HEADER OXIDOREDUCTASE 30-MAY-14 4QI7
TITLE CELLOBIOSE DEHYDROGENASE FROM NEUROSPORA CRASSA, NCCDH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELLOBIOSE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CELLOBIOSE DEHYDROGENASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEUROSPORA CRASSA;
SOURCE 3 ORGANISM_TAXID: 367110;
SOURCE 4 STRAIN: OR74A;
SOURCE 5 GENE: CDH-1, NCU00206;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: X33;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZALPHAA
KEYWDS IMMUNOGLOBULIN-LIKE BETA-SANDWICH (CYTOCHROME), FAD/NAD(P)-BINDING
KEYWDS 2 DOMAIN (DEHYDROGENASE DOMAIN), CELLOBIOSE OXIDIZING, ELECTRON
KEYWDS 3 TRANSFER, LIGNOCELLULOSE DEGRADATION, CELLOBIOSE, LPMO,
KEYWDS 4 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.C.TAN,R.GANDINI,C.SYGMUND,R.KITTL,D.HALTRICH,R.LUDWIG,B.M.HALLBERG,
AUTHOR 2 C.DIVNE
REVDAT 4 29-JUL-20 4QI7 1 COMPND REMARK SEQADV SEQRES
REVDAT 4 2 1 HETNAM LINK SITE
REVDAT 3 07-MAR-18 4QI7 1 JRNL
REVDAT 2 21-FEB-18 4QI7 1 JRNL
REVDAT 1 15-JUL-15 4QI7 0
JRNL AUTH T.C.TAN,D.KRACHER,R.GANDINI,C.SYGMUND,R.KITTL,D.HALTRICH,
JRNL AUTH 2 B.M.HALLBERG,R.LUDWIG,C.DIVNE
JRNL TITL STRUCTURAL BASIS FOR CELLOBIOSE DEHYDROGENASE ACTION DURING
JRNL TITL 2 OXIDATIVE CELLULOSE DEGRADATION.
JRNL REF NAT COMMUN V. 6 7542 2015
JRNL REFN ESSN 2041-1723
JRNL PMID 26151670
JRNL DOI 10.1038/NCOMMS8542
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.3_1477)
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.04
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 62460
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.190
REMARK 3 FREE R VALUE TEST SET COUNT : 1994
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 51.0453 - 6.9840 0.99 4537 149 0.1911 0.2428
REMARK 3 2 6.9840 - 5.5455 1.00 4403 142 0.1821 0.1917
REMARK 3 3 5.5455 - 4.8452 1.00 4366 141 0.1423 0.1922
REMARK 3 4 4.8452 - 4.4024 1.00 4340 148 0.1206 0.1646
REMARK 3 5 4.4024 - 4.0870 1.00 4301 145 0.1255 0.1583
REMARK 3 6 4.0870 - 3.8462 1.00 4314 143 0.1491 0.2065
REMARK 3 7 3.8462 - 3.6536 1.00 4313 136 0.1526 0.2240
REMARK 3 8 3.6536 - 3.4946 1.00 4275 148 0.1795 0.2378
REMARK 3 9 3.4946 - 3.3601 1.00 4258 139 0.2026 0.2661
REMARK 3 10 3.3601 - 3.2442 1.00 4298 141 0.2539 0.3395
REMARK 3 11 3.2442 - 3.1427 1.00 4247 142 0.2866 0.3681
REMARK 3 12 3.1427 - 3.0529 1.00 4280 136 0.3159 0.3577
REMARK 3 13 3.0529 - 2.9726 1.00 4259 148 0.3377 0.4149
REMARK 3 14 2.9726 - 2.9000 1.00 4275 136 0.4004 0.4615
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) : 0.500
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.170
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 : 0.011 12821
REMARK 3 ANGLE : 1.656 17537
REMARK 3 CHIRALITY : 0.058 1951
REMARK 3 PLANARITY : 0.007 2229
REMARK 3 DIHEDRAL : 15.469 4481
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 188 )
REMARK 3 ORIGIN FOR THE GROUP (A): 129.7641 -28.5180 162.7006
REMARK 3 T TENSOR
REMARK 3 T11: 0.8735 T22: 0.6874
REMARK 3 T33: 0.7002 T12: -0.0624
REMARK 3 T13: 0.0534 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.0395 L22: 0.0115
REMARK 3 L33: 0.0255 L12: -0.0173
REMARK 3 L13: 0.0358 L23: -0.0053
REMARK 3 S TENSOR
REMARK 3 S11: 0.0081 S12: -0.0202 S13: -0.0224
REMARK 3 S21: -0.1840 S22: 0.0872 S23: 0.0363
REMARK 3 S31: -0.1240 S32: -0.0397 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 189 THROUGH 251 )
REMARK 3 ORIGIN FOR THE GROUP (A): 133.9525 -2.9267 166.6186
REMARK 3 T TENSOR
REMARK 3 T11: 0.3447 T22: 0.1667
