE 27-JAN-19 6NSZ
TITLE X-RAY REDUCED CATALASE 3 FROM N.CRASSA (0.526 MGY)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATALASE-3;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 1.11.1.6;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEUROSPORA CRASSA (STRAIN ATCC 24698 / 74-OR23-
SOURCE 3 1A / CBS 708.71 / DSM 1257 / FGSC 987);
SOURCE 4 ORGANISM_TAXID: 5141;
SOURCE 5 STRAIN: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
SOURCE 6 GENE: CAT-3, NCU00355;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCOLD I
KEYWDS X-RAY REDUCED, HEME, CATALASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ZARATE-ROMERO,E.RUDINO-PINERA,V.STOJANOFF
REVDAT 2 11-OCT-23 6NSZ 1 LINK
REVDAT 1 01-MAY-19 6NSZ 0
JRNL AUTH A.ZARATE-ROMERO,V.STOJANOFF,A.E.COHEN,W.HANSBERG,
JRNL AUTH 2 E.RUDINO-PINERA
JRNL TITL X-RAY DRIVEN REDUCTION OF CPD I OF CATALASE-3 FROM N. CRASSA
JRNL TITL 2 REVEALS DIFFERENTIAL SENSITIVITY OF ACTIVE SITES AND
JRNL TITL 3 FORMATION OF FERROUS STATE.
JRNL REF ARCH.BIOCHEM.BIOPHYS. V. 666 107 2019
JRNL REFN ESSN 1096-0384
JRNL PMID 30940570
JRNL DOI 10.1016/J.ABB.2019.03.020
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 160353
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 8043
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 29.5984 - 6.8090 0.95 5259 335 0.1384 0.1585
REMARK 3 2 6.8090 - 5.4153 0.97 5208 275 0.1431 0.1784
REMARK 3 3 5.4153 - 4.7340 0.96 5172 230 0.1243 0.1492
REMARK 3 4 4.7340 - 4.3026 0.96 5122 257 0.1216 0.1450
REMARK 3 5 4.3026 - 3.9950 0.97 5102 268 0.1220 0.1598
REMARK 3 6 3.9950 - 3.7599 0.97 5061 291 0.1265 0.1560
REMARK 3 7 3.7599 - 3.5719 0.97 5073 292 0.1416 0.1909
REMARK 3 8 3.5719 - 3.4167 0.97 5095 299 0.1528 0.1848
REMARK 3 9 3.4167 - 3.2853 0.97 5111 236 0.1570 0.2190
REMARK 3 10 3.2853 - 3.1721 0.97 5129 249 0.1591 0.1934
REMARK 3 11 3.1721 - 3.0730 0.97 5088 248 0.1642 0.2083
REMARK 3 12 3.0730 - 2.9853 0.97 5074 262 0.1603 0.2084
REMARK 3 13 2.9853 - 2.9067 0.97 5052 293 0.1611 0.2284
REMARK 3 14 2.9067 - 2.8359 0.97 5120 256 0.1566 0.2133
REMARK 3 15 2.8359 - 2.7715 0.97 5030 288 0.1612 0.2239
REMARK 3 16 2.7715 - 2.7125 0.97 5089 276 0.1631 0.2278
REMARK 3 17 2.7125 - 2.6583 0.97 5035 293 0.1629 0.2250
REMARK 3 18 2.6583 - 2.6082 0.97 5074 280 0.1720 0.2472
REMARK 3 19 2.6082 - 2.5616 0.98 5103 229 0.1687 0.2254
REMARK 3 20 2.5616 - 2.5182 0.97 5077 251 0.1721 0.2187
REMARK 3 21 2.5182 - 2.4776 0.97 5032 279 0.1754 0.2195
REMARK 3 22 2.4776 - 2.4395 0.97 5034 254 0.1801 0.2400
REMARK 3 23 2.4395 - 2.4037 0.97 5093 240 0.1770 0.2478
REMARK 3 24 2.4037 - 2.3698 0.97 5052 248 0.1798 0.2328
REMARK 3 25 2.3698 - 2.3378 0.97 5023 257 0.1891 0.2649
REMARK 3 26 2.3378 - 2.3074 0.97 4980 280 0.1814 0.2624
REMARK 3 27 2.3074 - 2.2786 0.96 5005 275 0.1937 0.2552
REMARK 3 28 2.2786 - 2.2512 0.97 5019 250 0.2110 0.2728
REMARK 3 29 2.2512 - 2.2250 0.96 4995 267 0.2092 0.2749
REMARK 3 30 2.2250 - 2.2000 0.96 5003 285 0.2078 0.2680
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.650
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.07
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.70
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 : 0.003 22519
REMARK 3 ANGLE : 0.572 30568
REMARK 3 CHIRALITY : 0.042 3195
REMARK 3 PLANARITY : 0.003 4069
REMARK 3 DIHEDRAL : 16.363 13176
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 6NSZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1000239364.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9674
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 160372
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 29.596
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 3.270
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.1200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.29
REMARK 200 R MERGE FOR SHELL (I) : 0.37100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.346
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: 4AJ9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM DIBASIC TATRATE, PEG 3350, PH
REMARK 280 6, BATCH MODE, TEMPERATURE 277K
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 65.55000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.45000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 77.25000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.45000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 65.55000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 77.25000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 62970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 71670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -197.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ARG A 2
REMARK 465 VAL A 3
REMARK 465 ASN A 4
REMARK 465 ALA A 5
REMARK 465 LEU A 6
REMARK 465 LEU A 7
REMARK 465 PRO A 8
REMARK 465 LEU A 9
REMARK 465 SER A 10
REMARK 465 GLY A 11
REMARK 465 LEU A 12
REMARK 465 ILE A 13
REMARK 465 GLY A 14
REMARK 465 THR A 15
REMARK 465 ALA A 16
REMARK 465 LEU A 17
REMARK 465 ALA A 18
REMARK 465 ALA A 19
REMARK 465 CYS A 20
REMARK 465 PRO A 21
REMARK 465 PHE A 22
REMARK 465 ALA A 23
REMARK 465 ASP A 24
REMARK 465 PRO A 25
REMARK 465 SER A 26
REMARK 465 ALA A 27
REMARK 465 LEU A 28
REMARK 465 GLY A 29
REMARK 465 ARG A 30
REMARK 465 ARG A 31
