HEADER PHOTOSYNTHESIS 06-AUG-04 1W5C
TITLE PHOTOSYSTEM II FROM THERMOSYNECHOCOCCUS ELONGATUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTOSYSTEM Q(B) PROTEIN 1;
COMPND 3 CHAIN: A, G;
COMPND 4 SYNONYM: PHOTOSYSTEM II PROTEIN D1;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: PHOTOSYSTEM II CORE LIGHT HARVESTING PROTEIN;
COMPND 7 CHAIN: B, H;
COMPND 8 SYNONYM: PSII SUBUNIT PSBB;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: PHOTOSYSTEM II CP43 PROTEIN;
COMPND 11 CHAIN: C, I;
COMPND 12 SYNONYM: PSII SUBUNIT PSBC;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: PHOTOSYSTEM II REACTION CENTER D2 PROTEIN;
COMPND 15 CHAIN: D, J;
COMPND 16 SYNONYM: PSII SUBUNIT PSBD;
COMPND 17 MOL_ID: 5;
COMPND 18 MOLECULE: CYTOCHROME B559 ALPHA SUBUNIT;
COMPND 19 CHAIN: E, K;
COMPND 20 SYNONYM: PSII SUBUNIT PSBE, PSII REACTION CENTER SUBUNIT V;
COMPND 21 MOL_ID: 6;
COMPND 22 MOLECULE: CYTOCHROME B559 BETA SUBUNIT;
COMPND 23 CHAIN: F, L;
COMPND 24 SYNONYM: PSII SUBUNIT PSBF, PSII REACTION CENTER SUBUNIT VI;
COMPND 25 MOL_ID: 7;
COMPND 26 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;
COMPND 27 CHAIN: O, P;
COMPND 28 SYNONYM: PSII SUBUNIT PSBO, MSP;
COMPND 29 MOL_ID: 8;
COMPND 30 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;
COMPND 31 CHAIN: S, U;
COMPND 32 SYNONYM: PSII SUBUNIT PSBU, PS II COMPLEX 12KDA EXTRINSIC PROTEIN,
COMPND 33 PSII-U;
COMPND 34 MOL_ID: 9;
COMPND 35 MOLECULE: CYTOCHROME C-550;
COMPND 36 CHAIN: T, V;
COMPND 37 SYNONYM: PSII SUBUNIT PSBV, CYTOCHROME C550, LOW POTENTIAL
COMPND 38 CYTOCHROME C;
COMPND 39 MOL_ID: 10;
COMPND 40 MOLECULE: UNASSIGNED SUBUNITS;
COMPND 41 CHAIN: X, Y
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 3 ORGANISM_TAXID: 146786;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 6 ORGANISM_TAXID: 146786;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 9 ORGANISM_TAXID: 146786;
SOURCE 10 MOL_ID: 4;
SOURCE 11 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 12 ORGANISM_TAXID: 146786;
SOURCE 13 MOL_ID: 5;
SOURCE 14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 15 ORGANISM_TAXID: 146786;
SOURCE 16 MOL_ID: 6;
SOURCE 17 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 18 ORGANISM_TAXID: 146786;
SOURCE 19 MOL_ID: 7;
SOURCE 20 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 21 ORGANISM_TAXID: 146786;
SOURCE 22 MOL_ID: 8;
SOURCE 23 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 24 ORGANISM_TAXID: 146786;
SOURCE 25 MOL_ID: 9;
SOURCE 26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 27 ORGANISM_TAXID: 146786;
SOURCE 28 MOL_ID: 10;
SOURCE 29 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 30 ORGANISM_TAXID: 146786
KEYWDS PHOTOSYNTHESIS, WATER OXIDATION, PHOTOSYSTEM, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.BIESIADKA,B.LOLL,J.KERN,K.-D.IRRGANG,A.ZOUNI,W.SAENGER
REVDAT 5 08-JAN-14 1W5C 1 JRNL
REVDAT 4 08-AUG-12 1W5C 1 COMPND KEYWDS JRNL REMARK
REVDAT 4 2 DBREF HET HETNAM HETSYN
REVDAT 4 3 FORMUL LINK SITE ATOM
REVDAT 4 4 HETATM CONECT MASTER
REVDAT 3 24-FEB-09 1W5C 1 VERSN
REVDAT 2 06-JAN-05 1W5C 1 DBREF
REVDAT 1 21-DEC-04 1W5C 0
JRNL AUTH J.BIESIADKA,B.LOLL,J.KERN,K.-D.IRRGANG,A.ZOUNI
JRNL TITL CRYSTAL STRUCTURE OF CYANOBACTERIAL PHOTOSYSTEM II AT 3.2 A
JRNL TITL 2 RESOLUTION: A CLOSER LOOK AT THE MN- CLUSTER
JRNL REF PHYS.CHEM.CHEM.PHYS. V. 6 4733 2004
JRNL REFN ISSN 1463-9076
REMARK 2
REMARK 2 RESOLUTION. 3.2 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MLF
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.2
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 75.6
REMARK 3 NUMBER OF REFLECTIONS : 107320
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 31578
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4036
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 33.02
REMARK 3 B22 (A**2) : -5.16
REMARK 3 B33 (A**2) : -27.85
REMARK 3 B12 (A**2) : 0
REMARK 3 B13 (A**2) : 0
REMARK 3 B23 (A**2) : 0
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.76
REMARK 3 ESD FROM SIGMAA (A) : 0.65
REMARK 3 LOW RESOLUTION CUTOFF (A) : 10
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.78
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.76
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.954
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.9
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.98
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : RESTRAINTS
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE REFINEMENT PROCESS USED A NUMBER OF
REMARK 3 FAKE ATOMS AND RESIDUES WHOSE IDENTITY COULD NOT BE
REMARK 3 UNAMBIGUOUSLY ASSIGNED. THESE WERE REMOVED FROM THE STRUCTURE
REMARK 3 THAT WAS DEPOSITED TO THE PDB. THE REFINEMENT STATISTICS HAVE NOT
REMARK 3 BEEN INCLUDED HERE, SINCE THEY DO NOT ACCURATELY REFLECT THE
REMARK 3 REFINEMENT PROCESS FOR THE AVAILABLE STRUCTURE
REMARK 4
REMARK 4 1W5C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-AUG-04.
REMARK 100 THE PDBE ID CODE IS EBI-20669.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 133566
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 56.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.68000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS
REMARK 200 SOFTWARE USED: CCP4, SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 63.75850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 152.81600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 112.30600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 152.81600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 63.75850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 112.30600
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
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: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 72600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 135320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -344.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, O, U, V, X
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: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 68780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 135460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -312.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L, P, S, T, Y
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 THR A 2
REMARK 465 THR A 3
REMARK 465 THR A 4
REMARK 465 LEU A 5
REMARK 465 GLN A 6
REMARK 465 ARG A 7
REMARK 465 ALA A 233
REMARK 465 ASN A 234
REMARK 465 ASP A 342
REMARK 465 LEU A 343
REMARK 465 ALA A 344
REMARK 465 SER A 345
REMARK 465 ALA A 346
REMARK 465 GLU A 347
REMARK 465 SER A 348
REMARK 465 ALA A 349
REMARK 465 PRO A 350
REMARK 465 VAL A 351
REMARK 465 ALA A 352
REMARK 465 MET A 353
REMARK 465 ILE A 354
REMARK 465 ALA A 355
REMARK 465 PRO A 356
REMARK 465 SER A 357
REMARK 465 ILE A 358
REMARK 465 ASN A 359
REMARK 465 GLY A 360
REMARK 465 MET B 1
REMARK 465 TYR B 5
REMARK 465 ILE B 482
REMARK 465 ASP B 483
REMARK 465 PRO B 484
REMARK 465 GLU B 485
REMARK 465 LEU B 486
REMARK 465 SER B 487
REMARK 465 PRO B 488
REMARK 465 GLU B 489
REMARK 465 GLN B 490
REMARK 465 VAL B 491
REMARK 465 GLU B 492
REMARK 465 TRP B 493
REMARK 465 GLY B 494
REMARK 465 PHE B 495
REMARK 465 TYR B 496
REMARK 465 GLN B 497
REMARK 465 LYS B 498
REMARK 465 VAL B 499
REMARK 465 GLY B 500
REMARK 465 ASP B 501
REMARK 465 VAL B 502
REMARK 465 THR B 503
REMARK 465 THR B 504
REMARK 465 ARG B 505
REMARK 465 ARG B 506
REMARK 465 LYS B 507
REMARK 465 GLU B 508
REMARK 465 ALA B 509
REMARK 465 VAL B 510
REMARK 465 MET C 1
REMARK 465 LYS C 2
REMARK 465 THR C 3
REMARK 465 LEU C 4
REMARK 465 SER C 5
REMARK 465 SER C 6
REMARK 465 GLN C 7
REMARK 465 LYS C 8
REMARK 465 ARG C 9
REMARK 465 TYR C 10
REMARK 465 SER C 11
REMARK 465 PRO C 12
REMARK 465 VAL C 13
REMARK 465 VAL C 14
REMARK 465 THR C 15
REMARK 465 LEU C 16
REMARK 465 SER C 17
REMARK 465 SER C 18
REMARK 465 ASN C 19
REMARK 465 SER C 20
REMARK 465 ILE C 459
REMARK 465 ASP C 460
REMARK 465 ARG C 461
REMARK 465 GLU C 462
REMARK 465 SER C 463
REMARK 465 GLU C 464
REMARK 465 PRO C 465
REMARK 465 VAL C 466
REMARK 465 LEU C 467
REMARK 465 SER C 468
REMARK 465 MET C 469
REMARK 465 PRO C 470
REMARK 465 SER C 471
REMARK 465 LEU C 472
REMARK 465 ASP C 473
REMARK 465 ALA D 351
REMARK 465 LEU D 352
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 GLY E 3
REMARK 465 THR E 4
REMARK 465 THR E 5
REMARK 465 GLY E 6
REMARK 465 GLU E 7
REMARK 465 GLU E 71
REMARK 465 THR F 2
REMARK 465 SER F 3
REMARK 465 ASN F 4
REMARK 465 THR F 5
REMARK 465 PRO F 6
REMARK 465 ASN F 7
REMARK 465 GLN F 8
REMARK 465 MET G 1
REMARK 465 THR G 2
REMARK 465 THR G 3
REMARK 465 THR G 4
REMARK 465 LEU G 5
REMARK 465 GLN G 6
REMARK 465 ARG G 7
REMARK 465 ALA G 233
REMARK 465 ASN G 234
REMARK 465 ASP G 342
REMARK 465 LEU G 343
REMARK 465 ALA G 344
REMARK 465 SER G 345
REMARK 465 ALA G 346
REMARK 465 GLU G 347
REMARK 465 SER G 348
REMARK 465 ALA G 349
REMARK 465 PRO G 350
REMARK 465 VAL G 351
REMARK 465 ALA G 352
REMARK 465 MET G 353
REMARK 465 ILE G 354
REMARK 465 ALA G 355
REMARK 465 PRO G 356
REMARK 465 SER G 357
REMARK 465 ILE G 358
REMARK 465 ASN G 359
REMARK 465 GLY G 360
REMARK 465 MET H 0
REMARK 465 GLY H 1
REMARK 465 ILE H 482
REMARK 465 ASP H 483
REMARK 465 PRO H 484
REMARK 465 GLU H 485
REMARK 465 LEU H 486
REMARK 465 SER H 487
REMARK 465 PRO H 488
REMARK 465 GLU H 489
REMARK 465 GLN H 490
REMARK 465 VAL H 491
REMARK 465 GLU H 492
REMARK 465 TRP H 493
REMARK 465 GLY H 494
REMARK 465 PHE H 495
REMARK 465 TYR H 496
REMARK 465 GLN H 497
REMARK 465 LYS H 498
REMARK 465 VAL H 499
REMARK 465 GLY H 500
REMARK 465 ASP H 501
REMARK 465 VAL H 502
REMARK 465 THR H 504
REMARK 465 ARG H 506
REMARK 465 LYS H 507
REMARK 465 GLU H 508
REMARK 465 ALA H 509
REMARK 465 VAL H 510
REMARK 465 MET I 1
REMARK 465 LYS I 2