REMARK 3 T33: 0.3294 T12: 0.0693
REMARK 3 T13: 0.0653 T23: 0.0641
REMARK 3 L TENSOR
REMARK 3 L11: 0.0240 L22: 0.0522
REMARK 3 L33: 0.0728 L12: 0.0174
REMARK 3 L13: 0.0552 L23: -0.0156
REMARK 3 S TENSOR
REMARK 3 S11: 0.0119 S12: 0.1122 S13: -0.1723
REMARK 3 S21: 0.0174 S22: 0.0903 S23: 0.0218
REMARK 3 S31: 0.0374 S32: -0.0755 S33: 0.0084
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 252 THROUGH 806 )
REMARK 3 ORIGIN FOR THE GROUP (A): 150.4766 27.9552 172.4699
REMARK 3 T TENSOR
REMARK 3 T11: 0.1831 T22: 0.2345
REMARK 3 T33: 0.0851 T12: 0.0633
REMARK 3 T13: -0.0433 T23: 0.1264
REMARK 3 L TENSOR
REMARK 3 L11: 0.4672 L22: 0.2454
REMARK 3 L33: 0.4093 L12: 0.1579
REMARK 3 L13: -0.1322 L23: -0.2033
REMARK 3 S TENSOR
REMARK 3 S11: -0.0889 S12: -0.1654 S13: -0.4290
REMARK 3 S21: -0.0266 S22: 0.0583 S23: -0.1350
REMARK 3 S31: -0.4145 S32: 0.0674 S33: -0.0227
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 167.8689 -28.2147 154.1353
REMARK 3 T TENSOR
REMARK 3 T11: 1.2058 T22: 0.9841
REMARK 3 T33: 0.9926 T12: -0.1306
REMARK 3 T13: 0.2543 T23: 0.0940
REMARK 3 L TENSOR
REMARK 3 L11: 0.0147 L22: 0.0171
REMARK 3 L33: 0.0259 L12: 0.0125
REMARK 3 L13: -0.0031 L23: 0.0113
REMARK 3 S TENSOR
REMARK 3 S11: -0.0046 S12: 0.0286 S13: 0.1566
REMARK 3 S21: 0.0343 S22: 0.0796 S23: -0.0099
REMARK 3 S31: 0.0721 S32: -0.0445 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 131 THROUGH 225 )
REMARK 3 ORIGIN FOR THE GROUP (A): 165.8161 -29.8062 158.1673
REMARK 3 T TENSOR
REMARK 3 T11: 0.8178 T22: 0.6851
REMARK 3 T33: 0.7642 T12: -0.0629
REMARK 3 T13: 0.2331 T23: 0.0683
REMARK 3 L TENSOR
REMARK 3 L11: 0.0246 L22: -0.0085
REMARK 3 L33: 0.0197 L12: 0.0100
REMARK 3 L13: -0.0153 L23: 0.0385
REMARK 3 S TENSOR
REMARK 3 S11: 0.0687 S12: -0.1073 S13: -0.0554
REMARK 3 S21: -0.1008 S22: -0.0731 S23: 0.0960
REMARK 3 S31: 0.1246 S32: -0.0263 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 226 THROUGH 806 )
REMARK 3 ORIGIN FOR THE GROUP (A): 151.1894 -9.5942 211.9655
REMARK 3 T TENSOR
REMARK 3 T11: 0.0318 T22: 0.1003
REMARK 3 T33: 0.1345 T12: -0.0209
REMARK 3 T13: 0.1670 T23: 0.2059
REMARK 3 L TENSOR
REMARK 3 L11: 0.4373 L22: 0.6840
REMARK 3 L33: 0.4276 L12: 0.3948
REMARK 3 L13: -0.1456 L23: -0.2585
REMARK 3 S TENSOR
REMARK 3 S11: 0.1125 S12: 0.4092 S13: 0.1183
REMARK 3 S21: 0.6873 S22: 0.2071 S23: 0.0179
REMARK 3 S31: -0.1920 S32: -0.2008 S33: 0.4459
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 4QI7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000086086.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 1.05970
REMARK 200 MONOCHROMATOR : CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62494
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 58.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES-OH PH 6.5, 1.5 M MAGNESIUM
REMARK 280 SULFATE, 0.02 M LITHIUM SULFATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 66.79950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.49900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.92550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 73.49900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 66.79950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.92550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -325.0 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 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 PCA A 1
REMARK 465 PCA B 1
REMARK 465 THR B 206
REMARK 465 VAL B 207
REMARK 465 THR B 208
REMARK 465 GLY B 209
REMARK 465 THR B 210