REMARK 465 ALA A 32
REMARK 465 GLU A 33
REMARK 465 GLY A 34
REMARK 465 GLY A 35
REMARK 465 GLU A 36
REMARK 465 VAL A 37
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 VAL B 3
REMARK 465 ASN B 4
REMARK 465 ALA B 5
REMARK 465 LEU B 6
REMARK 465 LEU B 7
REMARK 465 PRO B 8
REMARK 465 LEU B 9
REMARK 465 SER B 10
REMARK 465 GLY B 11
REMARK 465 LEU B 12
REMARK 465 ILE B 13
REMARK 465 GLY B 14
REMARK 465 THR B 15
REMARK 465 ALA B 16
REMARK 465 LEU B 17
REMARK 465 ALA B 18
REMARK 465 ALA B 19
REMARK 465 CYS B 20
REMARK 465 PRO B 21
REMARK 465 PHE B 22
REMARK 465 ALA B 23
REMARK 465 ASP B 24
REMARK 465 PRO B 25
REMARK 465 SER B 26
REMARK 465 ALA B 27
REMARK 465 LEU B 28
REMARK 465 GLY B 29
REMARK 465 ARG B 30
REMARK 465 ARG B 31
REMARK 465 ALA B 32
REMARK 465 GLU B 33
REMARK 465 GLY B 34
REMARK 465 GLY B 35
REMARK 465 GLU B 36
REMARK 465 VAL B 37
REMARK 465 GLY B 715
REMARK 465 ASP B 716
REMARK 465 ASP B 717
REMARK 465 GLU B 718
REMARK 465 GLU B 719
REMARK 465 MET C 1
REMARK 465 ARG C 2
REMARK 465 VAL C 3
REMARK 465 ASN C 4
REMARK 465 ALA C 5
REMARK 465 LEU C 6
REMARK 465 LEU C 7
REMARK 465 PRO C 8
REMARK 465 LEU C 9
REMARK 465 SER C 10
REMARK 465 GLY C 11
REMARK 465 LEU C 12
REMARK 465 ILE C 13
REMARK 465 GLY C 14
REMARK 465 THR C 15
REMARK 465 ALA C 16
REMARK 465 LEU C 17
REMARK 465 ALA C 18
REMARK 465 ALA C 19
REMARK 465 CYS C 20
REMARK 465 PRO C 21
REMARK 465 PHE C 22
REMARK 465 ALA C 23
REMARK 465 ASP C 24
REMARK 465 PRO C 25
REMARK 465 SER C 26
REMARK 465 ALA C 27
REMARK 465 LEU C 28
REMARK 465 GLY C 29
REMARK 465 ARG C 30
REMARK 465 ARG C 31
REMARK 465 ALA C 32
REMARK 465 GLU C 33
REMARK 465 GLY C 34
REMARK 465 GLY C 35
REMARK 465 GLU C 36
REMARK 465 VAL C 37
REMARK 465 ASP C 717
REMARK 465 GLU C 718
REMARK 465 GLU C 719
REMARK 465 MET D 1
REMARK 465 ARG D 2
REMARK 465 VAL D 3
REMARK 465 ASN D 4
REMARK 465 ALA D 5
REMARK 465 LEU D 6
REMARK 465 LEU D 7
REMARK 465 PRO D 8
REMARK 465 LEU D 9
REMARK 465 SER D 10
REMARK 465 GLY D 11
REMARK 465 LEU D 12
REMARK 465 ILE D 13
REMARK 465 GLY D 14
REMARK 465 THR D 15
REMARK 465 ALA D 16
REMARK 465 LEU D 17
REMARK 465 ALA D 18
REMARK 465 ALA D 19
REMARK 465 CYS D 20
REMARK 465 PRO D 21
REMARK 465 PHE D 22
REMARK 465 ALA D 23
REMARK 465 ASP D 24
REMARK 465 PRO D 25
REMARK 465 SER D 26
REMARK 465 ALA D 27
REMARK 465 LEU D 28
REMARK 465 GLY D 29
REMARK 465 ARG D 30
REMARK 465 ARG D 31
REMARK 465 ALA D 32
REMARK 465 GLU D 33
REMARK 465 GLY D 34
REMARK 465 GLY D 35
REMARK 465 GLU D 36
REMARK 465 VAL D 37
REMARK 465 ASP D 716
REMARK 465 ASP D 717
REMARK 465 GLU D 718
REMARK 465 GLU D 719
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ARG C 147 O HOH C 901 2.13
REMARK 500 O HOH B 1150 O HOH B 1178 2.16
REMARK 500 NH1 ARG B 398 O HOH B 901 2.17
REMARK 500 O HOH D 1096 O HOH D 1323 2.18
REMARK 500 O ARG B 147 O HOH B 902 2.18
REMARK 500 O HOH A 1075 O HOH A 1263 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 GLU A 65 42.14 -140.29
REMARK 500 VAL A 143 -52.84 -127.23
REMARK 500 PHE A 159 78.45 -150.01
REMARK 500 ILE A 248 -63.95 69.99
REMARK 500 PHE A 251 -168.01 -110.00
REMARK 500 ASN A 304 63.23 -108.52
REMARK 500 GLU A 359 -68.60 -109.35
REMARK 500 ASP A 420 -144.37 63.51
REMARK 500 HIS A 432 76.45 -103.86
REMARK 500 ASN A 448 -155.33 -136.93
REMARK 500 ARG A 469 64.64 -105.03
REMARK 500 THR A 568 -11.28 69.15
REMARK 500 PHE A 705 -64.10 72.59
REMARK 500 GLU B 65 40.69 -140.07
REMARK 500 VAL B 143 -52.98 -127.44
REMARK 500 SER B 146 -168.71 -79.08
REMARK 500 PHE B 159 80.24 -152.14
REMARK 500 ILE B 248 -62.45 69.62
REMARK 500 ASN B 304 61.59 -104.28
REMARK 500 GLU B 359 -68.39 -104.32
REMARK 500 GLU B 378 22.05 -77.35
REMARK 500 ASP B 420 -147.10 64.68
REMARK 500 HIS B 432 76.75 -104.62
REMARK 500 ARG B 469 71.35 -106.54
REMARK 500 THR B 568 -11.39 71.91
REMARK 500 SER B 575 -161.66 -127.48
REMARK 500 PHE B 705 -58.32 66.68
REMARK 500 GLU C 65 40.94 -145.16
REMARK 500 VAL C 143 -53.24 -126.38
REMARK 500 PHE C 159 83.96 -152.29
REMARK 500 ILE C 248 -67.79 68.26
REMARK 500 ASN C 304 62.29 -101.52
REMARK 500 GLU C 359 -67.59 -103.27
REMARK 500 ASP C 420 -145.19 64.51
REMARK 500 HIS C 432 74.38 -104.72
REMARK 500 ASN C 448 -159.10 -137.91
REMARK 500 ARG C 469 69.32 -107.52
REMARK 500 THR C 568 -12.86 74.00
REMARK 500 PHE C 705 -63.58 70.41
REMARK 500 VAL D 143 -56.35 -125.06
REMARK 500 ILE D 248 -65.88 65.81
REMARK 500 ASN D 304 58.95 -106.96
REMARK 500 GLU D 359 -65.37 -101.90
REMARK 500 ASP D 420 -141.32 60.61
REMARK 500 HIS D 432 78.56 -100.18
REMARK 500 ASN D 448 -152.54 -138.22
REMARK 500 ARG D 469 70.75 -109.71
REMARK 500 THR D 568 -6.94 70.45
REMARK 500 SER D 575 -155.63 -127.08
REMARK 500 PHE D 705 -59.35 71.35
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 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 389 OH
REMARK 620 2 HEM A 801 NA 80.9
REMARK 620 3 HEM A 801 NB 89.0 90.1
REMARK 620 4 HEM A 801 NC 97.1 178.0 89.9
REMARK 620 5 HEM A 801 ND 90.9 89.2 179.3 90.8
REMARK 620 6 HOH A1263 O 167.8 89.8 83.0 92.1 97.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 389 OH
REMARK 620 2 HEM B 801 NA 79.2
REMARK 620 3 HEM B 801 NB 88.2 90.0
REMARK 620 4 HEM B 801 NC 96.3 175.4 91.0
REMARK 620 5 HEM B 801 ND 89.3 90.1 177.5 88.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 389 OH