REMARK 465 THR I 3
REMARK 465 LEU I 4
REMARK 465 SER I 5
REMARK 465 SER I 6
REMARK 465 GLN I 7
REMARK 465 LYS I 8
REMARK 465 ARG I 9
REMARK 465 TYR I 10
REMARK 465 SER I 11
REMARK 465 PRO I 12
REMARK 465 VAL I 13
REMARK 465 VAL I 14
REMARK 465 THR I 15
REMARK 465 LEU I 16
REMARK 465 SER I 17
REMARK 465 SER I 18
REMARK 465 ASN I 19
REMARK 465 SER I 20
REMARK 465 ILE I 459
REMARK 465 ASP I 460
REMARK 465 ARG I 461
REMARK 465 GLU I 462
REMARK 465 SER I 463
REMARK 465 GLU I 464
REMARK 465 PRO I 465
REMARK 465 VAL I 466
REMARK 465 LEU I 467
REMARK 465 SER I 468
REMARK 465 MET I 469
REMARK 465 PRO I 470
REMARK 465 SER I 471
REMARK 465 LEU I 472
REMARK 465 ASP I 473
REMARK 465 ALA J 351
REMARK 465 LEU J 352
REMARK 465 MET K 1
REMARK 465 ALA K 2
REMARK 465 GLY K 3
REMARK 465 THR K 4
REMARK 465 THR K 5
REMARK 465 GLY K 6
REMARK 465 GLU K 7
REMARK 465 GLU K 71
REMARK 465 THR L 2
REMARK 465 SER L 3
REMARK 465 ASN L 4
REMARK 465 THR L 5
REMARK 465 PRO L 6
REMARK 465 ASN L 7
REMARK 465 GLN L 8
REMARK 465 MET T -25
REMARK 465 LEU T -24
REMARK 465 LYS T -23
REMARK 465 LYS T -22
REMARK 465 CYS T -21
REMARK 465 VAL T -20
REMARK 465 TRP T -19
REMARK 465 LEU T -18
REMARK 465 ALA T -17
REMARK 465 VAL T -16
REMARK 465 ALA T -15
REMARK 465 LEU T -14
REMARK 465 CYS T -13
REMARK 465 LEU T -12
REMARK 465 CYS T -11
REMARK 465 LEU T -10
REMARK 465 TRP T -9
REMARK 465 GLN T -8
REMARK 465 PHE T -7
REMARK 465 THR T -6
REMARK 465 MET T -5
REMARK 465 GLY T -4
REMARK 465 THR T -3
REMARK 465 ALA T -2
REMARK 465 LEU T -1
REMARK 465 ALA T 0
REMARK 465 ALA T 1
REMARK 465 MET V -25
REMARK 465 LEU V -24
REMARK 465 LYS V -23
REMARK 465 LYS V -22
REMARK 465 CYS V -21
REMARK 465 VAL V -20
REMARK 465 TRP V -19
REMARK 465 LEU V -18
REMARK 465 ALA V -17
REMARK 465 VAL V -16
REMARK 465 ALA V -15
REMARK 465 LEU V -14
REMARK 465 CYS V -13
REMARK 465 LEU V -12
REMARK 465 CYS V -11
REMARK 465 LEU V -10
REMARK 465 TRP V -9
REMARK 465 GLN V -8
REMARK 465 PHE V -7
REMARK 465 THR V -6
REMARK 465 MET V -5
REMARK 465 GLY V -4
REMARK 465 THR V -3
REMARK 465 ALA V -2
REMARK 465 LEU V -1
REMARK 465 ALA V 0
REMARK 465 ALA V 1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 8 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 9 CG CD OE1 OE2
REMARK 470 SER A 10 OG
REMARK 470 ASN A 12 CG OD1 ND2
REMARK 470 LEU A 13 CG CD1 CD2
REMARK 470 TRP A 14 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 14 CZ3 CH2
REMARK 470 GLU A 15 CG CD OE1 OE2
REMARK 470 ARG A 16 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 17 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 CYS A 18 SG
REMARK 470 ASN A 19 CG OD1 ND2
REMARK 470 TRP A 20 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 20 CZ3 CH2
REMARK 470 VAL A 21 CG1 CG2
REMARK 470 THR A 22 OG1 CG2
REMARK 470 SER A 23 OG
REMARK 470 THR A 24 OG1 CG2
REMARK 470 ASP A 25 N C O CB CG OD1 OD2
REMARK 470 ASN A 26 N C O CB CG OD1 ND2
REMARK 470 ARG A 27 N C O CB CG CD NE
REMARK 470 ARG A 27 CZ NH1 NH2
REMARK 470 LEU A 28 N C O CB CG CD1 CD2
REMARK 470 TYR A 29 N C O CB CG CD1 CD2
REMARK 470 TYR A 29 CE1 CE2 CZ OH
REMARK 470 VAL A 30 N C O CB CG1 CG2
REMARK 470 LEU A 223 N C O CB CG CD1 CD2
REMARK 470 ILE A 224 N C O CB CG1 CG2 CD1
REMARK 470 ARG A 225 N C O CB CG CD NE
REMARK 470 ARG A 225 CZ NH1 NH2
REMARK 470 GLU A 226 N C O CB CG CD OE1
REMARK 470 GLU A 226 OE2
REMARK 470 THR A 227 N C O CB OG1 CG2
REMARK 470 THR A 228 N C O CB OG1 CG2
REMARK 470 GLU A 229 N C O CB CG CD OE1
REMARK 470 GLU A 229 OE2
REMARK 470 THR A 230 N C O CB OG1 CG2
REMARK 470 GLU A 231 N C O CB CG CD OE1
REMARK 470 GLU A 231 OE2
REMARK 470 SER A 232 N C O CB OG
REMARK 470 TYR A 235 N C O CB CG CD1 CD2
REMARK 470 TYR A 235 CE1 CE2 CZ OH
REMARK 470 GLY A 236 N C O
REMARK 470 TYR A 237 N C O CB CG CD1 CD2
REMARK 470 TYR A 237 CE1 CE2 CZ OH
REMARK 470 LYS A 238 N C O CB CG CD CE
REMARK 470 LYS A 238 NZ
REMARK 470 PHE A 239 N C O CB CG CD1 CD2
REMARK 470 PHE A 239 CE1 CE2 CZ
REMARK 470 GLY A 240 N C O
REMARK 470 GLN A 241 N C O CB CG CD OE1
REMARK 470 GLN A 241 NE2
REMARK 470 GLU A 242 N C O CB CG CD OE1
REMARK 470 GLU A 242 OE2
REMARK 470 ARG A 257 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 260 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 261 CG CD OE1 NE2
REMARK 470 TYR A 262 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER A 264 OG
REMARK 470 PHE A 265 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A 266 CG OD1 ND2
REMARK 470 HIS A 304 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 307 CG1 CG2 CD1
REMARK 470 ASN A 335 N C O CB CG OD1 ND2
REMARK 470 ALA A 336 N C O CB
REMARK 470 HIS A 337 N C O CB CG ND1 CD2
REMARK 470 HIS A 337 CE1 NE2
REMARK 470 ASN A 338 N C O CB CG OD1 ND2
REMARK 470 PHE A 339 N C O CB CG CD1 CD2
REMARK 470 PHE A 339 CE1 CE2 CZ
REMARK 470 PRO A 340 N C O CB CG CD
REMARK 470 LEU A 341 N C O CB CG CD1 CD2
REMARK 470 GLY B 2 N C O
REMARK 470 LEU B 3 N C O CB CG CD1 CD2
REMARK 470 PRO B 4 N C O CB CG CD
REMARK 470 TRP B 6 N C O CB CG CD1 CD2
REMARK 470 TRP B 6 NE1 CE2 CE3 CZ2 CZ3 CH2
REMARK 470 ARG B 7 N C O CB CG CD NE
REMARK 470 ARG B 7 CZ NH1 NH2
REMARK 470 VAL B 8 N C O CB CG1 CG2
REMARK 470 HIS B 9 N C O CB CG ND1 CD2
REMARK 470 HIS B 9 CE1 NE2
REMARK 470 THR B 10 N C O CB OG1 CG2
REMARK 470 VAL B 11 N C O CB CG1 CG2
REMARK 470 LEU B 12 N C O CB CG CD1 CD2
REMARK 470 ILE B 13 N C O CB CG1 CG2 CD1
REMARK 470 ASN B 14 N C O CB CG OD1 ND2
REMARK 470 ASP B 15 N C O CB CG OD1 OD2
REMARK 470 TRP B 56 N C O CB CG CD1 CD2
REMARK 470 TRP B 56 NE1 CE2 CE3 CZ2 CZ3 CH2
REMARK 470 ARG B 57 N C O CB CG CD NE
REMARK 470 ARG B 57 CZ NH1 NH2
REMARK 470 GLN B 58 N C O CB CG CD OE1
REMARK 470 GLN B 58 NE2
REMARK 470 GLY B 59 N C O
REMARK 470 MET B 60 N C O CB CG SD CE
REMARK 470 LEU B 63 CG CD1 CD2
REMARK 470 SER B 74 OG
REMARK 470 TRP B 75 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 75 CZ3 CH2
REMARK 470 SER B 76 OG
REMARK 470 THR B 81 N C O CB OG1 CG2
REMARK 470 GLY B 82 N C O
REMARK 470 GLU B 83 N C O CB CG CD OE1
REMARK 470 GLU B 83 OE2
REMARK 470 THR B 84 N C O CB OG1 CG2
REMARK 470 GLY B 85 N C O
REMARK 470 ILE B 86 N C O CB CG1 CG2 CD1
REMARK 470 ASP B 87 N C O CB CG OD1 OD2
REMARK 470 PRO B 88 N C O CB CG CD
REMARK 470 GLY B 89 N C O
REMARK 470 SER B 92 OG
REMARK 470 ASP B 119 N C O CB CG OD1 OD2
REMARK 470 LEU B 120 N C O CB CG CD1 CD2
REMARK 470 GLU B 121 N C O CB CG CD OE1
REMARK 470 GLU B 121 OE2
REMARK 470 LEU B 122 N C O CB CG CD1 CD2
REMARK 470 PHE B 123 N C O CB CG CD1 CD2
REMARK 470 PHE B 123 CE1 CE2 CZ
REMARK 470 ARG B 124 N C O CB CG CD NE
REMARK 470 ARG B 124 CZ NH1 NH2
REMARK 470 ASP B 125 N C O CB CG OD1 OD2
REMARK 470 PRO B 126 N C O CB CG CD
REMARK 470 ARG B 127 N C O CB CG CD NE
REMARK 470 ARG B 127 CZ NH1 NH2
REMARK 470 THR B 128 N C O CB OG1 CG2
REMARK 470 GLY B 129 N C O
REMARK 470 GLU B 130 N C O CB CG CD OE1
REMARK 470 GLU B 130 OE2
REMARK 470 PRO B 131 CG CD
REMARK 470 LEU B 133 CG CD1 CD2
REMARK 470 ASP B 134 CG OD1 OD2
REMARK 470 LYS B 137 CG CD CE NZ
REMARK 470 THR B 159 OG1 CG2
REMARK 470 VAL B 181 N C O CB CG1 CG2
REMARK 470 ALA B 182 N C O CB
REMARK 470 PRO B 183 N C O CB CG CD
REMARK 470 GLU B 184 N C O CB CG CD OE1
REMARK 470 GLU B 184 OE2
REMARK 470 TRP B 185 N C O CB CG CD1 CD2
REMARK 470 TRP B 185 NE1 CE2 CE3 CZ2 CZ3 CH2
REMARK 470 GLY B 186 N C O
REMARK 470 PRO B 187 N C O CB CG CD
REMARK 470 GLN B 223 CG CD OE1 NE2
REMARK 470 ARG B 224 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 225 CG CD1 CD2
REMARK 470 TYR B 226 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 227 CG CD CE NZ
REMARK 470 LEU B 229 CG CD1 CD2
REMARK 470 ARG B 230 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 234 CG1 CG2 CD1
REMARK 470 TYR B 258 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER B 260 OG
REMARK 470 THR B 262 OG1 CG2
REMARK 470 ARG B 287 CG CD NE CZ NH1 NH2
REMARK 470 ALA B 296 N C O CB
REMARK 470 THR B 297 N C O CB OG1 CG2
REMARK 470 LEU B 298 N C O CB CG CD1 CD2
REMARK 470 GLU B 299 N C O CB CG CD OE1
REMARK 470 GLU B 299 OE2
REMARK 470 GLU B 300 N C O CB CG CD OE1
REMARK 470 GLU B 300 OE2
REMARK 470 ALA B 301 N C O CB
REMARK 470 TRP B 302 N C O CB CG CD1 CD2
REMARK 470 TRP B 302 NE1 CE2 CE3 CZ2 CZ3 CH2
REMARK 470 SER B 303 N C O CB OG
REMARK 470 ALA B 304 N C O CB
REMARK 470 ILE B 305 N C O CB CG1 CG2 CD1
REMARK 470 PRO B 306 N C O CB CG CD
REMARK 470 ILE B 315 CG1 CG2 CD1
REMARK 470 LYS B 321 N C O CB CG CD CE
REMARK 470 LYS B 321 NZ
REMARK 470 GLY B 322 N C O
REMARK 470 GLY B 323 N C O
REMARK 470 LEU B 324 N C O CB CG CD1 CD2
REMARK 470 PHE B 325 N C O CB CG CD1 CD2
REMARK 470 PHE B 325 CE1 CE2 CZ
REMARK 470 ARG B 326 N C O CB CG CD NE
REMARK 470 ARG B 326 CZ NH1 NH2
REMARK 470 THR B 327 N C O CB OG1 CG2
REMARK 470 GLY B 328 N C O
REMARK 470 PRO B 329 N C O CB CG CD
REMARK 470 LYS B 332 CG CD CE NZ
REMARK 470 ILE B 336 CG1 CG2 CD1
REMARK 470 GLN B 338 CG CD OE1 NE2
REMARK 470 TRP B 340 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 340 CZ3 CH2
REMARK 470 LYS B 341 CG CD CE NZ
REMARK 470 HIS B 343 CG ND1 CD2 CE1 NE2
REMARK 470 ASN B 348 CG OD1 ND2
REMARK 470 VAL B 368 CG1 CG2
REMARK 470 ILE B 369 CG1 CG2 CD1
REMARK 470 LEU B 370 CG CD1 CD2
REMARK 470 THR B 371 OG1 CG2
REMARK 470 ASP B 372 CG OD1 OD2
REMARK 470 LYS B 373 CG CD CE NZ
REMARK 470 ASN B 374 CG OD1 ND2
REMARK 470 VAL B 376 CG1 CG2
REMARK 470 VAL B 377 CG1 CG2
REMARK 470 LYS B 378 CG CD CE NZ
REMARK 470 ASP B 380 CG OD1 OD2
REMARK 470 ILE B 381 CG1 CG2 CD1
REMARK 470 PRO B 382 CG CD
REMARK 470 PHE B 383 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 384 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 385 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 387 CG CD OE1 OE2
REMARK 470 SER B 388 OG
REMARK 470 LYS B 389 CG CD CE NZ
REMARK 470 TYR B 390 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER B 391 OG