REMARK 465 CYS B 211
REMARK 465 SER B 212
REMARK 465 GLY B 213
REMARK 465 PRO B 214
REMARK 465 VAL B 215
REMARK 465 THR B 216
REMARK 465 THR B 217
REMARK 465 SER B 218
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 773 C - N - CA ANGL. DEV. = 9.8 DEGREES
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 ALA A 57 -75.93 -87.70
REMARK 500 ALA A 61 -77.47 -82.63
REMARK 500 TRP A 83 142.83 -177.77
REMARK 500 ASP A 86 -10.58 69.42
REMARK 500 ILE A 114 -59.50 -124.57
REMARK 500 THR A 121 -60.07 -103.53
REMARK 500 ASP A 138 -113.80 54.38
REMARK 500 CYS A 211 -67.43 -95.78
REMARK 500 SER A 212 -13.16 68.46
REMARK 500 ILE A 219 76.64 58.08
REMARK 500 SER A 264 -71.28 -102.91
REMARK 500 LYS A 296 -65.43 -102.84
REMARK 500 LYS A 342 -176.73 -69.40
REMARK 500 LYS A 394 -64.68 -128.65
REMARK 500 THR A 421 -73.75 -123.52
REMARK 500 THR A 472 -36.08 72.93
REMARK 500 PHE A 547 -24.51 71.88
REMARK 500 ASN A 553 66.21 -117.88
REMARK 500 SER A 604 -164.00 -124.77
REMARK 500 PHE A 605 -73.21 -33.04
REMARK 500 TYR A 611 -10.07 62.80
REMARK 500 LEU A 635 38.79 70.66
REMARK 500 PRO A 643 44.35 -90.35
REMARK 500 ASP A 736 -178.88 171.85
REMARK 500 TRP A 775 -2.70 72.37
REMARK 500 ALA B 57 -120.82 58.11
REMARK 500 ASP B 86 -2.09 66.68
REMARK 500 ALA B 100 167.51 175.37
REMARK 500 THR B 121 -60.29 -120.94
REMARK 500 ASP B 138 -129.90 54.87
REMARK 500 SER B 264 -75.45 -104.61
REMARK 500 LYS B 296 -60.19 -102.31
REMARK 500 PRO B 363 45.70 -93.70
REMARK 500 ASP B 366 -91.64 -98.27
REMARK 500 ASN B 471 -74.13 -48.70
REMARK 500 HIS B 539 157.58 178.26
REMARK 500 PHE B 547 -25.95 64.94
REMARK 500 SER B 604 -75.80 -102.20
REMARK 500 PHE B 605 -154.37 -80.46
REMARK 500 PRO B 643 47.38 -91.57
REMARK 500 ASP B 730 -62.82 -104.92
REMARK 500 ASP B 736 -174.35 171.90
REMARK 500 TRP B 775 -4.87 72.31
REMARK 500 PRO B 792 53.48 -95.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 604 PHE A 605 -144.60
REMARK 500 THR B 470 ASN B 471 -149.28
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 901 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 74 SD
REMARK 620 2 HEM A 901 NA 104.2
REMARK 620 3 HEM A 901 NB 100.4 85.2
REMARK 620 4 HEM A 901 NC 110.3 145.5 89.0
REMARK 620 5 HEM A 901 ND 96.8 84.8 161.8 90.7
REMARK 620 6 HIS A 176 NE2 175.5 71.3 79.1 74.2 83.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 901 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET B 74 SD
REMARK 620 2 HEM B 901 NA 113.3
REMARK 620 3 HEM B 901 NB 93.6 82.5
REMARK 620 4 HEM B 901 NC 111.6 134.2 86.6
REMARK 620 5 HEM B 901 ND 113.6 84.0 152.7 85.9
REMARK 620 6 HIS B 176 NE2 168.4 64.3 74.9 69.9 77.9
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QI3 RELATED DB: PDB
REMARK 900 RELATED ID: 4QI4 RELATED DB: PDB
REMARK 900 RELATED ID: 4QI5 RELATED DB: PDB
REMARK 900 RELATED ID: 4QI6 RELATED DB: PDB
REMARK 900 RELATED ID: 4QI8 RELATED DB: PDB
DBREF 4QI7 A 2 806 UNP Q7RXM0 Q7RXM0_NEUCR 25 829
DBREF 4QI7 B 2 806 UNP Q7RXM0 Q7RXM0_NEUCR 25 829
SEQADV 4QI7 PCA A 1 UNP Q7RXM0 EXPRESSION TAG
SEQADV 4QI7 PCA B 1 UNP Q7RXM0 EXPRESSION TAG
SEQRES 1 A 806 PCA THR ALA PRO LYS THR PHE THR HIS PRO ASP THR GLY
SEQRES 2 A 806 ILE VAL PHE ASN THR TRP SER ALA SER ASP SER GLN THR
SEQRES 3 A 806 LYS GLY GLY PHE THR VAL GLY MET ALA LEU PRO SER ASN
SEQRES 4 A 806 ALA LEU THR THR ASP ALA THR GLU PHE ILE GLY TYR LEU
SEQRES 5 A 806 GLU CYS SER SER ALA LYS ASN GLY ALA ASN SER GLY TRP
SEQRES 6 A 806 CYS GLY VAL SER LEU ARG GLY ALA MET THR ASN ASN LEU