REMARK 620 2 HEM C 801 NA 81.8
REMARK 620 3 HEM C 801 NB 90.3 89.5
REMARK 620 4 HEM C 801 NC 98.2 179.6 90.1
REMARK 620 5 HEM C 801 ND 91.5 90.0 178.1 90.4
REMARK 620 6 HOH C1311 O 164.7 88.3 78.0 91.6 100.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR D 389 OH
REMARK 620 2 HEM D 801 NA 82.2
REMARK 620 3 HEM D 801 NB 91.4 89.3
REMARK 620 4 HEM D 801 NC 97.3 178.6 91.9
REMARK 620 5 HEM D 801 ND 89.6 88.5 177.5 90.2
REMARK 620 6 HOH D1323 O 167.5 88.6 80.1 92.2 98.6
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 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EOH A 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EOH B 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM C 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 C 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM D 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE D 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EOH D 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EOH D 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EOH D 810
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4AJ9 RELATED DB: PDB
REMARK 900 4AJ9 CONTAINS THE SAME PROTEIN
REMARK 900 RELATED ID: 6NSW RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN AT A LOWER RADIATION DOSE
REMARK 900 RELATED ID: 6NSY RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN AT A LOWER RADIATION DOSE
DBREF 6NSZ A 1 719 UNP Q9C169 CAT3_NEUCR 1 719
DBREF 6NSZ B 1 719 UNP Q9C169 CAT3_NEUCR 1 719
DBREF 6NSZ C 1 719 UNP Q9C169 CAT3_NEUCR 1 719
DBREF 6NSZ D 1 719 UNP Q9C169 CAT3_NEUCR 1 719
SEQRES 1 A 719 MET ARG VAL ASN ALA LEU LEU PRO LEU SER GLY LEU ILE
SEQRES 2 A 719 GLY THR ALA LEU ALA ALA CYS PRO PHE ALA ASP PRO SER
SEQRES 3 A 719 ALA LEU GLY ARG ARG ALA GLU GLY GLY GLU VAL ASP ALA
SEQRES 4 A 719 ARG GLN ARG LEU LYS GLU VAL GLU VAL ASP ASP ASN GLY
SEQRES 5 A 719 GLN PHE MET THR THR ASP PHE GLY GLY ASN ILE GLU GLU
SEQRES 6 A 719 GLN PHE SER LEU LYS ALA GLY GLY ARG GLY SER THR LEU
SEQRES 7 A 719 LEU GLU ASP PHE ILE PHE ARG GLN LYS LEU GLN HIS PHE
SEQRES 8 A 719 ASP HIS GLU ARG ILE PRO GLU ARG VAL VAL HIS ALA ARG
SEQRES 9 A 719 GLY ALA GLY ALA HIS GLY ILE PHE THR SER TYR GLY ASP
SEQRES 10 A 719 TRP SER ASN ILE THR ALA ALA SER PHE LEU GLY ALA LYS
SEQRES 11 A 719 ASP LYS GLN THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES 12 A 719 ALA GLY SER ARG GLY SER ALA ASP THR ALA ARG ASP VAL
SEQRES 13 A 719 HIS GLY PHE ALA THR ARG PHE TYR THR ASP GLU GLY ASN
SEQRES 14 A 719 PHE ASP ILE VAL GLY ASN ASN ILE PRO VAL PHE PHE ILE
SEQRES 15 A 719 GLN ASP ALA ILE ARG PHE PRO ASP LEU ILE HIS SER VAL
SEQRES 16 A 719 LYS PRO SER PRO ASP ASN GLU VAL PRO GLN ALA ALA THR
SEQRES 17 A 719 ALA HIS ASP SER ALA TRP ASP PHE PHE SER SER GLN PRO
SEQRES 18 A 719 SER ALA LEU HIS THR LEU PHE TRP ALA MET SER GLY ASN
SEQRES 19 A 719 GLY ILE PRO ARG SER TYR ARG HIS MET ASP GLY PHE GLY
SEQRES 20 A 719 ILE HIS THR PHE ARG LEU VAL THR GLU ASP GLY LYS SER
SEQRES 21 A 719 LYS LEU VAL LYS TRP HIS TRP LYS THR LYS GLN GLY LYS
SEQRES 22 A 719 ALA ALA LEU VAL TRP GLU GLU ALA GLN VAL LEU ALA GLY
SEQRES 23 A 719 LYS ASN ALA ASP PHE HIS ARG GLN ASP LEU TRP ASP ALA
SEQRES 24 A 719 ILE GLU SER GLY ASN ALA PRO SER TRP GLU LEU ALA VAL
SEQRES 25 A 719 GLN LEU ILE ASP GLU ASP LYS ALA GLN ALA TYR GLY PHE
SEQRES 26 A 719 ASP LEU LEU ASP PRO THR LYS PHE LEU PRO GLU GLU PHE
SEQRES 27 A 719 ALA PRO LEU GLN VAL LEU GLY GLU MET THR LEU ASN ARG
SEQRES 28 A 719 ASN PRO MET ASN TYR PHE ALA GLU THR GLU GLN ILE SER
SEQRES 29 A 719 PHE GLN PRO GLY HIS ILE VAL ARG GLY VAL ASP PHE THR
SEQRES 30 A 719 GLU ASP PRO LEU LEU GLN GLY ARG LEU TYR SER TYR LEU
SEQRES 31 A 719 ASP THR GLN LEU ASN ARG HIS ARG GLY PRO ASN PHE GLU
SEQRES 32 A 719 GLN LEU PRO ILE ASN ARG PRO VAL SER GLY VAL HIS ASN
SEQRES 33 A 719 ASN HIS ARG ASP GLY GLN GLY GLN ALA TRP ILE HIS LYS
SEQRES 34 A 719 ASN ILE HIS HIS TYR SER PRO SER TYR LEU ASN LYS GLY
SEQRES 35 A 719 TYR PRO ALA GLN ALA ASN GLN THR VAL GLY ARG GLY PHE
SEQRES 36 A 719 PHE THR THR PRO GLY ARG THR ALA SER GLY VAL LEU ASN
SEQRES 37 A 719 ARG GLU LEU SER ALA THR PHE ASP ASP HIS TYR THR GLN
SEQRES 38 A 719 PRO ARG LEU PHE PHE ASN SER LEU THR PRO VAL GLU GLN
SEQRES 39 A 719 GLN PHE VAL ILE ASN ALA ILE ARG PHE GLU ALA SER HIS
SEQRES 40 A 719 VAL THR ASN GLU GLN VAL LYS LYS ASN VAL LEU GLU GLN
SEQRES 41 A 719 LEU ASN LYS ILE SER ASN ASP VAL ALA LYS ARG VAL ALA
SEQRES 42 A 719 VAL ALA LEU GLY LEU GLU ALA PRO GLN PRO ASP PRO THR
SEQRES 43 A 719 TYR TYR HIS ASN ASN VAL THR ARG GLY VAL SER ILE PHE
SEQRES 44 A 719 ASN GLU SER LEU PRO THR ILE ALA THR LEU ARG VAL GLY
SEQRES 45 A 719 VAL LEU SER THR THR LYS GLY GLY SER LEU ASP LYS ALA
SEQRES 46 A 719 LYS ALA LEU LYS GLU GLN LEU GLU LYS ASP GLY LEU LYS
SEQRES 47 A 719 VAL THR VAL ILE ALA GLU TYR LEU ALA SER GLY VAL ASP
SEQRES 48 A 719 GLN THR TYR SER ALA ALA ASP ALA THR ALA PHE ASP ALA
SEQRES 49 A 719 VAL VAL VAL ALA GLU GLY ALA GLU ARG VAL PHE SER GLY
SEQRES 50 A 719 LYS GLY ALA MET SER PRO LEU PHE PRO ALA GLY ARG PRO
SEQRES 51 A 719 SER GLN ILE LEU THR ASP GLY TYR ARG TRP GLY LYS PRO
SEQRES 52 A 719 VAL ALA ALA VAL GLY SER ALA LYS LYS ALA LEU GLN SER
SEQRES 53 A 719 ILE GLY VAL GLU GLU LYS GLU ALA GLY VAL TYR ALA GLY
SEQRES 54 A 719 ALA GLN ASP GLU VAL ILE LYS GLY VAL GLU GLU GLY LEU