REMARK 470 PHE B 392 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 393 CG CD OE1 OE2
REMARK 470 GLN B 394 CG CD OE1 NE2
REMARK 470 GLN B 395 CG CD OE1 NE2
REMARK 470 VAL B 397 CG1 CG2
REMARK 470 THR B 398 OG1 CG2
REMARK 470 VAL B 399 CG1 CG2
REMARK 470 PHE B 430 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 431 CG CD OE1 OE2
REMARK 470 PHE B 432 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP B 433 O CG OD1 OD2
REMARK 470 THR B 434 OG1 CG2
REMARK 470 GLU B 435 CG CD OE1 OE2
REMARK 470 THR B 436 OG1 CG2
REMARK 470 ASP B 440 CG OD1 OD2
REMARK 470 ARG B 476 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 477 CG OD1 OD2
REMARK 470 VAL B 478 CG1 CG2
REMARK 470 PHE B 479 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER B 480 OG
REMARK 470 ILE C 21 CG1 CG2 CD1
REMARK 470 PHE C 22 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR C 24 OG1 CG2
REMARK 470 ASN C 25 CG OD1 ND2
REMARK 470 ARG C 26 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 27 CG OD1 OD2
REMARK 470 GLN C 28 CG CD OE1 NE2
REMARK 470 GLU C 29 CG CD OE1 OE2
REMARK 470 LEU C 42 CG CD1 CD2
REMARK 470 LYS C 48 CG CD CE NZ
REMARK 470 LEU C 49 CG CD1 CD2
REMARK 470 GLU C 71 CG CD OE1 OE2
REMARK 470 GLN C 84 CG CD OE1 NE2
REMARK 470 LEU C 86 CG CD1 CD2
REMARK 470 ILE C 87 CG1 CG2 CD1
REMARK 470 LEU C 88 CG CD1 CD2
REMARK 470 VAL C 99 CG1 CG2
REMARK 470 PRO C 101 CG CD
REMARK 470 GLU C 104 CG CD OE1 OE2
REMARK 470 VAL C 105 CG1 CG2
REMARK 470 VAL C 106 CG1 CG2
REMARK 470 TYR C 131 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR C 139 N C O CB OG1 CG2
REMARK 470 LEU C 140 N C O CB CG CD1 CD2
REMARK 470 GLU C 141 N C O CB CG CD OE1
REMARK 470 GLU C 141 OE2
REMARK 470 GLU C 142 N C O CB CG CD OE1
REMARK 470 GLU C 142 OE2
REMARK 470 TYR C 143 N C O CB CG CD1 CD2
REMARK 470 TYR C 143 CE1 CE2 CZ OH
REMARK 470 SER C 144 N C O CB OG
REMARK 470 SER C 145 N C O CB OG
REMARK 470 PHE C 146 N C O CB CG CD1 CD2
REMARK 470 PHE C 146 CE1 CE2 CZ
REMARK 470 PHE C 147 N C O CB CG CD1 CD2
REMARK 470 PHE C 147 CE1 CE2 CZ
REMARK 470 GLY C 148 N C O
REMARK 470 TYR C 149 N C O CB CG CD1 CD2
REMARK 470 TYR C 149 CE1 CE2 CZ OH
REMARK 470 ASP C 150 CG OD1 OD2
REMARK 470 LYS C 152 CG CD CE NZ
REMARK 470 LEU C 165 CG CD1 CD2
REMARK 470 LEU C 185 CG CD1 CD2
REMARK 470 PRO C 191 N C O CB CG CD
REMARK 470 GLY C 192 N C O
REMARK 470 GLY C 193 N C O
REMARK 470 GLY C 194 N C O
REMARK 470 ASP C 195 N C O CB CG OD1 OD2
REMARK 470 VAL C 196 N C O CB CG1 CG2
REMARK 470 ARG C 197 N C O CB CG CD NE
REMARK 470 ARG C 197 CZ NH1 NH2
REMARK 470 VAL C 198 N C O CB CG1 CG2
REMARK 470 ILE C 199 N C O CB CG1 CG2 CD1
REMARK 470 THR C 200 N C O CB OG1 CG2
REMARK 470 ASN C 201 N C O CB CG OD1 ND2
REMARK 470 PRO C 202 N C O CB CG CD
REMARK 470 THR C 203 N C O CB OG1 CG2
REMARK 470 LEU C 204 N C O CB CG CD1 CD2
REMARK 470 ASP C 205 N C O CB CG OD1 OD2
REMARK 470 PRO C 206 N C O CB CG CD
REMARK 470 ARG C 207 CG CD NE CZ NH1 NH2
REMARK 470 VAL C 208 CG1 CG2
REMARK 470 ILE C 209 CG1 CG2 CD1
REMARK 470 PHE C 210 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR C 212 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU C 213 N C O CB CG CD1 CD2
REMARK 470 LEU C 214 N C O CB CG CD1 CD2
REMARK 470 LYS C 215 N C O CB CG CD CE
REMARK 470 LYS C 215 NZ
REMARK 470 SER C 216 N C O CB OG
REMARK 470 PRO C 217 N C O CB CG CD
REMARK 470 PHE C 218 N C O CB CG CD1 CD2
REMARK 470 PHE C 218 CE1 CE2 CZ
REMARK 470 GLY C 219 N C O
REMARK 470 GLY C 220 N C O
REMARK 470 GLU C 221 N C O CB CG CD OE1
REMARK 470 GLU C 221 OE2
REMARK 470 GLY C 222 N C O
REMARK 470 TRP C 223 N C O CB CG CD1 CD2
REMARK 470 TRP C 223 NE1 CE2 CE3 CZ2 CZ3 CH2
REMARK 470 ILE C 224 N C O CB CG1 CG2 CD1
REMARK 470 THR C 254 OG1 CG2
REMARK 470 ASN C 293 CG OD1 ND2
REMARK 470 GLU C 308 CG CD OE1 OE2
REMARK 470 ASP C 321 CG OD1 OD2
REMARK 470 MET C 342 N C O CB CG SD CE
REMARK 470 ARG C 343 N C O CB CG CD NE
REMARK 470 ARG C 343 CZ NH1 NH2
REMARK 470 SER C 344 N C O CB OG
REMARK 470 PRO C 345 N C O CB CG CD
REMARK 470 THR C 346 N C O CB OG1 CG2
REMARK 470 GLY C 347 N C O
REMARK 470 GLU C 348 N C O CB CG CD OE1
REMARK 470 GLU C 348 OE2
REMARK 470 ILE C 349 N C O CB CG1 CG2 CD1
REMARK 470 ILE C 350 N C O CB CG1 CG2 CD1
REMARK 470 PHE C 351 N C O CB CG CD1 CD2
REMARK 470 PHE C 351 CE1 CE2 CZ
REMARK 470 GLY C 352 N C O
REMARK 470 GLY C 353 N C O
REMARK 470 GLU C 354 CG CD OE1 OE2
REMARK 470 ARG C 357 CG CD NE CZ NH1 NH2
REMARK 470 THR C 397 OG1 CG2
REMARK 470 ALA C 399 N C O CB
REMARK 470 PRO C 400 N C O CB CG CD
REMARK 470 LEU C 401 N C O CB CG CD1 CD2
REMARK 470 GLY C 402 N C O
REMARK 470 SER C 403 N C O CB OG
REMARK 470 LEU C 404 N C O CB CG CD1 CD2
REMARK 470 ASN C 405 N C O CB CG OD1 ND2
REMARK 470 SER C 406 N C O CB OG
REMARK 470 VAL C 407 N C O CB CG1 CG2
REMARK 470 GLY C 408 N C O
REMARK 470 GLY C 409 N C O
REMARK 470 VAL C 410 N C O CB CG1 CG2
REMARK 470 ALA C 411 N C O CB
REMARK 470 THR C 412 N C O CB OG1 CG2
REMARK 470 GLU C 413 N C O CB CG CD OE1
REMARK 470 GLU C 413 OE2
REMARK 470 ILE C 414 N C O CB CG1 CG2 CD1
REMARK 470 ASN C 415 N C O CB CG OD1 ND2
REMARK 470 SER C 416 N C O CB OG
REMARK 470 VAL C 417 N C O CB CG1 CG2
REMARK 470 ASN C 418 N C O CB CG OD1 ND2
REMARK 470 SER C 421 OG
REMARK 470 LYS C 457 N C O CB CG CD CE
REMARK 470 LYS C 457 NZ
REMARK 470 GLY C 458 N C O
REMARK 470 MET D 1 CG SD CE
REMARK 470 THR D 2 OG1 CG2
REMARK 470 ILE D 3 CG1 CG2 CD1
REMARK 470 ILE D 5 CG1 CG2 CD1
REMARK 470 ARG D 7 CG CD NE CZ NH1 NH2
REMARK 470 PRO D 9 CG CD
REMARK 470 GLU D 11 CG CD OE1 OE2
REMARK 470 ARG D 12 CG CD NE CZ NH1 NH2
REMARK 470 TRP D 14 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 14 CZ3 CH2
REMARK 470 PHE D 15 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP D 16 CG OD1 OD2
REMARK 470 ILE D 17 CG1 CG2 CD1
REMARK 470 LEU D 18 CG CD1 CD2
REMARK 470 ASP D 19 CG OD1 OD2
REMARK 470 ASP D 20 CG OD1 OD2
REMARK 470 TRP D 21 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 21 CZ3 CH2
REMARK 470 LEU D 22 CG CD1 CD2
REMARK 470 LYS D 23 CG CD CE NZ
REMARK 470 ARG D 24 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 25 CG OD1 OD2
REMARK 470 ARG D 26 CG CD NE CZ NH1 NH2
REMARK 470 PHE D 27 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL D 28 CG1 CG2
REMARK 470 PHE D 29 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL D 30 CG1 CG2
REMARK 470 LEU D 89 CG CD1 CD2
REMARK 470 GLN D 98 CG CD OE1 NE2
REMARK 470 ASP D 100 CG OD1 OD2
REMARK 470 GLU D 227 CG CD OE1 OE2
REMARK 470 SER D 230 OG
REMARK 470 THR D 231 OG1 CG2
REMARK 470 PHE D 232 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 233 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 239 CG CD OE1 NE2
REMARK 470 ARG D 251 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 265 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 304 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 334 CG CD OE1 NE2
REMARK 470 ASN D 338 CG OD1 ND2
REMARK 470 LEU D 346 CG CD1 CD2
REMARK 470 PRO D 347 CG CD
REMARK 470 ARG D 348 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 350 CG OD1 ND2
REMARK 470 ASP E 12 CG OD1 OD2
REMARK 470 LEU E 65 CG CD1 CD2
REMARK 470 VAL E 66 N C O CB CG1 CG2
REMARK 470 THR E 67 N C O CB OG1 CG2
REMARK 470 ASP E 68 N C O CB CG OD1 OD2
REMARK 470 ARG E 69 N C O CB CG CD NE
REMARK 470 ARG E 69 CZ NH1 NH2
REMARK 470 PHE E 70 N C O CB CG CD1 CD2
REMARK 470 PHE E 70 CE1 CE2 CZ
REMARK 470 LYS E 73 CG CD CE NZ
REMARK 470 GLN E 74 CG CD OE1 NE2
REMARK 470 GLN E 75 CG CD OE1 NE2
REMARK 470 VAL E 76 CG1 CG2
REMARK 470 GLU E 77 CG CD OE1 OE2
REMARK 470 THR E 78 OG1 CG2
REMARK 470 PHE E 79 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU E 80 CG CD1 CD2
REMARK 470 GLU E 81 CG CD OE1 OE2
REMARK 470 GLN E 82 CG CD OE1 NE2
REMARK 470 LEU E 83 CG CD1 CD2
REMARK 470 LYS E 84 CG CD CE NZ
REMARK 470 ARG G 8 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 9 CG CD OE1 OE2
REMARK 470 SER G 10 OG
REMARK 470 ASN G 12 CG OD1 ND2
REMARK 470 LEU G 13 CG CD1 CD2
REMARK 470 TRP G 14 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP G 14 CZ3 CH2
REMARK 470 GLU G 15 CG CD OE1 OE2
REMARK 470 ARG G 16 CG CD NE CZ NH1 NH2
REMARK 470 PHE G 17 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 CYS G 18 SG
REMARK 470 ASN G 19 CG OD1 ND2
REMARK 470 TRP G 20 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP G 20 CZ3 CH2
REMARK 470 VAL G 21 CG1 CG2
REMARK 470 THR G 22 OG1 CG2
REMARK 470 SER G 23 OG
REMARK 470 THR G 24 OG1 CG2
REMARK 470 ASP G 25 N C O CB CG OD1 OD2
REMARK 470 ASN G 26 N C O CB CG OD1 ND2
REMARK 470 ARG G 27 N C O CB CG CD NE
REMARK 470 ARG G 27 CZ NH1 NH2
REMARK 470 LEU G 28 N C O CB CG CD1 CD2
REMARK 470 TYR G 29 N C O CB CG CD1 CD2
REMARK 470 TYR G 29 CE1 CE2 CZ OH
REMARK 470 VAL G 30 N C O CB CG1 CG2
REMARK 470 LEU G 223 N C O CB CG CD1 CD2
REMARK 470 ILE G 224 N C O CB CG1 CG2 CD1
REMARK 470 ARG G 225 N C O CB CG CD NE
REMARK 470 ARG G 225 CZ NH1 NH2
REMARK 470 GLU G 226 N C O CB CG CD OE1
REMARK 470 GLU G 226 OE2
REMARK 470 THR G 227 N C O CB OG1 CG2
REMARK 470 THR G 228 N C O CB OG1 CG2
REMARK 470 GLU G 229 N C O CB CG CD OE1
REMARK 470 GLU G 229 OE2
REMARK 470 THR G 230 N C O CB OG1 CG2
REMARK 470 GLU G 231 N C O CB CG CD OE1
REMARK 470 GLU G 231 OE2
REMARK 470 SER G 232 N C O CB OG
REMARK 470 TYR G 235 N C O CB CG CD1 CD2
REMARK 470 TYR G 235 CE1 CE2 CZ OH
REMARK 470 GLY G 236 N C O
REMARK 470 TYR G 237 N C O CB CG CD1 CD2
REMARK 470 TYR G 237 CE1 CE2 CZ OH
REMARK 470 LYS G 238 N C O CB CG CD CE
REMARK 470 LYS G 238 NZ
REMARK 470 PHE G 239 N C O CB CG CD1 CD2
REMARK 470 PHE G 239 CE1 CE2 CZ
REMARK 470 GLY G 240 N C O
REMARK 470 GLN G 241 N C O CB CG CD OE1
REMARK 470 GLN G 241 NE2
REMARK 470 GLU G 242 N C O CB CG CD OE1
REMARK 470 GLU G 242 OE2
REMARK 470 ARG G 257 CG CD NE CZ NH1 NH2