SEQRES 7 A 806 LEU ILE THR ALA TRP PRO SER ASP GLY GLU VAL TYR THR
SEQRES 8 A 806 ASN LEU MET PHE ALA THR GLY TYR ALA MET PRO LYS ASN
SEQRES 9 A 806 TYR ALA GLY ASP ALA LYS ILE THR GLN ILE ALA SER SER
SEQRES 10 A 806 VAL ASN ALA THR HIS PHE THR LEU VAL PHE ARG CYS GLN
SEQRES 11 A 806 ASN CYS LEU SER TRP ASP GLN ASP GLY VAL THR GLY GLY
SEQRES 12 A 806 ILE SER THR SER ASN LYS GLY ALA GLN LEU GLY TRP VAL
SEQRES 13 A 806 GLN ALA PHE PRO SER PRO GLY ASN PRO THR CYS PRO THR
SEQRES 14 A 806 GLN ILE THR LEU SER GLN HIS ASP ASN GLY MET GLY GLN
SEQRES 15 A 806 TRP GLY ALA ALA PHE ASP SER ASN ILE ALA ASN PRO SER
SEQRES 16 A 806 TYR THR ALA TRP ALA ALA LYS ALA THR LYS THR VAL THR
SEQRES 17 A 806 GLY THR CYS SER GLY PRO VAL THR THR SER ILE ALA ALA
SEQRES 18 A 806 THR PRO VAL PRO THR GLY VAL SER PHE ASP TYR ILE VAL
SEQRES 19 A 806 VAL GLY GLY GLY ALA GLY GLY ILE PRO VAL ALA ASP LYS
SEQRES 20 A 806 LEU SER GLU SER GLY LYS SER VAL LEU LEU ILE GLU LYS
SEQRES 21 A 806 GLY PHE ALA SER THR GLY GLU HIS GLY GLY THR LEU LYS
SEQRES 22 A 806 PRO GLU TRP LEU ASN ASN THR SER LEU THR ARG PHE ASP
SEQRES 23 A 806 VAL PRO GLY LEU CYS ASN GLN ILE TRP LYS ASP SER ASP
SEQRES 24 A 806 GLY ILE ALA CYS SER ASP THR ASP GLN MET ALA GLY CYS
SEQRES 25 A 806 VAL LEU GLY GLY GLY THR ALA ILE ASN ALA GLY LEU TRP
SEQRES 26 A 806 TYR LYS PRO TYR THR LYS ASP TRP ASP TYR LEU PHE PRO
SEQRES 27 A 806 SER GLY TRP LYS GLY SER ASP ILE ALA GLY ALA THR SER
SEQRES 28 A 806 ARG ALA LEU SER ARG ILE PRO GLY THR THR THR PRO SER
SEQRES 29 A 806 GLN ASP GLY LYS ARG TYR LEU GLN GLN GLY PHE GLU VAL
SEQRES 30 A 806 LEU ALA ASN GLY LEU LYS ALA SER GLY TRP LYS GLU VAL
SEQRES 31 A 806 ASP SER LEU LYS ASP SER GLU GLN LYS ASN ARG THR PHE
SEQRES 32 A 806 SER HIS THR SER TYR MET TYR ILE ASN GLY GLU ARG GLY
SEQRES 33 A 806 GLY PRO LEU ALA THR TYR LEU VAL SER ALA LYS LYS ARG
SEQRES 34 A 806 SER ASN PHE LYS LEU TRP LEU ASN THR ALA VAL LYS ARG
SEQRES 35 A 806 VAL ILE ARG GLU GLY GLY HIS ILE THR GLY VAL GLU VAL
SEQRES 36 A 806 GLU ALA PHE ARG ASN GLY GLY TYR SER GLY ILE ILE PRO
SEQRES 37 A 806 VAL THR ASN THR THR GLY ARG VAL VAL LEU SER ALA GLY
SEQRES 38 A 806 THR PHE GLY SER ALA LYS ILE LEU LEU ARG SER GLY ILE
SEQRES 39 A 806 GLY PRO LYS ASP GLN LEU GLU VAL VAL LYS ALA SER ALA
SEQRES 40 A 806 ASP GLY PRO THR MET VAL SER ASN SER SER TRP ILE ASP
SEQRES 41 A 806 LEU PRO VAL GLY HIS ASN LEU VAL ASP HIS THR ASN THR
SEQRES 42 A 806 ASP THR VAL ILE GLN HIS ASN ASN VAL THR PHE TYR ASP
SEQRES 43 A 806 PHE TYR LYS ALA TRP ASP ASN PRO ASN THR THR ASP MET
SEQRES 44 A 806 ASN LEU TYR LEU ASN GLY ARG SER GLY ILE PHE ALA GLN
SEQRES 45 A 806 ALA ALA PRO ASN ILE GLY PRO LEU PHE TRP GLU GLU ILE
SEQRES 46 A 806 THR GLY ALA ASP GLY ILE VAL ARG GLN LEU HIS TRP THR
SEQRES 47 A 806 ALA ARG VAL GLU GLY SER PHE GLU THR PRO ASP GLY TYR
SEQRES 48 A 806 ALA MET THR MET SER GLN TYR LEU GLY ARG GLY ALA THR
SEQRES 49 A 806 SER ARG GLY ARG MET THR LEU SER PRO THR LEU ASN THR
SEQRES 50 A 806 VAL VAL SER ASP LEU PRO TYR LEU LYS ASP PRO ASN ASP
SEQRES 51 A 806 LYS ALA ALA VAL VAL GLN GLY ILE VAL ASN LEU GLN LYS
SEQRES 52 A 806 ALA LEU ALA ASN VAL LYS GLY LEU THR TRP ALA TYR PRO
SEQRES 53 A 806 SER ALA ASN GLN THR ALA ALA ASP PHE VAL ASP LYS GLN
SEQRES 54 A 806 PRO VAL THR TYR GLN SER ARG ARG SER ASN HIS TRP MET
SEQRES 55 A 806 GLY THR ASN LYS MET GLY THR ASP ASP GLY ARG SER GLY
SEQRES 56 A 806 GLY THR ALA VAL VAL ASP THR ASN THR ARG VAL TYR GLY
SEQRES 57 A 806 THR ASP ASN LEU TYR VAL VAL ASP ALA SER ILE PHE PRO
SEQRES 58 A 806 GLY VAL PRO THR THR ASN PRO THR ALA TYR ILE VAL VAL