SEQRES 55 A 719 LYS VAL PHE LYS PHE LEU GLU ARG PHE ALA VAL ASP GLY
SEQRES 56 A 719 ASP ASP GLU GLU
SEQRES 1 B 719 MET ARG VAL ASN ALA LEU LEU PRO LEU SER GLY LEU ILE
SEQRES 2 B 719 GLY THR ALA LEU ALA ALA CYS PRO PHE ALA ASP PRO SER
SEQRES 3 B 719 ALA LEU GLY ARG ARG ALA GLU GLY GLY GLU VAL ASP ALA
SEQRES 4 B 719 ARG GLN ARG LEU LYS GLU VAL GLU VAL ASP ASP ASN GLY
SEQRES 5 B 719 GLN PHE MET THR THR ASP PHE GLY GLY ASN ILE GLU GLU
SEQRES 6 B 719 GLN PHE SER LEU LYS ALA GLY GLY ARG GLY SER THR LEU
SEQRES 7 B 719 LEU GLU ASP PHE ILE PHE ARG GLN LYS LEU GLN HIS PHE
SEQRES 8 B 719 ASP HIS GLU ARG ILE PRO GLU ARG VAL VAL HIS ALA ARG
SEQRES 9 B 719 GLY ALA GLY ALA HIS GLY ILE PHE THR SER TYR GLY ASP
SEQRES 10 B 719 TRP SER ASN ILE THR ALA ALA SER PHE LEU GLY ALA LYS
SEQRES 11 B 719 ASP LYS GLN THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES 12 B 719 ALA GLY SER ARG GLY SER ALA ASP THR ALA ARG ASP VAL
SEQRES 13 B 719 HIS GLY PHE ALA THR ARG PHE TYR THR ASP GLU GLY ASN
SEQRES 14 B 719 PHE ASP ILE VAL GLY ASN ASN ILE PRO VAL PHE PHE ILE
SEQRES 15 B 719 GLN ASP ALA ILE ARG PHE PRO ASP LEU ILE HIS SER VAL
SEQRES 16 B 719 LYS PRO SER PRO ASP ASN GLU VAL PRO GLN ALA ALA THR
SEQRES 17 B 719 ALA HIS ASP SER ALA TRP ASP PHE PHE SER SER GLN PRO
SEQRES 18 B 719 SER ALA LEU HIS THR LEU PHE TRP ALA MET SER GLY ASN
SEQRES 19 B 719 GLY ILE PRO ARG SER TYR ARG HIS MET ASP GLY PHE GLY
SEQRES 20 B 719 ILE HIS THR PHE ARG LEU VAL THR GLU ASP GLY LYS SER
SEQRES 21 B 719 LYS LEU VAL LYS TRP HIS TRP LYS THR LYS GLN GLY LYS
SEQRES 22 B 719 ALA ALA LEU VAL TRP GLU GLU ALA GLN VAL LEU ALA GLY
SEQRES 23 B 719 LYS ASN ALA ASP PHE HIS ARG GLN ASP LEU TRP ASP ALA
SEQRES 24 B 719 ILE GLU SER GLY ASN ALA PRO SER TRP GLU LEU ALA VAL
SEQRES 25 B 719 GLN LEU ILE ASP GLU ASP LYS ALA GLN ALA TYR GLY PHE
SEQRES 26 B 719 ASP LEU LEU ASP PRO THR LYS PHE LEU PRO GLU GLU PHE
SEQRES 27 B 719 ALA PRO LEU GLN VAL LEU GLY GLU MET THR LEU ASN ARG
SEQRES 28 B 719 ASN PRO MET ASN TYR PHE ALA GLU THR GLU GLN ILE SER
SEQRES 29 B 719 PHE GLN PRO GLY HIS ILE VAL ARG GLY VAL ASP PHE THR
SEQRES 30 B 719 GLU ASP PRO LEU LEU GLN GLY ARG LEU TYR SER TYR LEU
SEQRES 31 B 719 ASP THR GLN LEU ASN ARG HIS ARG GLY PRO ASN PHE GLU
SEQRES 32 B 719 GLN LEU PRO ILE ASN ARG PRO VAL SER GLY VAL HIS ASN
SEQRES 33 B 719 ASN HIS ARG ASP GLY GLN GLY GLN ALA TRP ILE HIS LYS
SEQRES 34 B 719 ASN ILE HIS HIS TYR SER PRO SER TYR LEU ASN LYS GLY
SEQRES 35 B 719 TYR PRO ALA GLN ALA ASN GLN THR VAL GLY ARG GLY PHE
SEQRES 36 B 719 PHE THR THR PRO GLY ARG THR ALA SER GLY VAL LEU ASN
SEQRES 37 B 719 ARG GLU LEU SER ALA THR PHE ASP ASP HIS TYR THR GLN
SEQRES 38 B 719 PRO ARG LEU PHE PHE ASN SER LEU THR PRO VAL GLU GLN
SEQRES 39 B 719 GLN PHE VAL ILE ASN ALA ILE ARG PHE GLU ALA SER HIS
SEQRES 40 B 719 VAL THR ASN GLU GLN VAL LYS LYS ASN VAL LEU GLU GLN
SEQRES 41 B 719 LEU ASN LYS ILE SER ASN ASP VAL ALA LYS ARG VAL ALA
SEQRES 42 B 719 VAL ALA LEU GLY LEU GLU ALA PRO GLN PRO ASP PRO THR
SEQRES 43 B 719 TYR TYR HIS ASN ASN VAL THR ARG GLY VAL SER ILE PHE
SEQRES 44 B 719 ASN GLU SER LEU PRO THR ILE ALA THR LEU ARG VAL GLY
SEQRES 45 B 719 VAL LEU SER THR THR LYS GLY GLY SER LEU ASP LYS ALA
SEQRES 46 B 719 LYS ALA LEU LYS GLU GLN LEU GLU LYS ASP GLY LEU LYS
SEQRES 47 B 719 VAL THR VAL ILE ALA GLU TYR LEU ALA SER GLY VAL ASP
SEQRES 48 B 719 GLN THR TYR SER ALA ALA ASP ALA THR ALA PHE ASP ALA
SEQRES 49 B 719 VAL VAL VAL ALA GLU GLY ALA GLU ARG VAL PHE SER GLY
SEQRES 50 B 719 LYS GLY ALA MET SER PRO LEU PHE PRO ALA GLY ARG PRO
SEQRES 51 B 719 SER GLN ILE LEU THR ASP GLY TYR ARG TRP GLY LYS PRO
SEQRES 52 B 719 VAL ALA ALA VAL GLY SER ALA LYS LYS ALA LEU GLN SER
SEQRES 53 B 719 ILE GLY VAL GLU GLU LYS GLU ALA GLY VAL TYR ALA GLY
SEQRES 54 B 719 ALA GLN ASP GLU VAL ILE LYS GLY VAL GLU GLU GLY LEU
SEQRES 55 B 719 LYS VAL PHE LYS PHE LEU GLU ARG PHE ALA VAL ASP GLY
SEQRES 56 B 719 ASP ASP GLU GLU
SEQRES 1 C 719 MET ARG VAL ASN ALA LEU LEU PRO LEU SER GLY LEU ILE
SEQRES 2 C 719 GLY THR ALA LEU ALA ALA CYS PRO PHE ALA ASP PRO SER
SEQRES 3 C 719 ALA LEU GLY ARG ARG ALA GLU GLY GLY GLU VAL ASP ALA
SEQRES 4 C 719 ARG GLN ARG LEU LYS GLU VAL GLU VAL ASP ASP ASN GLY
SEQRES 5 C 719 GLN PHE MET THR THR ASP PHE GLY GLY ASN ILE GLU GLU
SEQRES 6 C 719 GLN PHE SER LEU LYS ALA GLY GLY ARG GLY SER THR LEU
SEQRES 7 C 719 LEU GLU ASP PHE ILE PHE ARG GLN LYS LEU GLN HIS PHE
SEQRES 8 C 719 ASP HIS GLU ARG ILE PRO GLU ARG VAL VAL HIS ALA ARG
SEQRES 9 C 719 GLY ALA GLY ALA HIS GLY ILE PHE THR SER TYR GLY ASP
SEQRES 10 C 719 TRP SER ASN ILE THR ALA ALA SER PHE LEU GLY ALA LYS
SEQRES 11 C 719 ASP LYS GLN THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES 12 C 719 ALA GLY SER ARG GLY SER ALA ASP THR ALA ARG ASP VAL
SEQRES 13 C 719 HIS GLY PHE ALA THR ARG PHE TYR THR ASP GLU GLY ASN
SEQRES 14 C 719 PHE ASP ILE VAL GLY ASN ASN ILE PRO VAL PHE PHE ILE
SEQRES 15 C 719 GLN ASP ALA ILE ARG PHE PRO ASP LEU ILE HIS SER VAL
SEQRES 16 C 719 LYS PRO SER PRO ASP ASN GLU VAL PRO GLN ALA ALA THR
SEQRES 17 C 719 ALA HIS ASP SER ALA TRP ASP PHE PHE SER SER GLN PRO
SEQRES 18 C 719 SER ALA LEU HIS THR LEU PHE TRP ALA MET SER GLY ASN
SEQRES 19 C 719 GLY ILE PRO ARG SER TYR ARG HIS MET ASP GLY PHE GLY
SEQRES 20 C 719 ILE HIS THR PHE ARG LEU VAL THR GLU ASP GLY LYS SER