REMARK 470 PHE G 260 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN G 261 CG CD OE1 NE2
REMARK 470 TYR G 262 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER G 264 OG
REMARK 470 PHE G 265 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN G 266 CG OD1 ND2
REMARK 470 HIS G 304 CG ND1 CD2 CE1 NE2
REMARK 470 ILE G 307 CG1 CG2 CD1
REMARK 470 ASN G 335 N C O CB CG OD1 ND2
REMARK 470 ALA G 336 N C O CB
REMARK 470 HIS G 337 N C O CB CG ND1 CD2
REMARK 470 HIS G 337 CE1 NE2
REMARK 470 ASN G 338 N C O CB CG OD1 ND2
REMARK 470 PHE G 339 N C O CB CG CD1 CD2
REMARK 470 PHE G 339 CE1 CE2 CZ
REMARK 470 PRO G 340 N C O CB CG CD
REMARK 470 LEU G 341 N C O CB CG CD1 CD2
REMARK 470 LEU H 2 N C O CB CG CD1 CD2
REMARK 470 PRO H 3 N C O CB CG CD
REMARK 470 TRP H 4 N C O CB CG CD1 CD2
REMARK 470 TRP H 4 NE1 CE2 CE3 CZ2 CZ3 CH2
REMARK 470 TYR H 5 N C O CB CG CD1 CD2
REMARK 470 TYR H 5 CE1 CE2 CZ OH
REMARK 470 ARG H 7 N C O CB CG CD NE
REMARK 470 ARG H 7 CZ NH1 NH2
REMARK 470 VAL H 8 N C O CB CG1 CG2
REMARK 470 HIS H 9 N C O CB CG ND1 CD2
REMARK 470 HIS H 9 CE1 NE2
REMARK 470 THR H 10 N C O CB OG1 CG2
REMARK 470 VAL H 11 N C O CB CG1 CG2
REMARK 470 LEU H 12 N C O CB CG CD1 CD2
REMARK 470 ILE H 13 N C O CB CG1 CG2 CD1
REMARK 470 ASN H 14 N C O CB CG OD1 ND2
REMARK 470 ASP H 15 N C O CB CG OD1 OD2
REMARK 470 TRP H 56 N C O CB CG CD1 CD2
REMARK 470 TRP H 56 NE1 CE2 CE3 CZ2 CZ3 CH2
REMARK 470 ARG H 57 N C O CB CG CD NE
REMARK 470 ARG H 57 CZ NH1 NH2
REMARK 470 GLN H 58 N C O CB CG CD OE1
REMARK 470 GLN H 58 NE2
REMARK 470 GLY H 59 N C O
REMARK 470 MET H 60 N C O CB CG SD CE
REMARK 470 LEU H 63 CG CD1 CD2
REMARK 470 SER H 74 OG
REMARK 470 TRP H 75 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP H 75 CZ3 CH2
REMARK 470 SER H 76 OG
REMARK 470 THR H 81 N C O CB OG1 CG2
REMARK 470 GLY H 82 N C O
REMARK 470 GLU H 83 N C O CB CG CD OE1
REMARK 470 GLU H 83 OE2
REMARK 470 THR H 84 N C O CB OG1 CG2
REMARK 470 GLY H 85 N C O
REMARK 470 ILE H 86 N C O CB CG1 CG2 CD1
REMARK 470 ASP H 87 N C O CB CG OD1 OD2
REMARK 470 PRO H 88 N C O CB CG CD
REMARK 470 GLY H 89 N C O
REMARK 470 SER H 92 OG
REMARK 470 ASP H 119 N C O CB CG OD1 OD2
REMARK 470 LEU H 120 N C O CB CG CD1 CD2
REMARK 470 GLU H 121 N C O CB CG CD OE1
REMARK 470 GLU H 121 OE2
REMARK 470 LEU H 122 N C O CB CG CD1 CD2
REMARK 470 PHE H 123 N C O CB CG CD1 CD2
REMARK 470 PHE H 123 CE1 CE2 CZ
REMARK 470 ARG H 124 N C O CB CG CD NE
REMARK 470 ARG H 124 CZ NH1 NH2
REMARK 470 ASP H 125 N C O CB CG OD1 OD2
REMARK 470 PRO H 126 N C O CB CG CD
REMARK 470 ARG H 127 N C O CB CG CD NE
REMARK 470 ARG H 127 CZ NH1 NH2
REMARK 470 THR H 128 N C O CB OG1 CG2
REMARK 470 GLY H 129 N C O
REMARK 470 GLU H 130 N C O CB CG CD OE1
REMARK 470 GLU H 130 OE2
REMARK 470 PRO H 131 CG CD
REMARK 470 LEU H 133 CG CD1 CD2
REMARK 470 ASP H 134 CG OD1 OD2
REMARK 470 LYS H 137 CG CD CE NZ
REMARK 470 THR H 159 OG1 CG2
REMARK 470 VAL H 181 N C O CB CG1 CG2
REMARK 470 ALA H 182 N C O CB
REMARK 470 PRO H 183 N C O CB CG CD
REMARK 470 GLU H 184 N C O CB CG CD OE1
REMARK 470 GLU H 184 OE2
REMARK 470 TRP H 185 N C O CB CG CD1 CD2
REMARK 470 TRP H 185 NE1 CE2 CE3 CZ2 CZ3 CH2
REMARK 470 GLY H 186 N C O
REMARK 470 PRO H 187 N C O CB CG CD
REMARK 470 GLN H 223 CG CD OE1 NE2
REMARK 470 ARG H 224 CG CD NE CZ NH1 NH2
REMARK 470 LEU H 225 CG CD1 CD2
REMARK 470 TYR H 226 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS H 227 CG CD CE NZ
REMARK 470 LEU H 229 CG CD1 CD2
REMARK 470 ARG H 230 CG CD NE CZ NH1 NH2
REMARK 470 ILE H 234 CG1 CG2 CD1
REMARK 470 TYR H 258 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER H 260 OG
REMARK 470 THR H 262 OG1 CG2
REMARK 470 ARG H 287 CG CD NE CZ NH1 NH2
REMARK 470 ALA H 296 N C O CB
REMARK 470 THR H 297 N C O CB OG1 CG2
REMARK 470 LEU H 298 N C O CB CG CD1 CD2
REMARK 470 GLU H 299 N C O CB CG CD OE1
REMARK 470 GLU H 299 OE2
REMARK 470 GLU H 300 N C O CB CG CD OE1
REMARK 470 GLU H 300 OE2
REMARK 470 ALA H 301 N C O CB
REMARK 470 TRP H 302 N C O CB CG CD1 CD2
REMARK 470 TRP H 302 NE1 CE2 CE3 CZ2 CZ3 CH2
REMARK 470 SER H 303 N C O CB OG
REMARK 470 ALA H 304 N C O CB
REMARK 470 ILE H 305 N C O CB CG1 CG2 CD1
REMARK 470 PRO H 306 N C O CB CG CD
REMARK 470 ILE H 315 CG1 CG2 CD1
REMARK 470 LYS H 321 N C O CB CG CD CE
REMARK 470 LYS H 321 NZ
REMARK 470 GLY H 322 N C O
REMARK 470 GLY H 323 N C O
REMARK 470 LEU H 324 N C O CB CG CD1 CD2
REMARK 470 PHE H 325 N C O CB CG CD1 CD2
REMARK 470 PHE H 325 CE1 CE2 CZ
REMARK 470 ARG H 326 N C O CB CG CD NE
REMARK 470 ARG H 326 CZ NH1 NH2
REMARK 470 THR H 327 N C O CB OG1 CG2
REMARK 470 GLY H 328 N C O
REMARK 470 PRO H 329 N C O CB CG CD
REMARK 470 LYS H 332 CG CD CE NZ
REMARK 470 ILE H 336 CG1 CG2 CD1
REMARK 470 GLN H 338 CG CD OE1 NE2
REMARK 470 TRP H 340 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP H 340 CZ3 CH2
REMARK 470 LYS H 341 CG CD CE NZ
REMARK 470 HIS H 343 CG ND1 CD2 CE1 NE2
REMARK 470 ASN H 348 CG OD1 ND2
REMARK 470 VAL H 368 CG1 CG2
REMARK 470 ILE H 369 CG1 CG2 CD1
REMARK 470 LEU H 370 CG CD1 CD2
REMARK 470 THR H 371 OG1 CG2
REMARK 470 ASP H 372 CG OD1 OD2
REMARK 470 LYS H 373 CG CD CE NZ
REMARK 470 ASN H 374 CG OD1 ND2
REMARK 470 VAL H 376 CG1 CG2
REMARK 470 VAL H 377 CG1 CG2
REMARK 470 LYS H 378 CG CD CE NZ
REMARK 470 ASP H 380 CG OD1 OD2
REMARK 470 ILE H 381 CG1 CG2 CD1
REMARK 470 PRO H 382 CG CD
REMARK 470 PHE H 383 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG H 384 CG CD NE CZ NH1 NH2
REMARK 470 ARG H 385 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 387 CG CD OE1 OE2
REMARK 470 SER H 388 OG
REMARK 470 LYS H 389 CG CD CE NZ
REMARK 470 TYR H 390 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER H 391 OG
REMARK 470 PHE H 392 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU H 393 CG CD OE1 OE2
REMARK 470 GLN H 394 CG CD OE1 NE2
REMARK 470 GLN H 395 CG CD OE1 NE2
REMARK 470 VAL H 397 CG1 CG2
REMARK 470 THR H 398 OG1 CG2
REMARK 470 VAL H 399 CG1 CG2
REMARK 470 PHE H 430 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU H 431 CG CD OE1 OE2
REMARK 470 PHE H 432 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP H 433 O CG OD1 OD2
REMARK 470 THR H 434 OG1 CG2
REMARK 470 GLU H 435 CG CD OE1 OE2
REMARK 470 THR H 436 OG1 CG2
REMARK 470 ASP H 440 CG OD1 OD2
REMARK 470 ARG H 476 CG CD NE CZ NH1 NH2
REMARK 470 ASP H 477 CG OD1 OD2
REMARK 470 VAL H 478 CG1 CG2
REMARK 470 PHE H 479 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER H 480 OG
REMARK 470 ILE I 21 CG1 CG2 CD1
REMARK 470 PHE I 22 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR I 24 OG1 CG2
REMARK 470 ASN I 25 CG OD1 ND2
REMARK 470 ARG I 26 CG CD NE CZ NH1 NH2
REMARK 470 ASP I 27 CG OD1 OD2
REMARK 470 GLN I 28 CG CD OE1 NE2
REMARK 470 GLU I 29 CG CD OE1 OE2
REMARK 470 LEU I 42 CG CD1 CD2
REMARK 470 LYS I 48 CG CD CE NZ
REMARK 470 LEU I 49 CG CD1 CD2
REMARK 470 GLU I 71 CG CD OE1 OE2
REMARK 470 GLN I 84 CG CD OE1 NE2
REMARK 470 LEU I 86 CG CD1 CD2
REMARK 470 ILE I 87 CG1 CG2 CD1
REMARK 470 LEU I 88 CG CD1 CD2
REMARK 470 VAL I 99 CG1 CG2
REMARK 470 PRO I 101 CG CD
REMARK 470 GLU I 104 CG CD OE1 OE2
REMARK 470 VAL I 105 CG1 CG2
REMARK 470 VAL I 106 CG1 CG2
REMARK 470 TYR I 131 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR I 139 N C O CB OG1 CG2
REMARK 470 LEU I 140 N C O CB CG CD1 CD2
REMARK 470 GLU I 141 N C O CB CG CD OE1
REMARK 470 GLU I 141 OE2
REMARK 470 GLU I 142 N C O CB CG CD OE1
REMARK 470 GLU I 142 OE2
REMARK 470 TYR I 143 N C O CB CG CD1 CD2
REMARK 470 TYR I 143 CE1 CE2 CZ OH
REMARK 470 SER I 144 N C O CB OG
REMARK 470 SER I 145 N C O CB OG
REMARK 470 PHE I 146 N C O CB CG CD1 CD2
REMARK 470 PHE I 146 CE1 CE2 CZ
REMARK 470 PHE I 147 N C O CB CG CD1 CD2
REMARK 470 PHE I 147 CE1 CE2 CZ
REMARK 470 GLY I 148 N C O
REMARK 470 TYR I 149 N C O CB CG CD1 CD2
REMARK 470 TYR I 149 CE1 CE2 CZ OH
REMARK 470 ASP I 150 CG OD1 OD2
REMARK 470 LYS I 152 CG CD CE NZ
REMARK 470 LEU I 165 CG CD1 CD2
REMARK 470 LEU I 185 CG CD1 CD2
REMARK 470 PRO I 191 N C O CB CG CD
REMARK 470 GLY I 192 N C O
REMARK 470 GLY I 193 N C O
REMARK 470 GLY I 194 N C O
REMARK 470 ASP I 195 N C O CB CG OD1 OD2
REMARK 470 VAL I 196 N C O CB CG1 CG2
REMARK 470 ARG I 197 N C O CB CG CD NE
REMARK 470 ARG I 197 CZ NH1 NH2
REMARK 470 VAL I 198 N C O CB CG1 CG2
REMARK 470 ILE I 199 N C O CB CG1 CG2 CD1
REMARK 470 THR I 200 N C O CB OG1 CG2
REMARK 470 ASN I 201 N C O CB CG OD1 ND2
REMARK 470 PRO I 202 N C O CB CG CD
REMARK 470 THR I 203 N C O CB OG1 CG2
REMARK 470 LEU I 204 N C O CB CG CD1 CD2
REMARK 470 ASP I 205 N C O CB CG OD1 OD2
REMARK 470 PRO I 206 N C O CB CG CD
REMARK 470 ARG I 207 CG CD NE CZ NH1 NH2
REMARK 470 VAL I 208 CG1 CG2
REMARK 470 ILE I 209 CG1 CG2 CD1
REMARK 470 PHE I 210 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR I 212 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU I 213 N C O CB CG CD1 CD2
REMARK 470 LEU I 214 N C O CB CG CD1 CD2
REMARK 470 LYS I 215 N C O CB CG CD CE
REMARK 470 LYS I 215 NZ
REMARK 470 SER I 216 N C O CB OG
REMARK 470 PRO I 217 N C O CB CG CD
REMARK 470 PHE I 218 N C O CB CG CD1 CD2
REMARK 470 PHE I 218 CE1 CE2 CZ
REMARK 470 GLY I 219 N C O
REMARK 470 GLY I 220 N C O
REMARK 470 GLU I 221 N C O CB CG CD OE1
REMARK 470 GLU I 221 OE2
REMARK 470 GLY I 222 N C O
REMARK 470 TRP I 223 N C O CB CG CD1 CD2
REMARK 470 TRP I 223 NE1 CE2 CE3 CZ2 CZ3 CH2
REMARK 470 ILE I 224 N C O CB CG1 CG2 CD1
REMARK 470 THR I 254 OG1 CG2
REMARK 470 ASN I 293 CG OD1 ND2
REMARK 470 GLU I 308 CG CD OE1 OE2
REMARK 470 ASP I 321 CG OD1 OD2
REMARK 470 MET I 342 N C O CB CG SD CE
REMARK 470 ARG I 343 N C O CB CG CD NE
REMARK 470 ARG I 343 CZ NH1 NH2
REMARK 470 SER I 344 N C O CB OG
REMARK 470 PRO I 345 N C O CB CG CD
REMARK 470 THR I 346 N C O CB OG1 CG2
REMARK 470 GLY I 347 N C O
REMARK 470 GLU I 348 N C O CB CG CD OE1
REMARK 470 GLU I 348 OE2
REMARK 470 ILE I 349 N C O CB CG1 CG2 CD1