SEQRES 59 A 806 ALA ALA GLU HIS ALA ALA ALA LYS ILE LEU ALA GLN PRO
SEQRES 60 A 806 ALA ASN GLU ALA VAL PRO LYS TRP GLY TRP CYS GLY GLY
SEQRES 61 A 806 PRO THR TYR THR GLY SER GLN THR CYS GLN ALA PRO TYR
SEQRES 62 A 806 LYS CYS GLU LYS GLN ASN ASP TRP TYR TRP GLN CYS VAL
SEQRES 1 B 806 PCA THR ALA PRO LYS THR PHE THR HIS PRO ASP THR GLY
SEQRES 2 B 806 ILE VAL PHE ASN THR TRP SER ALA SER ASP SER GLN THR
SEQRES 3 B 806 LYS GLY GLY PHE THR VAL GLY MET ALA LEU PRO SER ASN
SEQRES 4 B 806 ALA LEU THR THR ASP ALA THR GLU PHE ILE GLY TYR LEU
SEQRES 5 B 806 GLU CYS SER SER ALA LYS ASN GLY ALA ASN SER GLY TRP
SEQRES 6 B 806 CYS GLY VAL SER LEU ARG GLY ALA MET THR ASN ASN LEU
SEQRES 7 B 806 LEU ILE THR ALA TRP PRO SER ASP GLY GLU VAL TYR THR
SEQRES 8 B 806 ASN LEU MET PHE ALA THR GLY TYR ALA MET PRO LYS ASN
SEQRES 9 B 806 TYR ALA GLY ASP ALA LYS ILE THR GLN ILE ALA SER SER
SEQRES 10 B 806 VAL ASN ALA THR HIS PHE THR LEU VAL PHE ARG CYS GLN
SEQRES 11 B 806 ASN CYS LEU SER TRP ASP GLN ASP GLY VAL THR GLY GLY
SEQRES 12 B 806 ILE SER THR SER ASN LYS GLY ALA GLN LEU GLY TRP VAL
SEQRES 13 B 806 GLN ALA PHE PRO SER PRO GLY ASN PRO THR CYS PRO THR
SEQRES 14 B 806 GLN ILE THR LEU SER GLN HIS ASP ASN GLY MET GLY GLN
SEQRES 15 B 806 TRP GLY ALA ALA PHE ASP SER ASN ILE ALA ASN PRO SER
SEQRES 16 B 806 TYR THR ALA TRP ALA ALA LYS ALA THR LYS THR VAL THR
SEQRES 17 B 806 GLY THR CYS SER GLY PRO VAL THR THR SER ILE ALA ALA
SEQRES 18 B 806 THR PRO VAL PRO THR GLY VAL SER PHE ASP TYR ILE VAL
SEQRES 19 B 806 VAL GLY GLY GLY ALA GLY GLY ILE PRO VAL ALA ASP LYS
SEQRES 20 B 806 LEU SER GLU SER GLY LYS SER VAL LEU LEU ILE GLU LYS
SEQRES 21 B 806 GLY PHE ALA SER THR GLY GLU HIS GLY GLY THR LEU LYS
SEQRES 22 B 806 PRO GLU TRP LEU ASN ASN THR SER LEU THR ARG PHE ASP
SEQRES 23 B 806 VAL PRO GLY LEU CYS ASN GLN ILE TRP LYS ASP SER ASP
SEQRES 24 B 806 GLY ILE ALA CYS SER ASP THR ASP GLN MET ALA GLY CYS
SEQRES 25 B 806 VAL LEU GLY GLY GLY THR ALA ILE ASN ALA GLY LEU TRP
SEQRES 26 B 806 TYR LYS PRO TYR THR LYS ASP TRP ASP TYR LEU PHE PRO
SEQRES 27 B 806 SER GLY TRP LYS GLY SER ASP ILE ALA GLY ALA THR SER
SEQRES 28 B 806 ARG ALA LEU SER ARG ILE PRO GLY THR THR THR PRO SER
SEQRES 29 B 806 GLN ASP GLY LYS ARG TYR LEU GLN GLN GLY PHE GLU VAL
SEQRES 30 B 806 LEU ALA ASN GLY LEU LYS ALA SER GLY TRP LYS GLU VAL
SEQRES 31 B 806 ASP SER LEU LYS ASP SER GLU GLN LYS ASN ARG THR PHE
SEQRES 32 B 806 SER HIS THR SER TYR MET TYR ILE ASN GLY GLU ARG GLY
SEQRES 33 B 806 GLY PRO LEU ALA THR TYR LEU VAL SER ALA LYS LYS ARG
SEQRES 34 B 806 SER ASN PHE LYS LEU TRP LEU ASN THR ALA VAL LYS ARG
SEQRES 35 B 806 VAL ILE ARG GLU GLY GLY HIS ILE THR GLY VAL GLU VAL
SEQRES 36 B 806 GLU ALA PHE ARG ASN GLY GLY TYR SER GLY ILE ILE PRO
SEQRES 37 B 806 VAL THR ASN THR THR GLY ARG VAL VAL LEU SER ALA GLY
SEQRES 38 B 806 THR PHE GLY SER ALA LYS ILE LEU LEU ARG SER GLY ILE
SEQRES 39 B 806 GLY PRO LYS ASP GLN LEU GLU VAL VAL LYS ALA SER ALA
SEQRES 40 B 806 ASP GLY PRO THR MET VAL SER ASN SER SER TRP ILE ASP
SEQRES 41 B 806 LEU PRO VAL GLY HIS ASN LEU VAL ASP HIS THR ASN THR
SEQRES 42 B 806 ASP THR VAL ILE GLN HIS ASN ASN VAL THR PHE TYR ASP
SEQRES 43 B 806 PHE TYR LYS ALA TRP ASP ASN PRO ASN THR THR ASP MET
SEQRES 44 B 806 ASN LEU TYR LEU ASN GLY ARG SER GLY ILE PHE ALA GLN
SEQRES 45 B 806 ALA ALA PRO ASN ILE GLY PRO LEU PHE TRP GLU GLU ILE
SEQRES 46 B 806 THR GLY ALA ASP GLY ILE VAL ARG GLN LEU HIS TRP THR
SEQRES 47 B 806 ALA ARG VAL GLU GLY SER PHE GLU THR PRO ASP GLY TYR