SEQRES 21 C 719 LYS LEU VAL LYS TRP HIS TRP LYS THR LYS GLN GLY LYS
SEQRES 22 C 719 ALA ALA LEU VAL TRP GLU GLU ALA GLN VAL LEU ALA GLY
SEQRES 23 C 719 LYS ASN ALA ASP PHE HIS ARG GLN ASP LEU TRP ASP ALA
SEQRES 24 C 719 ILE GLU SER GLY ASN ALA PRO SER TRP GLU LEU ALA VAL
SEQRES 25 C 719 GLN LEU ILE ASP GLU ASP LYS ALA GLN ALA TYR GLY PHE
SEQRES 26 C 719 ASP LEU LEU ASP PRO THR LYS PHE LEU PRO GLU GLU PHE
SEQRES 27 C 719 ALA PRO LEU GLN VAL LEU GLY GLU MET THR LEU ASN ARG
SEQRES 28 C 719 ASN PRO MET ASN TYR PHE ALA GLU THR GLU GLN ILE SER
SEQRES 29 C 719 PHE GLN PRO GLY HIS ILE VAL ARG GLY VAL ASP PHE THR
SEQRES 30 C 719 GLU ASP PRO LEU LEU GLN GLY ARG LEU TYR SER TYR LEU
SEQRES 31 C 719 ASP THR GLN LEU ASN ARG HIS ARG GLY PRO ASN PHE GLU
SEQRES 32 C 719 GLN LEU PRO ILE ASN ARG PRO VAL SER GLY VAL HIS ASN
SEQRES 33 C 719 ASN HIS ARG ASP GLY GLN GLY GLN ALA TRP ILE HIS LYS
SEQRES 34 C 719 ASN ILE HIS HIS TYR SER PRO SER TYR LEU ASN LYS GLY
SEQRES 35 C 719 TYR PRO ALA GLN ALA ASN GLN THR VAL GLY ARG GLY PHE
SEQRES 36 C 719 PHE THR THR PRO GLY ARG THR ALA SER GLY VAL LEU ASN
SEQRES 37 C 719 ARG GLU LEU SER ALA THR PHE ASP ASP HIS TYR THR GLN
SEQRES 38 C 719 PRO ARG LEU PHE PHE ASN SER LEU THR PRO VAL GLU GLN
SEQRES 39 C 719 GLN PHE VAL ILE ASN ALA ILE ARG PHE GLU ALA SER HIS
SEQRES 40 C 719 VAL THR ASN GLU GLN VAL LYS LYS ASN VAL LEU GLU GLN
SEQRES 41 C 719 LEU ASN LYS ILE SER ASN ASP VAL ALA LYS ARG VAL ALA
SEQRES 42 C 719 VAL ALA LEU GLY LEU GLU ALA PRO GLN PRO ASP PRO THR
SEQRES 43 C 719 TYR TYR HIS ASN ASN VAL THR ARG GLY VAL SER ILE PHE
SEQRES 44 C 719 ASN GLU SER LEU PRO THR ILE ALA THR LEU ARG VAL GLY
SEQRES 45 C 719 VAL LEU SER THR THR LYS GLY GLY SER LEU ASP LYS ALA
SEQRES 46 C 719 LYS ALA LEU LYS GLU GLN LEU GLU LYS ASP GLY LEU LYS
SEQRES 47 C 719 VAL THR VAL ILE ALA GLU TYR LEU ALA SER GLY VAL ASP
SEQRES 48 C 719 GLN THR TYR SER ALA ALA ASP ALA THR ALA PHE ASP ALA
SEQRES 49 C 719 VAL VAL VAL ALA GLU GLY ALA GLU ARG VAL PHE SER GLY
SEQRES 50 C 719 LYS GLY ALA MET SER PRO LEU PHE PRO ALA GLY ARG PRO
SEQRES 51 C 719 SER GLN ILE LEU THR ASP GLY TYR ARG TRP GLY LYS PRO
SEQRES 52 C 719 VAL ALA ALA VAL GLY SER ALA LYS LYS ALA LEU GLN SER
SEQRES 53 C 719 ILE GLY VAL GLU GLU LYS GLU ALA GLY VAL TYR ALA GLY
SEQRES 54 C 719 ALA GLN ASP GLU VAL ILE LYS GLY VAL GLU GLU GLY LEU
SEQRES 55 C 719 LYS VAL PHE LYS PHE LEU GLU ARG PHE ALA VAL ASP GLY
SEQRES 56 C 719 ASP ASP GLU GLU
SEQRES 1 D 719 MET ARG VAL ASN ALA LEU LEU PRO LEU SER GLY LEU ILE
SEQRES 2 D 719 GLY THR ALA LEU ALA ALA CYS PRO PHE ALA ASP PRO SER
SEQRES 3 D 719 ALA LEU GLY ARG ARG ALA GLU GLY GLY GLU VAL ASP ALA
SEQRES 4 D 719 ARG GLN ARG LEU LYS GLU VAL GLU VAL ASP ASP ASN GLY
SEQRES 5 D 719 GLN PHE MET THR THR ASP PHE GLY GLY ASN ILE GLU GLU
SEQRES 6 D 719 GLN PHE SER LEU LYS ALA GLY GLY ARG GLY SER THR LEU
SEQRES 7 D 719 LEU GLU ASP PHE ILE PHE ARG GLN LYS LEU GLN HIS PHE
SEQRES 8 D 719 ASP HIS GLU ARG ILE PRO GLU ARG VAL VAL HIS ALA ARG
SEQRES 9 D 719 GLY ALA GLY ALA HIS GLY ILE PHE THR SER TYR GLY ASP
SEQRES 10 D 719 TRP SER ASN ILE THR ALA ALA SER PHE LEU GLY ALA LYS
SEQRES 11 D 719 ASP LYS GLN THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES 12 D 719 ALA GLY SER ARG GLY SER ALA ASP THR ALA ARG ASP VAL
SEQRES 13 D 719 HIS GLY PHE ALA THR ARG PHE TYR THR ASP GLU GLY ASN
SEQRES 14 D 719 PHE ASP ILE VAL GLY ASN ASN ILE PRO VAL PHE PHE ILE
SEQRES 15 D 719 GLN ASP ALA ILE ARG PHE PRO ASP LEU ILE HIS SER VAL
SEQRES 16 D 719 LYS PRO SER PRO ASP ASN GLU VAL PRO GLN ALA ALA THR
SEQRES 17 D 719 ALA HIS ASP SER ALA TRP ASP PHE PHE SER SER GLN PRO
SEQRES 18 D 719 SER ALA LEU HIS THR LEU PHE TRP ALA MET SER GLY ASN
SEQRES 19 D 719 GLY ILE PRO ARG SER TYR ARG HIS MET ASP GLY PHE GLY
SEQRES 20 D 719 ILE HIS THR PHE ARG LEU VAL THR GLU ASP GLY LYS SER
SEQRES 21 D 719 LYS LEU VAL LYS TRP HIS TRP LYS THR LYS GLN GLY LYS
SEQRES 22 D 719 ALA ALA LEU VAL TRP GLU GLU ALA GLN VAL LEU ALA GLY
SEQRES 23 D 719 LYS ASN ALA ASP PHE HIS ARG GLN ASP LEU TRP ASP ALA
SEQRES 24 D 719 ILE GLU SER GLY ASN ALA PRO SER TRP GLU LEU ALA VAL
SEQRES 25 D 719 GLN LEU ILE ASP GLU ASP LYS ALA GLN ALA TYR GLY PHE
SEQRES 26 D 719 ASP LEU LEU ASP PRO THR LYS PHE LEU PRO GLU GLU PHE
SEQRES 27 D 719 ALA PRO LEU GLN VAL LEU GLY GLU MET THR LEU ASN ARG
SEQRES 28 D 719 ASN PRO MET ASN TYR PHE ALA GLU THR GLU GLN ILE SER
SEQRES 29 D 719 PHE GLN PRO GLY HIS ILE VAL ARG GLY VAL ASP PHE THR
SEQRES 30 D 719 GLU ASP PRO LEU LEU GLN GLY ARG LEU TYR SER TYR LEU
SEQRES 31 D 719 ASP THR GLN LEU ASN ARG HIS ARG GLY PRO ASN PHE GLU
SEQRES 32 D 719 GLN LEU PRO ILE ASN ARG PRO VAL SER GLY VAL HIS ASN
SEQRES 33 D 719 ASN HIS ARG ASP GLY GLN GLY GLN ALA TRP ILE HIS LYS
SEQRES 34 D 719 ASN ILE HIS HIS TYR SER PRO SER TYR LEU ASN LYS GLY
SEQRES 35 D 719 TYR PRO ALA GLN ALA ASN GLN THR VAL GLY ARG GLY PHE
SEQRES 36 D 719 PHE THR THR PRO GLY ARG THR ALA SER GLY VAL LEU ASN
SEQRES 37 D 719 ARG GLU LEU SER ALA THR PHE ASP ASP HIS TYR THR GLN
SEQRES 38 D 719 PRO ARG LEU PHE PHE ASN SER LEU THR PRO VAL GLU GLN
SEQRES 39 D 719 GLN PHE VAL ILE ASN ALA ILE ARG PHE GLU ALA SER HIS
SEQRES 40 D 719 VAL THR ASN GLU GLN VAL LYS LYS ASN VAL LEU GLU GLN
SEQRES 41 D 719 LEU ASN LYS ILE SER ASN ASP VAL ALA LYS ARG VAL ALA
SEQRES 42 D 719 VAL ALA LEU GLY LEU GLU ALA PRO GLN PRO ASP PRO THR