REMARK 470 ILE I 350 N C O CB CG1 CG2 CD1
REMARK 470 PHE I 351 N C O CB CG CD1 CD2
REMARK 470 PHE I 351 CE1 CE2 CZ
REMARK 470 GLY I 352 N C O
REMARK 470 GLY I 353 N C O
REMARK 470 GLU I 354 CG CD OE1 OE2
REMARK 470 ARG I 357 CG CD NE CZ NH1 NH2
REMARK 470 THR I 397 OG1 CG2
REMARK 470 ALA I 399 N C O CB
REMARK 470 PRO I 400 N C O CB CG CD
REMARK 470 LEU I 401 N C O CB CG CD1 CD2
REMARK 470 GLY I 402 N C O
REMARK 470 SER I 403 N C O CB OG
REMARK 470 LEU I 404 N C O CB CG CD1 CD2
REMARK 470 ASN I 405 N C O CB CG OD1 ND2
REMARK 470 SER I 406 N C O CB OG
REMARK 470 VAL I 407 N C O CB CG1 CG2
REMARK 470 GLY I 408 N C O
REMARK 470 GLY I 409 N C O
REMARK 470 VAL I 410 N C O CB CG1 CG2
REMARK 470 ALA I 411 N C O CB
REMARK 470 THR I 412 N C O CB OG1 CG2
REMARK 470 GLU I 413 N C O CB CG CD OE1
REMARK 470 GLU I 413 OE2
REMARK 470 ILE I 414 N C O CB CG1 CG2 CD1
REMARK 470 ASN I 415 N C O CB CG OD1 ND2
REMARK 470 SER I 416 N C O CB OG
REMARK 470 VAL I 417 N C O CB CG1 CG2
REMARK 470 ASN I 418 N C O CB CG OD1 ND2
REMARK 470 SER I 421 OG
REMARK 470 LYS I 457 N C O CB CG CD CE
REMARK 470 LYS I 457 NZ
REMARK 470 GLY I 458 N C O
REMARK 470 MET J 1 CG SD CE
REMARK 470 THR J 2 OG1 CG2
REMARK 470 ILE J 3 CG1 CG2 CD1
REMARK 470 ILE J 5 CG1 CG2 CD1
REMARK 470 ARG J 7 CG CD NE CZ NH1 NH2
REMARK 470 PRO J 9 CG CD
REMARK 470 GLU J 11 CG CD OE1 OE2
REMARK 470 ARG J 12 CG CD NE CZ NH1 NH2
REMARK 470 TRP J 14 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP J 14 CZ3 CH2
REMARK 470 PHE J 15 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP J 16 CG OD1 OD2
REMARK 470 ILE J 17 CG1 CG2 CD1
REMARK 470 LEU J 18 CG CD1 CD2
REMARK 470 ASP J 19 CG OD1 OD2
REMARK 470 ASP J 20 CG OD1 OD2
REMARK 470 TRP J 21 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP J 21 CZ3 CH2
REMARK 470 LEU J 22 CG CD1 CD2
REMARK 470 LYS J 23 CG CD CE NZ
REMARK 470 ARG J 24 CG CD NE CZ NH1 NH2
REMARK 470 ASP J 25 CG OD1 OD2
REMARK 470 ARG J 26 CG CD NE CZ NH1 NH2
REMARK 470 PHE J 27 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL J 28 CG1 CG2
REMARK 470 PHE J 29 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL J 30 CG1 CG2
REMARK 470 LEU J 89 CG CD1 CD2
REMARK 470 GLN J 98 CG CD OE1 NE2
REMARK 470 ASP J 100 CG OD1 OD2
REMARK 470 GLU J 227 CG CD OE1 OE2
REMARK 470 SER J 230 OG
REMARK 470 THR J 231 OG1 CG2
REMARK 470 PHE J 232 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG J 233 CG CD NE CZ NH1 NH2
REMARK 470 GLN J 239 CG CD OE1 NE2
REMARK 470 ARG J 251 CG CD NE CZ NH1 NH2
REMARK 470 ARG J 265 CG CD NE CZ NH1 NH2
REMARK 470 ARG J 304 CG CD NE CZ NH1 NH2
REMARK 470 GLN J 334 CG CD OE1 NE2
REMARK 470 ASN J 338 CG OD1 ND2
REMARK 470 LEU J 346 CG CD1 CD2
REMARK 470 PRO J 347 CG CD
REMARK 470 ARG J 348 CG CD NE CZ NH1 NH2
REMARK 470 ASN J 350 CG OD1 ND2
REMARK 470 ASP K 12 CG OD1 OD2
REMARK 470 LEU K 65 CG CD1 CD2
REMARK 470 VAL K 66 N C O CB CG1 CG2
REMARK 470 THR K 67 N C O CB OG1 CG2
REMARK 470 ASP K 68 N C O CB CG OD1 OD2
REMARK 470 ARG K 69 N C O CB CG CD NE
REMARK 470 ARG K 69 CZ NH1 NH2
REMARK 470 PHE K 70 N C O CB CG CD1 CD2
REMARK 470 PHE K 70 CE1 CE2 CZ
REMARK 470 LYS K 73 CG CD CE NZ
REMARK 470 GLN K 74 CG CD OE1 NE2
REMARK 470 GLN K 75 CG CD OE1 NE2
REMARK 470 VAL K 76 CG1 CG2
REMARK 470 GLU K 77 CG CD OE1 OE2
REMARK 470 THR K 78 OG1 CG2
REMARK 470 PHE K 79 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU K 80 CG CD1 CD2
REMARK 470 GLU K 81 CG CD OE1 OE2
REMARK 470 GLN K 82 CG CD OE1 NE2
REMARK 470 LEU K 83 CG CD1 CD2
REMARK 470 LYS K 84 CG CD CE NZ
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 ALA A 309 CA GLU V 2 1.91
REMARK 500 O ALA A 309 CB GLU V 2 2.09
REMARK 500 O ILE A 307 N ALA A 309 2.09
REMARK 500 O VAL J 340 CD PRO J 342 2.13
REMARK 500 O GLY B 163 N GLY B 165 2.13
REMARK 500 O SER I 424 OG1 THR I 428 2.15
REMARK 500 O SER K 62 CD PRO K 64 2.18
REMARK 500 O UNK S 59 N UNK S 61 2.18
REMARK 500 O UNK X 470 N UNK X 473 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 84 C - N - CA ANGL. DEV. = 12.2 DEGREES
REMARK 500 PRO A 141 C - N - CA ANGL. DEV. = 10.6 DEGREES
REMARK 500 PRO A 173 C - N - CA ANGL. DEV. = 11.8 DEGREES
REMARK 500 PRO B 47 CA - N - CD ANGL. DEV. = -15.9 DEGREES
REMARK 500 PRO B 54 C - N - CA ANGL. DEV. = 11.6 DEGREES
REMARK 500 SER B 76 N - CA - C ANGL. DEV. = -28.0 DEGREES
REMARK 500 GLY B 163 C - N - CA ANGL. DEV. = 13.1 DEGREES
REMARK 500 PRO B 164 CA - N - CD ANGL. DEV. = -8.7 DEGREES
REMARK 500 PRO B 221 C - N - CA ANGL. DEV. = 11.4 DEGREES
REMARK 500 PRO B 270 CA - N - CD ANGL. DEV. = -19.1 DEGREES
REMARK 500 PRO B 360 C - N - CA ANGL. DEV. = 13.3 DEGREES
REMARK 500 GLY B 396 N - CA - C ANGL. DEV. = -27.2 DEGREES
REMARK 500 PRO C 80 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO C 110 CA - N - CD ANGL. DEV. = -15.3 DEGREES
REMARK 500 PRO C 137 CA - N - CD ANGL. DEV. = -12.3 DEGREES
REMARK 500 PRO C 137 C - N - CD ANGL. DEV. = -15.5 DEGREES
REMARK 500 PRO C 334 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 PRO C 386 C - N - CA ANGL. DEV. = 12.1 DEGREES
REMARK 500 PRO D 195 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 PRO D 335 CA - N - CD ANGL. DEV. = -13.9 DEGREES
REMARK 500 PRO D 342 CA - N - CD ANGL. DEV. = -14.6 DEGREES
REMARK 500 PRO E 64 C - N - CA ANGL. DEV. = 14.1 DEGREES
REMARK 500 PRO F 14 CA - N - CD ANGL. DEV. = -12.6 DEGREES
REMARK 500 PRO F 14 C - N - CD ANGL. DEV. = -20.1 DEGREES
REMARK 500 ARG F 45 N - CA - C ANGL. DEV. = -21.5 DEGREES
REMARK 500 PRO G 56 C - N - CA ANGL. DEV. = 10.0 DEGREES
REMARK 500 PRO G 84 C - N - CA ANGL. DEV. = 13.0 DEGREES
REMARK 500 PRO G 141 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 PRO G 173 CA - N - CD ANGL. DEV. = -14.1 DEGREES
REMARK 500 PRO G 173 C - N - CD ANGL. DEV. = -19.7 DEGREES
REMARK 500 PRO H 47 CA - N - CD ANGL. DEV. = -13.2 DEGREES
REMARK 500 PRO H 54 C - N - CA ANGL. DEV. = 11.9 DEGREES
REMARK 500 SER H 76 N - CA - C ANGL. DEV. = -27.9 DEGREES
REMARK 500 GLY H 163 C - N - CA ANGL. DEV. = 14.4 DEGREES
REMARK 500 PRO H 192 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 PRO H 221 C - N - CA ANGL. DEV. = 10.7 DEGREES
REMARK 500 PRO H 264 CA - N - CD ANGL. DEV. = -14.5 DEGREES
REMARK 500 PRO H 264 C - N - CD ANGL. DEV. = -12.7 DEGREES
REMARK 500 PRO H 270 CA - N - CD ANGL. DEV. = -21.2 DEGREES
REMARK 500 PRO H 360 C - N - CA ANGL. DEV. = 13.0 DEGREES
REMARK 500 GLY H 396 N - CA - C ANGL. DEV. = -27.0 DEGREES
REMARK 500 PRO I 80 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 PRO I 80 C - N - CD ANGL. DEV. = -12.6 DEGREES
REMARK 500 PRO I 137 CA - N - CD ANGL. DEV. = -11.6 DEGREES
REMARK 500 PRO I 256 CA - N - CD ANGL. DEV. = -8.4 DEGREES
REMARK 500 PRO I 334 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 PRO I 386 C - N - CA ANGL. DEV. = 10.9 DEGREES
REMARK 500 PRO J 171 CA - N - CD ANGL. DEV. = -16.6 DEGREES
REMARK 500 PRO J 342 CA - N - CD ANGL. DEV. = -14.9 DEGREES
REMARK 500 PRO K 64 CA - N - CD ANGL. DEV. = -11.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 54 ANGLE DEVIATIONS.
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 11 -167.58 -52.05
REMARK 500 ASN A 12 -169.70 36.75
REMARK 500 TRP A 32 -78.95 -34.03
REMARK 500 VAL A 35 -14.07 -39.43
REMARK 500 MET A 37 -72.19 -46.43
REMARK 500 ILE A 38 -72.47 -31.50
REMARK 500 ASP A 59 47.44 -80.09
REMARK 500 ILE A 63 -129.75 176.61
REMARK 500 ARG A 64 33.10 -154.02
REMARK 500 ALA A 81 -116.51 -124.29
REMARK 500 SER A 85 -175.49 -46.85
REMARK 500 HIS A 92 163.08 -47.94
REMARK 500 TYR A 94 75.91 -108.11
REMARK 500 PRO A 95 -115.58 -53.23
REMARK 500 TRP A 97 -69.26 -90.46
REMARK 500 GLU A 98 117.49 -32.77
REMARK 500 ALA A 99 138.20 98.51
REMARK 500 ASN A 108 17.52 -63.40
REMARK 500 LEU A 114 -71.94 -59.29
REMARK 500 ILE A 116 -74.14 -37.39
REMARK 500 PHE A 119 -71.36 -38.12
REMARK 500 LEU A 120 -72.09 -39.40
REMARK 500 LEU A 133 -5.66 -50.33
REMARK 500 TYR A 135 44.06 -68.55
REMARK 500 ARG A 136 13.89 -157.06
REMARK 500 LEU A 137 8.93 -161.11
REMARK 500 MET A 139 161.98 -34.59
REMARK 500 PRO A 141 -108.10 -38.84
REMARK 500 TRP A 142 -64.47 40.67
REMARK 500 ILE A 143 -37.80 -39.62
REMARK 500 LEU A 159 -56.18 -120.61
REMARK 500 SER A 167 123.94 171.50
REMARK 500 MET A 172 124.52 -1.03
REMARK 500 ILE A 176 -70.15 -49.65
REMARK 500 ASN A 181 -86.21 -68.80
REMARK 500 PHE A 182 -67.85 -11.71
REMARK 500 ASN A 191 18.95 57.50
REMARK 500 ILE A 192 -58.23 -22.59
REMARK 500 LEU A 193 -28.96 -38.54
REMARK 500 SER A 221 31.74 -71.89
REMARK 500 ASN A 247 93.45 63.03
REMARK 500 ILE A 248 -87.14 -26.34
REMARK 500 VAL A 249 -60.59 -4.37
REMARK 500 PHE A 260 -161.52 155.09
REMARK 500 ASN A 266 85.99 -162.92
REMARK 500 ASN A 267 -127.26 6.42
REMARK 500 SER A 268 -55.60 -25.99
REMARK 500 PHE A 295 8.13 -61.03
REMARK 500 ASN A 296 94.20 61.72
REMARK 500 ASP A 308 4.19 6.73
REMARK 500
REMARK 500 THIS ENTRY HAS 896 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 HIS A 332 0.09 SIDE CHAIN
REMARK 500 TYR B 273 0.07 SIDE CHAIN
REMARK 500 HIS G 332 0.09 SIDE CHAIN
REMARK 500 TYR H 273 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 SER B 76 48.8 L L OUTSIDE RANGE
REMARK 500 GLU B 353 24.4 L L OUTSIDE RANGE
REMARK 500 SER B 391 24.6 L L OUTSIDE RANGE
REMARK 500 ILE D 5 24.3 L L OUTSIDE RANGE
REMARK 500 TYR F 13 24.6 L L OUTSIDE RANGE
REMARK 500 SER H 76 48.7 L L OUTSIDE RANGE
REMARK 500 SER H 391 24.6 L L OUTSIDE RANGE
REMARK 500 ILE J 5 24.7 L L OUTSIDE RANGE
REMARK 500 TYR L 13 24.6 L L OUTSIDE RANGE
REMARK 500 UNK O 5 19.5 L L OUTSIDE RANGE
REMARK 500 UNK O 36 22.4 L L OUTSIDE RANGE
REMARK 500 UNK O 55 22.8 L L OUTSIDE RANGE
REMARK 500 UNK O 57 24.2 L L OUTSIDE RANGE
REMARK 500 UNK O 58 22.4 L L OUTSIDE RANGE
REMARK 500 UNK P 5 19.9 L L OUTSIDE RANGE
REMARK 500 UNK P 36 22.5 L L OUTSIDE RANGE
REMARK 500 UNK P 55 23.1 L L OUTSIDE RANGE
REMARK 500 UNK P 57 24.2 L L OUTSIDE RANGE