SEQRES 48 B 806 ALA MET THR MET SER GLN TYR LEU GLY ARG GLY ALA THR
SEQRES 49 B 806 SER ARG GLY ARG MET THR LEU SER PRO THR LEU ASN THR
SEQRES 50 B 806 VAL VAL SER ASP LEU PRO TYR LEU LYS ASP PRO ASN ASP
SEQRES 51 B 806 LYS ALA ALA VAL VAL GLN GLY ILE VAL ASN LEU GLN LYS
SEQRES 52 B 806 ALA LEU ALA ASN VAL LYS GLY LEU THR TRP ALA TYR PRO
SEQRES 53 B 806 SER ALA ASN GLN THR ALA ALA ASP PHE VAL ASP LYS GLN
SEQRES 54 B 806 PRO VAL THR TYR GLN SER ARG ARG SER ASN HIS TRP MET
SEQRES 55 B 806 GLY THR ASN LYS MET GLY THR ASP ASP GLY ARG SER GLY
SEQRES 56 B 806 GLY THR ALA VAL VAL ASP THR ASN THR ARG VAL TYR GLY
SEQRES 57 B 806 THR ASP ASN LEU TYR VAL VAL ASP ALA SER ILE PHE PRO
SEQRES 58 B 806 GLY VAL PRO THR THR ASN PRO THR ALA TYR ILE VAL VAL
SEQRES 59 B 806 ALA ALA GLU HIS ALA ALA ALA LYS ILE LEU ALA GLN PRO
SEQRES 60 B 806 ALA ASN GLU ALA VAL PRO LYS TRP GLY TRP CYS GLY GLY
SEQRES 61 B 806 PRO THR TYR THR GLY SER GLN THR CYS GLN ALA PRO TYR
SEQRES 62 B 806 LYS CYS GLU LYS GLN ASN ASP TRP TYR TRP GLN CYS VAL
MODRES 4QI7 ASN A 119 ASN GLYCOSYLATION SITE
MODRES 4QI7 ASN B 119 ASN GLYCOSYLATION SITE
MODRES 4QI7 ASN A 278 ASN GLYCOSYLATION SITE
MODRES 4QI7 ASN B 278 ASN GLYCOSYLATION SITE
MODRES 4QI7 ASN A 400 ASN GLYCOSYLATION SITE
MODRES 4QI7 ASN B 400 ASN GLYCOSYLATION SITE
MODRES 4QI7 ASN A 471 ASN GLYCOSYLATION SITE
MODRES 4QI7 ASN A 515 ASN GLYCOSYLATION SITE
MODRES 4QI7 ASN B 515 ASN GLYCOSYLATION SITE
MODRES 4QI7 ASN A 541 ASN GLYCOSYLATION SITE
MODRES 4QI7 ASN B 541 ASN GLYCOSYLATION SITE
MODRES 4QI7 ASN A 555 ASN GLYCOSYLATION SITE
MODRES 4QI7 ASN B 555 ASN GLYCOSYLATION SITE
MODRES 4QI7 THR A 222 THR GLYCOSYLATION SITE
MODRES 4QI7 THR B 222 THR GLYCOSYLATION SITE
MODRES 4QI7 THR A 226 THR GLYCOSYLATION SITE
MODRES 4QI7 THR B 226 THR GLYCOSYLATION SITE
HET HEM A 901 43
HET FAD A 902 53
HET NAG A 903 14
HET NAG A 904 14
HET NAG A 905 14
HET NAG A 906 14
HET NAG A 907 14
HET NAG A 908 14
HET NAG A 909 14
HET MAN A 910 11
HET MAN A 911 11
HET PT A 912 1
HET PT A 913 1
HET PT A 914 1
HET PT A 915 1
HET PT A 916 1
HET PT A 917 1
HET PT A 918 1
HET PT A 919 1
HET PT A 920 1
HET PT A 921 1
HET PT A 922 1
HET PT A 923 1
HET MG A 924 1
HET MG A 925 1
HET MG A 926 1
HET HEM B 901 43
HET FAD B 902 53
HET NAG B 903 14
HET NAG B 904 14
HET NAG B 905 14
HET NAG B 906 14
HET NAG B 907 14
HET NAG B 908 14
HET MAN B 909 11
HET MAN B 910 11
HET PT B 911 1
HET PT B 912 1
HET PT B 913 1
HET PT B 914 1
HET PT B 915 1
HET PT B 916 1
HET PT B 917 1
HET PT B 918 1
HET MG B 919 1
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM PT PLATINUM (II) ION
HETNAM MG MAGNESIUM ION
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 FAD 2(C27 H33 N9 O15 P2)
FORMUL 5 NAG 13(C8 H15 N O6)
FORMUL 12 MAN 4(C6 H12 O6)
FORMUL 14 PT 20(PT 2+)
FORMUL 26 MG 4(MG 2+)
HELIX 1 1 CYS A 167 ILE A 171 5 5
HELIX 2 2 ASP A 188 ALA A 192 5 5
HELIX 3 3 SER A 195 ALA A 200 1 6
HELIX 4 4 ALA A 201 ALA A 203 5 3
HELIX 5 5 GLY A 240 GLU A 250 1 11
HELIX 6 6 PRO A 274 ASN A 278 5 5
HELIX 7 7 VAL A 287 CYS A 291 5 5
HELIX 8 8 ASN A 292 LYS A 296 5 5
HELIX 9 9 GLY A 316 ASN A 321 1 6
HELIX 10 10 TYR A 329 PHE A 337 1 9
HELIX 11 11 ILE A 346 ILE A 357 1 12
HELIX 12 12 GLN A 372 ALA A 384 1 13
HELIX 13 13 GLY A 416 THR A 421 1 6
HELIX 14 14 THR A 421 LYS A 428 1 8
HELIX 15 15 GLY A 481 SER A 492 1 12
HELIX 16 16 PRO A 496 ALA A 505 1 10
HELIX 17 17 ASP A 508 MET A 512 5 5
HELIX 18 18 ASN A 555 ARG A 566 1 12
HELIX 19 19 GLY A 568 GLN A 572 5 5
HELIX 20 20 ASP A 647 LEU A 665 1 19