SEQRES 43 D 719 TYR TYR HIS ASN ASN VAL THR ARG GLY VAL SER ILE PHE
SEQRES 44 D 719 ASN GLU SER LEU PRO THR ILE ALA THR LEU ARG VAL GLY
SEQRES 45 D 719 VAL LEU SER THR THR LYS GLY GLY SER LEU ASP LYS ALA
SEQRES 46 D 719 LYS ALA LEU LYS GLU GLN LEU GLU LYS ASP GLY LEU LYS
SEQRES 47 D 719 VAL THR VAL ILE ALA GLU TYR LEU ALA SER GLY VAL ASP
SEQRES 48 D 719 GLN THR TYR SER ALA ALA ASP ALA THR ALA PHE ASP ALA
SEQRES 49 D 719 VAL VAL VAL ALA GLU GLY ALA GLU ARG VAL PHE SER GLY
SEQRES 50 D 719 LYS GLY ALA MET SER PRO LEU PHE PRO ALA GLY ARG PRO
SEQRES 51 D 719 SER GLN ILE LEU THR ASP GLY TYR ARG TRP GLY LYS PRO
SEQRES 52 D 719 VAL ALA ALA VAL GLY SER ALA LYS LYS ALA LEU GLN SER
SEQRES 53 D 719 ILE GLY VAL GLU GLU LYS GLU ALA GLY VAL TYR ALA GLY
SEQRES 54 D 719 ALA GLN ASP GLU VAL ILE LYS GLY VAL GLU GLU GLY LEU
SEQRES 55 D 719 LYS VAL PHE LYS PHE LEU GLU ARG PHE ALA VAL ASP GLY
SEQRES 56 D 719 ASP ASP GLU GLU
HET HEM A 801 43
HET ACT A 802 4
HET ACT A 803 4
HET PGE A 804 10
HET PEG A 805 7
HET PEG A 806 7
HET EDO A 807 4
HET EOH A 808 3
HET HEM B 801 43
HET ACT B 802 4
HET ACT B 803 4
HET 1PE B 804 16
HET PGE B 805 10
HET PEG B 806 7
HET EDO B 807 4
HET EDO B 808 4
HET EOH B 809 3
HET EOH B 810 3
HET HEM C 801 43
HET ACT C 802 4
HET ACT C 803 4
HET PG4 C 804 13
HET PEG C 805 7
HET PEG C 806 7
HET PEG C 807 7
HET EDO C 808 4
HET EDO C 809 4
HET EDO C 810 4
HET HEM D 801 43
HET ACT D 802 4
HET ACT D 803 4
HET PGE D 804 10
HET EDO D 805 4
HET EDO D 806 4
HET EDO D 807 4
HET EOH D 808 3
HET EOH D 809 3
HET EOH D 810 3
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM ACT ACETATE ION
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETNAM EOH ETHANOL
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETSYN HEM HEME
HETSYN EDO ETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 5 HEM 4(C34 H32 FE N4 O4)
FORMUL 6 ACT 8(C2 H3 O2 1-)
FORMUL 8 PGE 3(C6 H14 O4)
FORMUL 9 PEG 6(C4 H10 O3)
FORMUL 11 EDO 9(C2 H6 O2)
FORMUL 12 EOH 6(C2 H6 O)
FORMUL 16 1PE C10 H22 O6
FORMUL 26 PG4 C8 H18 O5
FORMUL 43 HOH *2014(H2 O)
HELIX 1 AA1 ARG A 40 GLU A 45 5 6
HELIX 2 AA2 ASP A 81 HIS A 93 1 13
HELIX 3 AA3 ALA A 124 GLY A 128 5 5
HELIX 4 AA4 ASP A 184 ILE A 186 5 3
HELIX 5 AA5 ARG A 187 LYS A 196 1 10
HELIX 6 AA6 HIS A 210 GLN A 220 1 11
HELIX 7 AA7 ALA A 223 MET A 231 1 9
HELIX 8 AA8 SER A 232 ILE A 236 5 5
HELIX 9 AA9 SER A 239 MET A 243 5 5
HELIX 10 AB1 VAL A 277 ASN A 288 1 12
HELIX 11 AB2 ASP A 290 SER A 302 1 13
HELIX 12 AB3 ASP A 316 ALA A 320 5 5
HELIX 13 AB4 ASN A 355 THR A 360 1 6
HELIX 14 AB5 ASP A 379 HIS A 397 1 19
HELIX 15 AB6 ASN A 401 LEU A 405 5 5
HELIX 16 AB7 SER A 472 ASP A 476 5 5
HELIX 17 AB8 TYR A 479 SER A 488 1 10
HELIX 18 AB9 THR A 490 SER A 506 1 17
HELIX 19 AC1 ASN A 510 SER A 525 1 16
HELIX 20 AC2 SER A 525 GLY A 537 1 13
HELIX 21 AC3 ASP A 544 TYR A 548 5 5
HELIX 22 AC4 GLY A 580 ASP A 595 1 16
HELIX 23 AC5 ASP A 618 PHE A 622 5 5
HELIX 24 AC6 GLY A 630 PHE A 635 5 6
HELIX 25 AC7 SER A 636 MET A 641 5 6
HELIX 26 AC8 GLY A 648 TRP A 660 1 13
HELIX 27 AC9 ALA A 670 ILE A 677 1 8
HELIX 28 AD1 ALA A 690 PHE A 705 1 16
HELIX 29 AD2 PHE A 707 PHE A 711 5 5
HELIX 30 AD3 ARG B 40 GLU B 45 5 6
HELIX 31 AD4 ASP B 81 HIS B 93 1 13
HELIX 32 AD5 ALA B 124 GLY B 128 5 5
HELIX 33 AD6 ASP B 184 ILE B 186 5 3
HELIX 34 AD7 ARG B 187 LYS B 196 1 10
HELIX 35 AD8 HIS B 210 GLN B 220 1 11
HELIX 36 AD9 ALA B 223 MET B 231 1 9
HELIX 37 AE1 SER B 232 ILE B 236 5 5
HELIX 38 AE2 SER B 239 MET B 243 5 5
HELIX 39 AE3 VAL B 277 ASN B 288 1 12
HELIX 40 AE4 ASP B 290 SER B 302 1 13
HELIX 41 AE5 ASP B 316 ALA B 320 5 5
HELIX 42 AE6 ASN B 355 THR B 360 1 6
HELIX 43 AE7 ASP B 379 ARG B 398 1 20
HELIX 44 AE8 ASN B 401 LEU B 405 5 5
HELIX 45 AE9 SER B 472 ASP B 476 5 5
HELIX 46 AF1 TYR B 479 SER B 488 1 10
HELIX 47 AF2 THR B 490 SER B 506 1 17
HELIX 48 AF3 ASN B 510 SER B 525 1 16
HELIX 49 AF4 SER B 525 GLY B 537 1 13
HELIX 50 AF5 ASP B 544 TYR B 548 5 5
HELIX 51 AF6 GLY B 580 ASP B 595 1 16
HELIX 52 AF7 ASP B 618 PHE B 622 5 5
HELIX 53 AF8 GLY B 630 MET B 641 5 12
HELIX 54 AF9 GLY B 648 TRP B 660 1 13
HELIX 55 AG1 ALA B 670 ILE B 677 1 8
HELIX 56 AG2 ALA B 690 PHE B 705 1 16
HELIX 57 AG3 PHE B 707 PHE B 711 5 5
HELIX 58 AG4 ARG C 40 GLU C 45 5 6
HELIX 59 AG5 ASP C 81 HIS C 93 1 13
HELIX 60 AG6 ALA C 124 GLY C 128 5 5
HELIX 61 AG7 ASP C 184 ILE C 186 5 3
HELIX 62 AG8 ARG C 187 LYS C 196 1 10
HELIX 63 AG9 HIS C 210 GLN C 220 1 11
HELIX 64 AH1 ALA C 223 MET C 231 1 9
HELIX 65 AH2 SER C 232 ILE C 236 5 5
HELIX 66 AH3 SER C 239 MET C 243 5 5
HELIX 67 AH4 VAL C 277 ASN C 288 1 12
HELIX 68 AH5 ASP C 290 SER C 302 1 13
HELIX 69 AH6 ASP C 316 ALA C 320 5 5
HELIX 70 AH7 ASN C 355 THR C 360 1 6
HELIX 71 AH8 ASP C 379 ARG C 398 1 20
HELIX 72 AH9 ASN C 401 LEU C 405 5 5
HELIX 73 AI1 SER C 472 ASP C 476 5 5
HELIX 74 AI2 TYR C 479 SER C 488 1 10
HELIX 75 AI3 THR C 490 SER C 506 1 17
HELIX 76 AI4 ASN C 510 SER C 525 1 16
HELIX 77 AI5 SER C 525 GLY C 537 1 13
HELIX 78 AI6 ASP C 544 TYR C 548 5 5
HELIX 79 AI7 GLY C 580 ASP C 595 1 16
HELIX 80 AI8 ASP C 618 PHE C 622 5 5
HELIX 81 AI9 GLY C 630 PHE C 635 5 6
HELIX 82 AJ1 SER C 636 MET C 641 5 6
HELIX 83 AJ2 GLY C 648 TRP C 660 1 13
HELIX 84 AJ3 ALA C 670 ILE C 677 1 8
HELIX 85 AJ4 ALA C 690 PHE C 705 1 16
HELIX 86 AJ5 PHE C 707 PHE C 711 5 5