REMARK 500 UNK P 58 22.0 L L OUTSIDE RANGE
REMARK 500 UNK S 40 24.3 L L OUTSIDE RANGE
REMARK 500 UNK U 40 24.5 L L OUTSIDE RANGE
REMARK 500 UNK X 184 22.5 L L OUTSIDE RANGE
REMARK 500 UNK X 336 21.7 L L OUTSIDE RANGE
REMARK 500 UNK Y 184 22.7 L L OUTSIDE RANGE
REMARK 500 UNK Y 336 21.6 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 CLA A 1343
REMARK 610 CLA A 1344
REMARK 610 CLA A 1346
REMARK 610 CLA B 1483
REMARK 610 CLA B 1484
REMARK 610 CLA B 1485
REMARK 610 CLA B 1486
REMARK 610 CLA B 1489
REMARK 610 CLA B 1490
REMARK 610 CLA B 1491
REMARK 610 CLA B 1493
REMARK 610 CLA B 1495
REMARK 610 CLA B 1497
REMARK 610 CLA C 1459
REMARK 610 CLA C 1460
REMARK 610 CLA C 1462
REMARK 610 CLA C 1463
REMARK 610 CLA C 1464
REMARK 610 CLA C 1466
REMARK 610 CLA C 1467
REMARK 610 CLA C 1468
REMARK 610 CLA C 1469
REMARK 610 CLA C 1470
REMARK 610 CLA C 1471
REMARK 610 CLA D 1353
REMARK 610 CLA G 1343
REMARK 610 CLA G 1344
REMARK 610 CLA G 1346
REMARK 610 CLA H 1483
REMARK 610 CLA H 1484
REMARK 610 CLA H 1485
REMARK 610 CLA H 1486
REMARK 610 CLA H 1489
REMARK 610 CLA H 1490
REMARK 610 CLA H 1491
REMARK 610 CLA H 1493
REMARK 610 CLA H 1495
REMARK 610 CLA H 1497
REMARK 610 CLA I 1459
REMARK 610 CLA I 1460
REMARK 610 CLA I 1461
REMARK 610 CLA I 1462
REMARK 610 CLA I 1463
REMARK 610 CLA I 1464
REMARK 610 CLA I 1466
REMARK 610 CLA I 1467
REMARK 610 CLA I 1468
REMARK 610 CLA I 1469
REMARK 610 CLA I 1470
REMARK 610 CLA I 1471
REMARK 610 CLA J 1353
REMARK 610 PHO D 1352
REMARK 610 PHO J 1352
REMARK 610 PL9 D 1354
REMARK 610 PL9 J 1354
REMARK 610 HEM E 1085
REMARK 610 HEM L 1046
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 CLA A1342 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 198 NE2
REMARK 620 2 CLA A1342 NA 94.2
REMARK 620 3 CLA A1342 NB 103.0 89.6
REMARK 620 4 CLA A1342 NC 104.4 161.1 89.0
REMARK 620 5 CLA A1342 ND 94.9 87.8 162.0 87.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA G1342 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 198 NE2
REMARK 620 2 CLA G1342 NA 100.1
REMARK 620 3 CLA G1342 NC 106.0 153.7
REMARK 620 4 CLA G1342 ND 98.9 87.6 85.6
REMARK 620 5 CLA G1342 NB 106.8 87.7 87.5 154.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA A1343 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA A1343 NA
REMARK 620 2 CLA A1343 NB 92.1
REMARK 620 3 CLA A1343 NC 163.7 88.0
REMARK 620 4 CLA A1343 ND 89.5 164.5 86.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA G1343 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA G1343 NB
REMARK 620 2 CLA G1343 NC 88.2
REMARK 620 3 CLA G1343 ND 163.7 85.3
REMARK 620 4 CLA G1343 NA 91.9 163.4 90.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA A1344 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA A1344 NC
REMARK 620 2 CLA A1344 NB 89.5
REMARK 620 3 CLA A1344 ND 86.4 162.3
REMARK 620 4 CLA A1344 NA 160.6 88.1 90.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA G1344 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA G1344 NA
REMARK 620 2 CLA G1344 ND 90.5
REMARK 620 3 CLA G1344 NC 162.6 87.0
REMARK 620 4 CLA G1344 NB 88.4 164.0 89.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA A1346 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA A1346 NC
REMARK 620 2 CLA A1346 ND 87.4
REMARK 620 3 CLA A1346 NB 88.7 162.4
REMARK 620 4 CLA A1346 NA 162.6 90.4 88.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA G1346 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA G1346 NA
REMARK 620 2 CLA G1346 NB 89.0
REMARK 620 3 CLA G1346 NC 163.0 89.0
REMARK 620 4 CLA G1346 ND 89.9 163.0 87.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B1482 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA B1482 NA
REMARK 620 2 CLA B1482 ND 89.4
REMARK 620 3 CLA B1482 NB 91.6 164.8
REMARK 620 4 CLA B1482 NC 164.8 86.7 88.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA H1482 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA H1482 ND
REMARK 620 2 CLA H1482 NA 88.1
REMARK 620 3 CLA H1482 NB 164.1 90.8
REMARK 620 4 CLA H1482 NC 87.9 163.7 88.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B1483 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 201 ND1
REMARK 620 2 CLA B1483 NC 102.0
REMARK 620 3 CLA B1483 ND 99.3 87.2
REMARK 620 4 CLA B1483 NA 96.2 161.4 86.7
REMARK 620 5 CLA B1483 NB 99.6 88.9 161.0 91.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA H1483 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA H1483 NA
REMARK 620 2 HIS H 201 ND1 96.6
REMARK 620 3 CLA H1483 NB 90.5 100.9
REMARK 620 4 CLA H1483 NC 161.7 101.4 89.2
REMARK 620 5 CLA H1483 ND 87.7 97.9 161.2 86.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B1484 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA B1484 ND
REMARK 620 2 CLA B1484 NC 86.3
REMARK 620 3 CLA B1484 NA 89.3 161.8
REMARK 620 4 CLA B1484 NB 161.7 87.9 90.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA H1484 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA H1484 NB
REMARK 620 2 CLA H1484 NC 87.2
REMARK 620 3 CLA H1484 NA 91.5 161.7
REMARK 620 4 CLA H1484 ND 161.8 86.3 89.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B1485 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA B1485 NA
REMARK 620 2 CLA B1485 ND 90.8
REMARK 620 3 HIS B 455 NE2 92.1 83.5
REMARK 620 4 CLA B1485 NB 90.6 162.7 113.7
REMARK 620 5 CLA B1485 NC 162.6 85.2 104.2 88.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA H1485 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 455 NE2
REMARK 620 2 CLA H1485 NA 92.5
REMARK 620 3 CLA H1485 NB 113.2 90.6
REMARK 620 4 CLA H1485 NC 103.7 163.0 87.8
REMARK 620 5 CLA H1485 ND 83.8 91.0 162.8 85.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B1486 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA B1486 NA
REMARK 620 2 CLA B1486 NB 91.3
REMARK 620 3 HIS B 100 NE2 99.5 96.9
REMARK 620 4 CLA B1486 NC 162.6 89.0 97.7
REMARK 620 5 CLA B1486 ND 87.9 162.4 100.5 86.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA H1486 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA H1486 NC
REMARK 620 2 CLA H1486 ND 86.4
REMARK 620 3 HIS H 100 NE2 97.0 102.1
REMARK 620 4 CLA H1486 NA 161.8 89.1 101.2
REMARK 620 5 CLA H1486 NB 88.2 161.6 96.0 90.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B1487 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA B1487 NA
REMARK 620 2 CLA B1487 NB 86.3
REMARK 620 3 CLA B1487 NC 161.3 90.3
REMARK 620 4 CLA B1487 ND 90.2 161.2 87.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA H1487 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA H1487 NA
REMARK 620 2 CLA H1487 NB 86.4
REMARK 620 3 CLA H1487 NC 160.6 89.8
REMARK 620 4 CLA H1487 ND 90.0 160.8 87.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B1488 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA B1488 NA
REMARK 620 2 CLA B1488 NB 88.3
REMARK 620 3 CLA B1488 NC 161.1 89.4
REMARK 620 4 CLA B1488 ND 89.8 160.8 86.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA H1488 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA H1488 NA
REMARK 620 2 CLA H1488 ND 89.7
REMARK 620 3 CLA H1488 NB 88.1 159.8
REMARK 620 4 CLA H1488 NC 159.9 86.0 89.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B1489 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 466 NE2
REMARK 620 2 CLA B1489 NC 104.4
REMARK 620 3 CLA B1489 ND 78.8 87.1
REMARK 620 4 CLA B1489 NA 90.3 163.6 88.7
REMARK 620 5 CLA B1489 NB 117.9 89.0 163.3 90.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA H1489 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 466 NE2
REMARK 620 2 CLA H1489 NA 90.9
REMARK 620 3 CLA H1489 NB 118.5 89.6
REMARK 620 4 CLA H1489 NC 104.8 162.7 89.2
REMARK 620 5 CLA H1489 ND 78.1 89.1 163.3 87.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B1490 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA B1490 NC
REMARK 620 2 HIS B 216 NE2 95.3
REMARK 620 3 CLA B1490 NB 88.6 119.0
REMARK 620 4 CLA B1490 NA 159.2 103.6 90.0
REMARK 620 5 CLA B1490 ND 86.9 84.2 156.8 86.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA H1490 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA H1490 NA
REMARK 620 2 CLA H1490 NB 89.2
REMARK 620 3 CLA H1490 ND 86.7 157.7
REMARK 620 4 CLA H1490 NC 160.5 89.3 87.3
REMARK 620 5 HIS H 216 NE2 101.9 118.2 84.1 96.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B1491 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA B1491 NA
REMARK 620 2 CLA B1491 ND 90.4
REMARK 620 3 CLA B1491 NB 88.6 163.3
REMARK 620 4 CLA B1491 NC 164.2 86.8 89.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA H1491 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA H1491 NA
REMARK 620 2 CLA H1491 NB 88.4
REMARK 620 3 CLA H1491 NC 164.6 89.4
REMARK 620 4 CLA H1491 ND 91.3 164.0 86.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B1492 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 469 NE2
REMARK 620 2 CLA B1492 NB 87.4
REMARK 620 3 CLA B1492 NC 112.3 87.8
REMARK 620 4 CLA B1492 NA 85.3 90.6 162.1
REMARK 620 5 CLA B1492 ND 111.2 161.2 87.4 88.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA H1492 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA H1492 ND
REMARK 620 2 HIS H 469 NE2 112.5
REMARK 620 3 CLA H1492 NA 88.7 86.7
REMARK 620 4 CLA H1492 NB 161.1 86.2 90.1
REMARK 620 5 CLA H1492 NC 87.0 111.5 161.6 88.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B1493 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA B1493 NA
REMARK 620 2 CLA B1493 ND 89.1
REMARK 620 3 CLA B1493 NB 89.8 165.3
REMARK 620 4 CLA B1493 NC 165.3 88.0 89.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA H1493 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA H1493 ND
REMARK 620 2 CLA H1493 NA 89.8
REMARK 620 3 CLA H1493 NB 164.7 89.2