HELIX 21 21 THR A 681 GLN A 689 1 9
HELIX 22 22 THR A 692 ARG A 697 1 6
HELIX 23 23 ASP A 711 GLY A 715 5 5
HELIX 24 24 ASP A 736 PHE A 740 5 5
HELIX 25 25 PRO A 748 GLN A 766 1 19
HELIX 26 26 PRO B 37 THR B 42 5 6
HELIX 27 27 ALA B 57 GLY B 60 5 4
HELIX 28 28 SER B 195 ALA B 200 1 6
HELIX 29 29 GLY B 240 SER B 251 1 12
HELIX 30 30 THR B 265 GLY B 269 5 5
HELIX 31 31 PRO B 274 ASN B 278 5 5
HELIX 32 32 VAL B 287 LYS B 296 5 10
HELIX 33 33 GLY B 316 ASN B 321 1 6
HELIX 34 34 TYR B 329 PHE B 337 1 9
HELIX 35 35 ILE B 346 ILE B 357 1 12
HELIX 36 36 GLN B 372 SER B 385 1 14
HELIX 37 37 GLY B 416 THR B 421 1 6
HELIX 38 38 THR B 421 ARG B 429 1 9
HELIX 39 39 ALA B 480 SER B 492 1 13
HELIX 40 40 PRO B 496 SER B 506 1 11
HELIX 41 41 SER B 514 TRP B 518 5 5
HELIX 42 42 ASN B 555 ARG B 566 1 12
HELIX 43 43 GLY B 568 GLN B 572 5 5
HELIX 44 44 ASP B 647 LEU B 665 1 19
HELIX 45 45 THR B 681 GLN B 689 1 9
HELIX 46 46 THR B 692 ARG B 697 1 6
HELIX 47 47 ASP B 711 GLY B 715 5 5
HELIX 48 48 ASP B 736 PHE B 740 5 5
HELIX 49 49 PRO B 748 GLN B 766 1 19
SHEET 1 A 6 LYS A 5 THR A 8 0
SHEET 2 A 6 VAL A 15 ALA A 21 -1 O PHE A 16 N PHE A 7
SHEET 3 A 6 PHE A 30 ALA A 35 -1 O PHE A 30 N ALA A 21
SHEET 4 A 6 PHE A 48 SER A 55 -1 O ILE A 49 N ALA A 35
SHEET 5 A 6 HIS A 122 GLN A 130 -1 O LEU A 125 N LEU A 52
SHEET 6 A 6 LYS A 110 VAL A 118 -1 N ALA A 115 O VAL A 126
SHEET 1 B 6 LYS A 103 ASN A 104 0
SHEET 2 B 6 GLU A 88 PHE A 95 -1 N PHE A 95 O LYS A 103
SHEET 3 B 6 LEU A 78 SER A 85 -1 N LEU A 79 O MET A 94
SHEET 4 B 6 TRP A 65 SER A 69 -1 N CYS A 66 O ALA A 82
SHEET 5 B 6 LEU A 153 ALA A 158 -1 O ALA A 158 N TRP A 65
SHEET 6 B 6 GLY A 179 TRP A 183 -1 O GLY A 181 N TRP A 155
SHEET 1 C 2 SER A 134 GLN A 137 0
SHEET 2 C 2 VAL A 140 GLY A 143 -1 O VAL A 140 N GLN A 137
SHEET 1 D 4 THR A 222 PRO A 223 0
SHEET 2 D 4 TYR A 463 PRO A 468 1 O SER A 464 N THR A 222
SHEET 3 D 4 HIS A 449 ALA A 457 -1 N VAL A 453 O ILE A 467
SHEET 4 D 4 THR A 438 GLU A 446 -1 N ILE A 444 O GLY A 452
SHEET 1 E 5 PHE A 432 TRP A 435 0
SHEET 2 E 5 VAL A 255 ILE A 258 1 N LEU A 257 O TRP A 435
SHEET 3 E 5 TYR A 232 VAL A 235 1 N VAL A 234 O LEU A 256
SHEET 4 E 5 ARG A 475 LEU A 478 1 O VAL A 477 N ILE A 233
SHEET 5 E 5 LEU A 732 VAL A 734 1 O TYR A 733 N LEU A 478
SHEET 1 F 7 LYS A 388 GLU A 389 0
SHEET 2 F 7 THR A 402 SER A 404 1 O PHE A 403 N LYS A 388
SHEET 3 F 7 ILE A 577 THR A 586 -1 O TRP A 582 N THR A 402
SHEET 4 F 7 VAL A 592 ARG A 600 -1 O TRP A 597 N PHE A 581
SHEET 5 F 7 ALA A 612 LEU A 619 -1 O SER A 616 N THR A 598
SHEET 6 F 7 THR A 531 GLN A 538 -1 N THR A 533 O GLN A 617
SHEET 7 F 7 THR A 672 TYR A 675 -1 O TYR A 675 N VAL A 536
SHEET 1 G 3 HIS A 525 LEU A 527 0
SHEET 2 G 3 GLY A 627 LEU A 631 -1 O GLY A 627 N LEU A 527
SHEET 3 G 3 THR A 637 ASP A 641 -1 O VAL A 638 N THR A 630
SHEET 1 H 3 TRP A 777 GLY A 779 0
SHEET 2 H 3 TRP A 803 CYS A 805 -1 O TRP A 803 N GLY A 779
SHEET 3 H 3 CYS A 795 LYS A 797 -1 N GLU A 796 O GLN A 804
SHEET 1 I 6 LYS B 5 THR B 8 0
SHEET 2 I 6 VAL B 15 SER B 20 -1 O PHE B 16 N PHE B 7
SHEET 3 I 6 PHE B 30 ALA B 35 -1 O VAL B 32 N TRP B 19
SHEET 4 I 6 GLU B 47 SER B 55 -1 O ILE B 49 N ALA B 35
SHEET 5 I 6 HIS B 122 GLN B 130 -1 O PHE B 123 N CYS B 54
SHEET 6 I 6 LYS B 110 VAL B 118 -1 N ALA B 115 O VAL B 126
SHEET 1 J 6 LYS B 103 ASN B 104 0
SHEET 2 J 6 GLU B 88 PHE B 95 -1 N PHE B 95 O LYS B 103
SHEET 3 J 6 LEU B 78 SER B 85 -1 N TRP B 83 O TYR B 90
SHEET 4 J 6 TRP B 65 SER B 69 -1 N VAL B 68 O ILE B 80