HELIX 87 AJ6 ARG D 40 GLU D 45 5 6
HELIX 88 AJ7 ASP D 81 HIS D 93 1 13
HELIX 89 AJ8 ALA D 124 GLY D 128 5 5
HELIX 90 AJ9 ASP D 184 ILE D 186 5 3
HELIX 91 AK1 ARG D 187 LYS D 196 1 10
HELIX 92 AK2 HIS D 210 GLN D 220 1 11
HELIX 93 AK3 ALA D 223 MET D 231 1 9
HELIX 94 AK4 SER D 232 ILE D 236 5 5
HELIX 95 AK5 SER D 239 MET D 243 5 5
HELIX 96 AK6 VAL D 277 ASN D 288 1 12
HELIX 97 AK7 ASP D 290 SER D 302 1 13
HELIX 98 AK8 ASP D 316 ALA D 320 5 5
HELIX 99 AK9 ASN D 355 THR D 360 1 6
HELIX 100 AL1 ASP D 379 ARG D 398 1 20
HELIX 101 AL2 ASN D 401 LEU D 405 5 5
HELIX 102 AL3 SER D 472 ASP D 476 5 5
HELIX 103 AL4 TYR D 479 SER D 488 1 10
HELIX 104 AL5 THR D 490 SER D 506 1 17
HELIX 105 AL6 ASN D 510 SER D 525 1 16
HELIX 106 AL7 SER D 525 GLY D 537 1 13
HELIX 107 AL8 GLY D 580 ASP D 595 1 16
HELIX 108 AL9 ASP D 618 PHE D 622 5 5
HELIX 109 AM1 GLY D 630 PHE D 635 5 6
HELIX 110 AM2 GLY D 648 TRP D 660 1 13
HELIX 111 AM3 ALA D 670 ILE D 677 1 8
HELIX 112 AM4 ALA D 690 PHE D 705 1 16
HELIX 113 AM5 PHE D 707 PHE D 711 5 5
SHEET 1 AA1 2 GLU A 47 VAL A 48 0
SHEET 2 AA1 2 ILE C 427 HIS C 428 1 O ILE C 427 N VAL A 48
SHEET 1 AA2 4 LYS A 70 ALA A 71 0
SHEET 2 AA2 4 THR D 462 ASN D 468 -1 O ASN D 468 N LYS A 70
SHEET 3 AA2 4 THR C 462 ASN C 468 -1 N ALA C 463 O GLY D 465
SHEET 4 AA2 4 LYS B 70 ALA B 71 -1 N LYS B 70 O ASN C 468
SHEET 1 AA311 VAL A 374 ASP A 375 0
SHEET 2 AA311 PHE A 251 VAL A 254 -1 N ARG A 252 O ASP A 375
SHEET 3 AA311 SER A 260 THR A 269 -1 O VAL A 263 N PHE A 251
SHEET 4 AA311 SER A 307 ILE A 315 -1 O ALA A 311 N HIS A 266
SHEET 5 AA311 GLN A 342 ARG A 351 -1 O LEU A 344 N LEU A 310
SHEET 6 AA311 GLY A 105 SER A 114 -1 N THR A 113 O GLU A 346
SHEET 7 AA311 GLN A 133 SER A 141 -1 O PHE A 140 N ALA A 106
SHEET 8 AA311 GLY A 158 THR A 165 -1 O TYR A 164 N PRO A 135
SHEET 9 AA311 GLY A 168 ASN A 175 -1 O PHE A 170 N PHE A 163
SHEET 10 AA311 GLY A 245 PHE A 246 -1 O PHE A 246 N ASN A 175
SHEET 11 AA311 SER A 260 THR A 269 -1 O TRP A 267 N GLY A 245
SHEET 1 AA4 2 ILE A 427 HIS A 428 0
SHEET 2 AA4 2 GLU C 47 VAL C 48 1 O VAL C 48 N ILE A 427
SHEET 1 AA5 4 LYS C 70 ALA C 71 0
SHEET 2 AA5 4 THR B 462 ASN B 468 -1 N ASN B 468 O LYS C 70
SHEET 3 AA5 4 THR A 462 ASN A 468 -1 N ALA A 463 O GLY B 465
SHEET 4 AA5 4 LYS D 70 ALA D 71 -1 O LYS D 70 N ASN A 468
SHEET 1 AA6 6 GLN A 612 THR A 613 0
SHEET 2 AA6 6 LYS A 598 ALA A 603 1 O VAL A 601 N GLN A 612
SHEET 3 AA6 6 ARG A 570 LEU A 574 1 N VAL A 573 O ILE A 602
SHEET 4 AA6 6 ALA A 624 VAL A 627 1 O ALA A 624 N GLY A 572
SHEET 5 AA6 6 VAL A 664 VAL A 667 1 O ALA A 665 N VAL A 627
SHEET 6 AA6 6 VAL A 686 GLY A 689 1 O TYR A 687 N ALA A 666
SHEET 1 AA7 2 GLU B 47 VAL B 48 0
SHEET 2 AA7 2 ILE D 427 HIS D 428 1 O ILE D 427 N VAL B 48
SHEET 1 AA811 VAL B 374 ASP B 375 0
SHEET 2 AA811 PHE B 251 VAL B 254 -1 N ARG B 252 O ASP B 375
SHEET 3 AA811 SER B 260 THR B 269 -1 O VAL B 263 N PHE B 251
SHEET 4 AA811 SER B 307 ILE B 315 -1 O ILE B 315 N LEU B 262
SHEET 5 AA811 GLN B 342 ARG B 351 -1 O LEU B 344 N LEU B 310
SHEET 6 AA811 GLY B 105 SER B 114 -1 N THR B 113 O GLU B 346
SHEET 7 AA811 GLN B 133 SER B 141 -1 O THR B 134 N PHE B 112
SHEET 8 AA811 GLY B 158 THR B 165 -1 O TYR B 164 N PRO B 135
SHEET 9 AA811 GLY B 168 ASN B 175 -1 O PHE B 170 N PHE B 163
SHEET 10 AA811 GLY B 245 PHE B 246 -1 O PHE B 246 N ASN B 175
SHEET 11 AA811 SER B 260 THR B 269 -1 O TRP B 267 N GLY B 245
SHEET 1 AA9 2 ILE B 427 HIS B 428 0
SHEET 2 AA9 2 GLU D 47 VAL D 48 1 O VAL D 48 N ILE B 427
SHEET 1 AB1 6 GLN B 612 THR B 613 0
SHEET 2 AB1 6 LYS B 598 ALA B 603 1 O VAL B 601 N GLN B 612
SHEET 3 AB1 6 ARG B 570 LEU B 574 1 N VAL B 573 O ILE B 602
SHEET 4 AB1 6 ALA B 624 VAL B 627 1 O ALA B 624 N GLY B 572
SHEET 5 AB1 6 VAL B 664 VAL B 667 1 O ALA B 665 N VAL B 627
SHEET 6 AB1 6 VAL B 686 GLY B 689 1 O TYR B 687 N VAL B 664
SHEET 1 AB2 2 THR C 56 THR C 57 0
SHEET 2 AB2 2 GLY C 60 ASN C 62 -1 O GLY C 61 N THR C 57
SHEET 1 AB311 VAL C 374 ASP C 375 0
SHEET 2 AB311 PHE C 251 VAL C 254 -1 N ARG C 252 O ASP C 375
SHEET 3 AB311 SER C 260 THR C 269 -1 O VAL C 263 N PHE C 251
SHEET 4 AB311 SER C 307 ILE C 315 -1 O ILE C 315 N LEU C 262
SHEET 5 AB311 GLN C 342 ARG C 351 -1 O MET C 347 N TRP C 308
SHEET 6 AB311 GLY C 105 SER C 114 -1 N HIS C 109 O ARG C 351
SHEET 7 AB311 GLN C 133 SER C 141 -1 O THR C 134 N PHE C 112
SHEET 8 AB311 GLY C 158 THR C 165 -1 O TYR C 164 N PRO C 135
SHEET 9 AB311 GLY C 168 ASN C 175 -1 O PHE C 170 N PHE C 163
SHEET 10 AB311 GLY C 245 PHE C 246 -1 O PHE C 246 N ASN C 175
SHEET 11 AB311 SER C 260 THR C 269 -1 O TRP C 267 N GLY C 245
SHEET 1 AB4 6 GLN C 612 THR C 613 0
SHEET 2 AB4 6 LYS C 598 ALA C 603 1 N ALA C 603 O GLN C 612
SHEET 3 AB4 6 ARG C 570 LEU C 574 1 N VAL C 573 O THR C 600
SHEET 4 AB4 6 ALA C 624 VAL C 627 1 O ALA C 624 N GLY C 572
SHEET 5 AB4 6 VAL C 664 VAL C 667 1 O ALA C 665 N VAL C 625
SHEET 6 AB4 6 VAL C 686 GLY C 689 1 O TYR C 687 N VAL C 664
SHEET 1 AB511 VAL D 374 ASP D 375 0
SHEET 2 AB511 PHE D 251 VAL D 254 -1 N ARG D 252 O ASP D 375
SHEET 3 AB511 SER D 260 THR D 269 -1 O VAL D 263 N PHE D 251
SHEET 4 AB511 SER D 307 ILE D 315 -1 O ALA D 311 N HIS D 266
SHEET 5 AB511 GLN D 342 ARG D 351 -1 O LEU D 344 N LEU D 310
SHEET 6 AB511 GLY D 105 SER D 114 -1 N HIS D 109 O ARG D 351
SHEET 7 AB511 GLN D 133 SER D 141 -1 O PHE D 140 N ALA D 106