REMARK 620 4 CLA H1493 NC 87.7 165.0 89.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B1494 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA B1494 NB
REMARK 620 2 CLA B1494 NC 89.0
REMARK 620 3 CLA B1494 NA 92.8 164.1
REMARK 620 4 CLA B1494 ND 164.2 86.5 87.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA H1494 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA H1494 NA
REMARK 620 2 CLA H1494 NB 92.5
REMARK 620 3 CLA H1494 ND 88.4 164.4
REMARK 620 4 CLA H1494 NC 164.7 88.8 86.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B1495 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA B1495 NA
REMARK 620 2 CLA B1495 ND 88.7
REMARK 620 3 CLA B1495 NB 91.0 163.1
REMARK 620 4 CLA B1495 NC 163.5 86.8 88.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA H1495 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA H1495 ND
REMARK 620 2 CLA H1495 NC 86.5
REMARK 620 3 CLA H1495 NA 88.0 161.8
REMARK 620 4 CLA H1495 NB 162.2 88.5 91.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B1496 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA B1496 NB
REMARK 620 2 CLA B1496 NC 87.6
REMARK 620 3 CLA B1496 NA 93.2 168.7
REMARK 620 4 CLA B1496 ND 165.7 86.9 89.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA H1496 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA H1496 NA
REMARK 620 2 CLA H1496 NB 91.7
REMARK 620 3 CLA H1496 NC 167.6 88.4
REMARK 620 4 CLA H1496 ND 90.0 165.0 86.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B1497 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA B1497 NA
REMARK 620 2 HIS B 114 NE2 93.5
REMARK 620 3 CLA B1497 NB 91.5 72.0
REMARK 620 4 CLA B1497 NC 163.3 102.2 87.9
REMARK 620 5 CLA B1497 ND 89.1 126.1 161.7 86.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA H1497 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 114 NE2
REMARK 620 2 CLA H1497 NC 100.4
REMARK 620 3 CLA H1497 NB 71.9 88.4
REMARK 620 4 CLA H1497 ND 124.4 86.2 163.5
REMARK 620 5 CLA H1497 NA 94.2 164.7 92.1 89.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C1459 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA C1459 NA
REMARK 620 2 CLA C1459 ND 89.0
REMARK 620 3 HIS C 237 NE2 90.8 99.9
REMARK 620 4 CLA C1459 NB 91.8 162.6 97.5
REMARK 620 5 CLA C1459 NC 162.7 86.4 106.4 87.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA I1459 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA I1459 NC
REMARK 620 2 HIS I 237 NE2 108.5
REMARK 620 3 CLA I1459 NA 162.5 88.9
REMARK 620 4 CLA I1459 ND 87.3 99.2 88.4
REMARK 620 5 CLA I1459 NB 88.7 98.0 90.4 162.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C1460 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 430 NE2
REMARK 620 2 CLA C1460 NB 128.3
REMARK 620 3 CLA C1460 NC 94.4 89.1
REMARK 620 4 CLA C1460 ND 69.7 161.8 86.8
REMARK 620 5 CLA C1460 NA 100.6 89.5 161.9 88.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA I1460 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS I 430 NE2
REMARK 620 2 CLA I1460 NA 100.7
REMARK 620 3 CLA I1460 NB 127.6 88.9
REMARK 620 4 CLA I1460 ND 69.7 90.0 162.5
REMARK 620 5 CLA I1460 NC 93.7 162.9 89.6 86.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C1461 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA C1461 ND
REMARK 620 2 HIS C 118 NE2 99.2
REMARK 620 3 CLA C1461 NC 88.2 107.5
REMARK 620 4 CLA C1461 NA 87.4 90.5 162.0
REMARK 620 5 CLA C1461 NB 161.0 99.5 89.1 89.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA I1461 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS I 118 NE2
REMARK 620 2 CLA I1461 NB 98.4
REMARK 620 3 CLA I1461 NC 107.8 88.6
REMARK 620 4 CLA I1461 NA 90.8 90.6 161.3
REMARK 620 5 CLA I1461 ND 100.8 160.6 87.9 86.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C1462 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA C1462 NA
REMARK 620 2 CLA C1462 NB 88.3
REMARK 620 3 CLA C1462 NC 161.9 88.9
REMARK 620 4 CLA C1462 ND 91.1 162.2 86.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA I1462 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA I1462 NB
REMARK 620 2 CLA I1462 NC 89.3
REMARK 620 3 CLA I1462 ND 162.1 86.3
REMARK 620 4 CLA I1462 NA 88.5 162.5 90.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C1463 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA C1463 NA
REMARK 620 2 CLA C1463 NB 90.2
REMARK 620 3 CLA C1463 ND 87.0 159.4
REMARK 620 4 CLA C1463 NC 160.6 88.6 87.4
REMARK 620 5 HIS C 441 NE2 109.1 93.6 106.6 90.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA I1463 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA I1463 ND
REMARK 620 2 HIS I 441 NE2 106.7
REMARK 620 3 CLA I1463 NA 87.2 109.9
REMARK 620 4 CLA I1463 NB 159.1 93.8 89.7
REMARK 620 5 CLA I1463 NC 87.3 90.1 160.0 88.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C1464 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA C1464 NA
REMARK 620 2 HIS C 251 NE2 75.1
REMARK 620 3 CLA C1464 NB 89.9 82.8
REMARK 620 4 CLA C1464 NC 162.7 121.7 88.8
REMARK 620 5 CLA C1464 ND 88.9 114.2 162.0 87.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA I1464 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA I1464 NC
REMARK 620 2 CLA I1464 ND 86.7
REMARK 620 3 HIS I 251 NE2 121.1 113.8
REMARK 620 4 CLA I1464 NA 163.3 89.4 75.2
REMARK 620 5 CLA I1464 NB 88.4 162.0 83.4 90.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C1465 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA C1465 NB
REMARK 620 2 CLA C1465 NC 89.0
REMARK 620 3 CLA C1465 ND 163.3 87.1
REMARK 620 4 CLA C1465 NA 90.1 164.7 89.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA I1465 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA I1465 NA
REMARK 620 2 CLA I1465 NB 90.8
REMARK 620 3 CLA I1465 NC 164.9 88.5
REMARK 620 4 CLA I1465 ND 90.1 163.4 86.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C1466 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA C1466 ND
REMARK 620 2 CLA C1466 NC 86.8
REMARK 620 3 HIS C 444 NE2 117.7 122.0
REMARK 620 4 CLA C1466 NA 87.8 160.0 77.4
REMARK 620 5 CLA C1466 NB 160.1 88.8 80.8 89.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA I1466 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA I1466 NB
REMARK 620 2 HIS I 444 NE2 79.7
REMARK 620 3 CLA I1466 NA 88.6 78.2
REMARK 620 4 CLA I1466 NC 88.7 121.7 159.0
REMARK 620 5 CLA I1466 ND 160.1 119.0 88.8 86.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C1467 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA C1467 NB
REMARK 620 2 CLA C1467 NC 89.2
REMARK 620 3 CLA C1467 ND 163.1 87.4
REMARK 620 4 HIS C 53 NE2 68.6 86.0 94.6
REMARK 620 5 CLA C1467 NA 90.6 164.7 88.4 79.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA I1467 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA I1467 NA
REMARK 620 2 CLA I1467 ND 89.1
REMARK 620 3 HIS I 53 NE2 80.5 94.8
REMARK 620 4 CLA I1467 NB 91.1 163.1 68.6
REMARK 620 5 CLA I1467 NC 164.8 86.3 85.5 89.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C1468 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA C1468 NA
REMARK 620 2 CLA C1468 ND 87.6
REMARK 620 3 CLA C1468 NB 91.6 162.2
REMARK 620 4 HIS C 56 NE2 103.3 93.7 103.7
REMARK 620 5 CLA C1468 NC 163.0 87.4 88.2 93.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA I1468 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS I 56 NE2
REMARK 620 2 CLA I1468 NB 103.3
REMARK 620 3 CLA I1468 NC 93.0 88.6
REMARK 620 4 CLA I1468 ND 94.9 161.5 86.7
REMARK 620 5 CLA I1468 NA 105.3 91.2 161.3 87.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C1469 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA C1469 NB
REMARK 620 2 CLA C1469 NC 88.3
REMARK 620 3 CLA C1469 ND 163.3 86.0
REMARK 620 4 ASN C 39 OD1 97.1 86.7 98.2
REMARK 620 5 CLA C1469 NA 90.6 163.7 90.6 109.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA I1469 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN I 39 OD1
REMARK 620 2 CLA I1469 NA 109.7
REMARK 620 3 CLA I1469 NB 98.6 89.2
REMARK 620 4 CLA I1469 NC 87.9 162.4 88.5
REMARK 620 5 CLA I1469 ND 98.2 90.4 162.3 86.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C1470 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA C1470 NA
REMARK 620 2 CLA C1470 NC 164.8
REMARK 620 3 CLA C1470 ND 89.3 86.9
REMARK 620 4 CLA C1470 NB 91.0 88.6 163.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA I1470 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA I1470 NC
REMARK 620 2 CLA I1470 NA 165.4
REMARK 620 3 CLA I1470 NB 88.5 91.4
REMARK 620 4 CLA I1470 ND 86.7 89.3 163.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C1471 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA C1471 NA
REMARK 620 2 CLA C1471 NB 90.1
REMARK 620 3 CLA C1471 NC 160.8 88.5
REMARK 620 4 CLA C1471 ND 88.8 160.3 86.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA I1471 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA I1471 NA
REMARK 620 2 CLA I1471 ND 88.9
REMARK 620 3 CLA I1471 NB 90.1 161.1
REMARK 620 4 CLA I1471 NC 161.3 86.9 88.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA D1351 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 197 NE2
REMARK 620 2 CLA D1351 NA 110.3
REMARK 620 3 CLA D1351 NB 104.8 88.7
REMARK 620 4 CLA D1351 ND 103.4 87.3 151.1
REMARK 620 5 CLA D1351 NC 96.7 153.0 85.4 85.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA J1351 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA J1351 NC
REMARK 620 2 HIS J 197 NE2 100.7
REMARK 620 3 CLA J1351 NB 90.6 110.2
REMARK 620 4 CLA J1351 ND 86.0 101.1 148.6
REMARK 620 5 CLA J1351 NA 149.9 108.0 87.7 80.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA D1353 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA D1353 NB
REMARK 620 2 HIS D 117 NE2 97.4
REMARK 620 3 CLA D1353 NA 91.4 69.8
REMARK 620 4 CLA D1353 NC 88.7 126.9 163.2
REMARK 620 5 CLA D1353 ND 164.3 97.4 88.7 86.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA J1353 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CLA J1353 NC