SHEET 5 J 6 GLY B 150 ALA B 158 -1 O VAL B 156 N GLY B 67
SHEET 6 J 6 GLY B 179 ALA B 186 -1 O GLY B 181 N TRP B 155
SHEET 1 K 4 THR B 222 PRO B 223 0
SHEET 2 K 4 TYR B 463 PRO B 468 1 O SER B 464 N THR B 222
SHEET 3 K 4 HIS B 449 ALA B 457 -1 N VAL B 455 O GLY B 465
SHEET 4 K 4 THR B 438 GLU B 446 -1 N ALA B 439 O GLU B 456
SHEET 1 L 5 PHE B 432 TRP B 435 0
SHEET 2 L 5 VAL B 255 ILE B 258 1 N LEU B 257 O TRP B 435
SHEET 3 L 5 TYR B 232 VAL B 235 1 N VAL B 234 O ILE B 258
SHEET 4 L 5 ARG B 475 LEU B 478 1 O VAL B 477 N VAL B 235
SHEET 5 L 5 LEU B 732 VAL B 734 1 O TYR B 733 N LEU B 478
SHEET 1 M 7 LYS B 388 GLU B 389 0
SHEET 2 M 7 THR B 402 SER B 404 1 O PHE B 403 N LYS B 388
SHEET 3 M 7 ILE B 577 THR B 586 -1 O LEU B 580 N SER B 404
SHEET 4 M 7 VAL B 592 ARG B 600 -1 O ALA B 599 N GLY B 578
SHEET 5 M 7 MET B 613 LEU B 619 -1 O TYR B 618 N HIS B 596
SHEET 6 M 7 THR B 531 GLN B 538 -1 N THR B 531 O LEU B 619
SHEET 7 M 7 THR B 672 TYR B 675 -1 O TYR B 675 N VAL B 536
SHEET 1 N 2 ARG B 628 LEU B 631 0
SHEET 2 N 2 THR B 637 ASP B 641 -1 O VAL B 638 N THR B 630
SHEET 1 O 3 TRP B 777 GLY B 779 0
SHEET 2 O 3 TRP B 803 VAL B 806 -1 O TRP B 803 N GLY B 779
SHEET 3 O 3 LYS B 794 LYS B 797 -1 N GLU B 796 O GLN B 804
SSBOND 1 CYS A 54 CYS A 66 1555 1555 2.03
SSBOND 2 CYS A 129 CYS A 132 1555 1555 2.02
SSBOND 3 CYS A 167 CYS A 211 1555 1555 2.04
SSBOND 4 CYS A 303 CYS A 312 1555 1555 2.04
SSBOND 5 CYS A 778 CYS A 795 1555 1555 2.03
SSBOND 6 CYS A 789 CYS A 805 1555 1555 2.05
SSBOND 7 CYS B 54 CYS B 66 1555 1555 2.04
SSBOND 8 CYS B 129 CYS B 132 1555 1555 2.03
SSBOND 9 CYS B 303 CYS B 312 1555 1555 2.04
SSBOND 10 CYS B 778 CYS B 795 1555 1555 2.04
SSBOND 11 CYS B 789 CYS B 805 1555 1555 2.04
LINK ND2 ASN A 119 C1 NAG A 903 1555 1555 1.49
LINK OG1 THR A 222 C1 MAN A 910 1555 1555 1.38
LINK OG1 THR A 226 C1 MAN A 911 1555 1555 1.41
LINK ND2 ASN A 278 C1 NAG A 904 1555 1555 1.42
LINK ND2 ASN A 400 C1 NAG A 905 1555 1555 1.42
LINK ND2 ASN A 471 C1 NAG A 906 1555 1555 1.51
LINK ND2 ASN A 515 C1 NAG A 907 1555 1555 1.44
LINK ND2 ASN A 541 C1 NAG A 908 1555 1555 1.39
LINK ND2 ASN A 555 C1 NAG A 909 1555 1555 1.46
LINK ND2 ASN B 119 C1 NAG B 903 1555 1555 1.52
LINK OG1 THR B 222 C1 MAN B 909 1555 1555 1.41
LINK OG1 THR B 226 C1 MAN B 910 1555 1555 1.43
LINK ND2 ASN B 278 C1 NAG B 904 1555 1555 1.52
LINK ND2 ASN B 400 C1 NAG B 905 1555 1555 1.43
LINK ND2 ASN B 515 C1 NAG B 906 1555 1555 1.46
LINK ND2 ASN B 541 C1 NAG B 907 1555 1555 1.42
LINK ND2 ASN B 555 C1 NAG B 908 1555 1555 1.43
LINK SD MET A 74 FE HEM A 901 1555 1555 2.05
LINK NE2 HIS A 176 FE HEM A 901 1555 1555 2.14
LINK O ASP A 177 MG MG A 926 1555 1555 2.95
LINK NZ LYS A 331 PT PT A 916 1555 1555 2.76
LINK NZ LYS A 433 PT PT A 919 1555 1555 2.35
LINK SD MET B 74 FE HEM B 901 1555 1555 2.10
LINK NE2 HIS B 176 FE HEM B 901 1555 1555 2.22
LINK NZ LYS B 433 PT PT B 917 1555 1555 2.58
CISPEP 1 ASN A 148 LYS A 149 0 -2.29
CISPEP 2 ALA A 574 PRO A 575 0 -16.78
CISPEP 3 TYR A 675 PRO A 676 0 -11.41
CISPEP 4 ALA A 791 PRO A 792 0 -2.02
CISPEP 5 ALA B 61 ASN B 62 0 2.31
CISPEP 6 ALA B 574 PRO B 575 0 -16.65
CISPEP 7 GLY B 578 PRO B 579 0 -0.71
CISPEP 8 TYR B 675 PRO B 676 0 7.08
CISPEP 9 ALA B 791 PRO B 792 0 -2.98
CRYST1 133.599 141.851 146.998 90.00 90.00 90.00 P 21 21 21 8
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 0.007485 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007050 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006803 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