SHEET 8 AB511 GLY D 158 THR D 165 -1 O TYR D 164 N PRO D 135
SHEET 9 AB511 GLY D 168 ASN D 175 -1 O GLY D 174 N PHE D 159
SHEET 10 AB511 GLY D 245 PHE D 246 -1 O PHE D 246 N ASN D 175
SHEET 11 AB511 SER D 260 THR D 269 -1 O TRP D 267 N GLY D 245
SHEET 1 AB6 6 GLN D 612 THR D 613 0
SHEET 2 AB6 6 LYS D 598 ALA D 603 1 O VAL D 601 N GLN D 612
SHEET 3 AB6 6 ARG D 570 LEU D 574 1 N VAL D 573 O ILE D 602
SHEET 4 AB6 6 ALA D 624 VAL D 627 1 O ALA D 624 N GLY D 572
SHEET 5 AB6 6 VAL D 664 VAL D 667 1 O VAL D 667 N VAL D 627
SHEET 6 AB6 6 VAL D 686 GLY D 689 1 O TYR D 687 N VAL D 664
LINK OH TYR A 389 FE HEM A 801 1555 1555 2.28
LINK FE HEM A 801 O HOH A1263 1555 1555 2.75
LINK OH TYR B 389 FE HEM B 801 1555 1555 2.31
LINK OH TYR C 389 FE HEM C 801 1555 1555 2.30
LINK FE HEM C 801 O HOH C1311 1555 1555 2.70
LINK OH TYR D 389 FE HEM D 801 1555 1555 2.31
LINK FE HEM D 801 O HOH D1323 1555 1555 2.76
CISPEP 1 VAL A 203 PRO A 204 0 -1.53
CISPEP 2 SER A 435 PRO A 436 0 -1.00
CISPEP 3 SER A 435 PRO A 436 0 -2.89
CISPEP 4 TYR A 443 PRO A 444 0 1.85
CISPEP 5 VAL B 203 PRO B 204 0 2.05
CISPEP 6 SER B 435 PRO B 436 0 1.34
CISPEP 7 SER B 435 PRO B 436 0 -1.07
CISPEP 8 TYR B 443 PRO B 444 0 -0.32
CISPEP 9 VAL C 203 PRO C 204 0 -0.14
CISPEP 10 SER C 435 PRO C 436 0 1.03
CISPEP 11 SER C 435 PRO C 436 0 1.04
CISPEP 12 TYR C 443 PRO C 444 0 -1.61
CISPEP 13 VAL D 203 PRO D 204 0 0.16
CISPEP 14 SER D 435 PRO D 436 0 -0.15
CISPEP 15 TYR D 443 PRO D 444 0 1.81
SITE 1 AC1 26 ARG A 99 VAL A 100 VAL A 101 HIS A 102
SITE 2 AC1 26 ARG A 139 GLY A 158 VAL A 173 GLY A 174
SITE 3 AC1 26 ASN A 175 PHE A 180 PHE A 188 ILE A 248
SITE 4 AC1 26 HIS A 249 PHE A 365 LEU A 381 ARG A 385
SITE 5 AC1 26 SER A 388 TYR A 389 THR A 392 GLN A 393
SITE 6 AC1 26 ARG A 396 HOH A 968 HOH A 973 HOH A1020
SITE 7 AC1 26 HOH A1263 LEU D 88
SITE 1 AC2 5 VAL A 143 ASP A 155 VAL A 156 PHE A 181
SITE 2 AC2 5 VAL A 195
SITE 1 AC3 9 ASN A 176 ASN A 234 PRO A 237 HIS A 242
SITE 2 AC3 9 MET A 243 LYS A 273 ALA A 274 ILE A 558
SITE 3 AC3 9 HOH A 961
SITE 1 AC4 6 GLN A 612 ALA A 616 HOH A1016 HOH A1025
SITE 2 AC4 6 HOH A1138 HOH A1204
SITE 1 AC5 3 ASP A 477 TYR A 547 GLN D 542
SITE 1 AC6 5 TYR A 438 LEU A 439 LYS A 441 ASN D 551
SITE 2 AC6 5 EOH D 810
SITE 1 AC7 2 ASN A 551 VAL A 552
SITE 1 AC8 2 GLU A 317 GLY A 460
SITE 1 AC9 25 ARG B 99 VAL B 100 VAL B 101 HIS B 102
SITE 2 AC9 25 ARG B 139 GLY B 158 VAL B 173 GLY B 174
SITE 3 AC9 25 ASN B 175 ALA B 185 PHE B 188 ILE B 248
SITE 4 AC9 25 HIS B 249 PHE B 365 LEU B 381 ARG B 385
SITE 5 AC9 25 SER B 388 TYR B 389 THR B 392 GLN B 393
SITE 6 AC9 25 ARG B 396 HOH B 955 HOH B 965 HOH B1084
SITE 7 AC9 25 HOH B1178
SITE 1 AD1 6 VAL B 143 ALA B 144 ASP B 155 VAL B 156
SITE 2 AD1 6 PHE B 181 VAL B 195
SITE 1 AD2 8 ASN B 176 ASN B 234 PRO B 237 HIS B 242
SITE 2 AD2 8 MET B 243 LYS B 273 ALA B 274 HOH B 907
SITE 1 AD3 6 SER B 651 GLN B 652 ARG B 659 SER C 651
SITE 2 AD3 6 GLN C 652 ARG C 659
SITE 1 AD4 4 THR B 600 GLN B 612 ALA B 621 HOH B 908
SITE 1 AD5 4 THR B 655 ARG B 659 ILE B 677 HOH B1111
SITE 1 AD6 3 TYR B 438 LEU B 439 LYS B 441
SITE 1 AD7 4 PHE B 338 ASN B 551 VAL B 552 HOH B 963
SITE 1 AD8 2 GLU B 317 GLY B 460
SITE 1 AD9 25 LEU B 88 ARG C 99 VAL C 100 VAL C 101
SITE 2 AD9 25 HIS C 102 ARG C 139 GLY C 158 VAL C 173
SITE 3 AD9 25 GLY C 174 ASN C 175 PHE C 188 ILE C 248
SITE 4 AD9 25 HIS C 249 PHE C 365 LEU C 381 ARG C 385
SITE 5 AD9 25 SER C 388 TYR C 389 THR C 392 GLN C 393
SITE 6 AD9 25 ARG C 396 HOH C 950 HOH C 991 HOH C1020
SITE 7 AD9 25 HOH C1311
SITE 1 AE1 6 VAL C 143 ALA C 144 ASP C 155 VAL C 156
SITE 2 AE1 6 PHE C 181 VAL C 195
SITE 1 AE2 7 ASN C 176 PRO C 237 HIS C 242 MET C 243
SITE 2 AE2 7 LYS C 273 ALA C 274 HOH C 955
SITE 1 AE3 5 TYR B 115 TRP C 118 LEU C 341 GLN C 342
SITE 2 AE3 5 HOH C1291
SITE 1 AE4 2 TYR C 323 GLY C 324
SITE 1 AE5 4 ARG C 570 THR C 600 GLN C 612 HOH C1368
SITE 1 AE6 4 ASP B 117 SER B 119 ASN B 120 ARG C 554
SITE 1 AE7 4 ARG C 409 VAL C 414 TRP C 426 HOH C 972
SITE 1 AE8 2 ASP C 200 ASN C 201
SITE 1 AE9 1 HOH C 903
SITE 1 AF1 26 LEU A 88 ARG D 99 VAL D 100 VAL D 101
SITE 2 AF1 26 HIS D 102 ARG D 139 GLY D 158 VAL D 173
SITE 3 AF1 26 GLY D 174 ASN D 175 PHE D 180 PHE D 188
SITE 4 AF1 26 ILE D 248 HIS D 249 PHE D 365 LEU D 381
SITE 5 AF1 26 ARG D 385 SER D 388 TYR D 389 THR D 392
SITE 6 AF1 26 GLN D 393 ARG D 396 HOH D 935 HOH D1003
SITE 7 AF1 26 HOH D1088 HOH D1323
SITE 1 AF2 6 VAL D 143 ALA D 144 ASP D 155 VAL D 156
SITE 2 AF2 6 PHE D 181 VAL D 195
SITE 1 AF3 9 ASN D 176 ASN D 234 PRO D 237 HIS D 242
SITE 2 AF3 9 MET D 243 LYS D 273 ALA D 274 ILE D 558
SITE 3 AF3 9 HOH D 954
SITE 1 AF4 5 SER A 651 GLN A 652 ARG A 659 GLN D 652
SITE 2 AF4 5 ARG D 659
SITE 1 AF5 4 TYR D 658 ARG D 659 ILE D 677 GLY D 678
SITE 1 AF6 2 TYR D 438 LYS D 441
SITE 1 AF7 4 GLN D 321 PHE D 325 THR D 474 HOH D 913
SITE 1 AF8 3 GLU B 45 ARG D 409 TRP D 426
SITE 1 AF9 2 ASN D 551 EOH D 810
SITE 1 AG1 5 LYS A 441 PEG A 806 GLU D 337 VAL D 552
SITE 2 AG1 5 EOH D 809
CRYST1 131.100 154.500 160.900 90.00 90.00 90.00 P 21 21 21 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 0.007628 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006472 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006215 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