REMARK 620 2 CLA J1353 ND 86.5
REMARK 620 3 HIS J 117 NE2 124.6 97.1
REMARK 620 4 CLA J1353 NA 163.6 89.7 71.8
REMARK 620 5 CLA J1353 NB 88.5 164.3 98.0 90.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1347 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 170 OD1
REMARK 620 2 GLU A 333 OE1 145.0
REMARK 620 3 GLU A 333 OE2 103.4 64.1
REMARK 620 4 MN A1349 MN 120.5 93.1 118.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN G1347 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 170 OD2
REMARK 620 2 GLU G 333 OE1 152.7
REMARK 620 3 ASP G 170 OD1 52.6 152.0
REMARK 620 4 GLU G 333 OE2 135.6 68.6 95.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 A1350 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 215 NE2
REMARK 620 2 HIS A 272 NE2 92.2
REMARK 620 3 HIS D 214 NE2 109.7 87.5
REMARK 620 4 HIS D 268 NE2 81.4 172.9 91.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 G1350 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 215 NE2
REMARK 620 2 HIS G 272 NE2 91.1
REMARK 620 3 HIS J 214 NE2 110.1 82.8
REMARK 620 4 HIS J 268 NE2 83.1 172.9 95.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM E1085 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 24 NE2
REMARK 620 2 HEM E1085 ND 88.8
REMARK 620 3 HEM E1085 NC 98.1 90.6
REMARK 620 4 HEM E1085 NA 82.0 91.1 178.4
REMARK 620 5 HEM E1085 NB 92.6 178.2 88.0 90.4
REMARK 620 6 HIS E 23 NE2 150.4 75.9 107.1 73.3 103.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM L1046 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS K 23 NE2
REMARK 620 2 HEM L1046 ND 74.9
REMARK 620 3 HIS L 24 NE2 148.9 87.0
REMARK 620 4 HEM L1046 NA 72.1 90.3 83.1
REMARK 620 5 HEM L1046 NB 101.8 176.2 96.7 90.6
REMARK 620 6 HEM L1046 NC 105.3 89.5 99.6 177.3 89.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC T1138 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS T 92 NE2
REMARK 620 2 HEC T1138 NA 81.0
REMARK 620 3 HEC T1138 NB 90.7 91.5
REMARK 620 4 HEC T1138 NC 97.1 178.1 88.6
REMARK 620 5 HEC T1138 ND 87.3 90.5 177.0 89.4
REMARK 620 6 HIS T 41 NE2 172.3 91.6 87.4 90.3 94.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC V1138 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HEC V1138 ND
REMARK 620 2 HIS V 41 NE2 97.0
REMARK 620 3 HIS V 92 NE2 88.3 171.4
REMARK 620 4 HEC V1138 NA 92.3 91.6 81.3
REMARK 620 5 HEC V1138 NB 176.0 85.6 89.4 90.5
REMARK 620 6 HEC V1138 NC 89.5 90.3 96.6 177.2 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 CLA A1342
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A1343
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A1344
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO A1345
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A1346
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A1347
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A1348
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A1349
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A1350
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A1354
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B1484
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B1485
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B1486
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B1487
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B1488
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B1489
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B1490
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B1491
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B1492
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B1493
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B1494
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B1495
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B1496
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B1497
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C1459
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C1462
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C1463
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C1464
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C1465
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C1466
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C1467
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C1468
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C1469
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C1470
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C1471
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D1351
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO D1352
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D1353
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 D1354
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM E1085
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR F1046
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA G1342
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA G1343
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA G1344
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO G1345
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA G1346
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G1347
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G1348
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G1349
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 G1350
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G5054
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H1483
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H1484
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H1485
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H1486
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H1487
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H1488
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H1489
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H1490
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H1491
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H1492
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H1493
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H1494
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H1495
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H1496
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H1497
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA I1459
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA I1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA I1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA I1462
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA I1463
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA I1464
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA I1465
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA I1466
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA I1467
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA I1468
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA I1469
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA I1470
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA I1471
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA J1351
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO J1352
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA J1353
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 J1354
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM L1046
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR L1047
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC T1138
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC V1138
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IZL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PHOTOSYSTEM II
REMARK 900 RELATED ID: 1MZ4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CYTOCHROME C550 FROM
REMARK 900 THERMOSYNECHOCOCCUS ELONGATUS
REMARK 900 RELATED ID: 1S5L RELATED DB: PDB
REMARK 900 ARCHITECTURE OF THE PHOTOSYNTHETIC OXYGEN EVOLVING CENTER
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CHAINS O AND P CORRESPOND TO UNIPROT ENTRY PSBO_SYNEL (P55221),
REMARK 999 CHAINS U AND S CORRESPOND TO UNIPROT ENTRY PSBU_SNYEL (Q9F1L5).
REMARK 999 THE ELECTRON DENSITY FOR THESE REGIONS DO NOT ALLOW FOR
REMARK 999 UNAMBIGUOUS ASSIGNMENT OF SEQUENCE AND THEY ARE THEREFORE
REMARK 999 REPRESENTED BY RESIDUE TYPE UNK (UNKNOWN), WHICH IS REFLECTED
REMARK 999 IN THE CORRESPONDING SEQRES AND DBREF RECORDS.
REMARK 999 THE SEQUENCE IN FRAGMENTS MODELED AS POLY-ALA AND CA WAS
REMARK 999 ASSIGNED TENTATIVELY AND SHOULD BE TREATED WITH CAUTION.
DBREF 1W5C A 1 360 UNP P0A444 PSBA1_THEEB 1 360
DBREF 1W5C G 1 360 UNP P0A444 PSBA1_THEEB 1 360
DBREF 1W5C B 1 510 UNP Q8DIQ1 Q8DIQ1 1 510
DBREF 1W5C H 0 510 UNP Q8DIQ1 Q8DIQ1 1 510
DBREF 1W5C C 1 473 UNP Q8DIF8 Q8DIF8 1 473
DBREF 1W5C I 1 473 UNP Q8DIF8 Q8DIF8 1 473
DBREF 1W5C D 1 352 UNP Q8CM25 Q8CM25 1 352
DBREF 1W5C J 1 352 UNP Q8CM25 Q8CM25 1 352
DBREF 1W5C E 1 1 PDB 1W5C 1W5C 1 1
DBREF 1W5C E 2 84 UNP P12238 PSBE_SYNVU 1 83
DBREF 1W5C K 1 1 PDB 1W5C 1W5C 1 1
DBREF 1W5C K 2 84 UNP P12238 PSBE_SYNVU 1 83
DBREF 1W5C F 2 45 UNP P12239 PSBF_SYNVU 2 45
DBREF 1W5C L 2 45 UNP P12239 PSBF_SYNVU 2 45
DBREF 1W5C O 1 179 PDB 1W5C 1W5C 1 179
DBREF 1W5C P 1 179 PDB 1W5C 1W5C 1 179
DBREF 1W5C U 1 100 PDB 1W5C 1W5C 1 100
DBREF 1W5C S 1 100 PDB 1W5C 1W5C 1 100
DBREF 1W5C V -25 137 UNP P56150 C550_SYNEL 1 163
DBREF 1W5C T -25 137 UNP P56150 C550_SYNEL 1 163
DBREF 1W5C X 2 584 PDB 1W5C 1W5C 2 584
DBREF 1W5C Y 2 584 PDB 1W5C 1W5C 2 584
SEQRES 1 A 360 MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU
SEQRES 2 A 360 TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN
SEQRES 3 A 360 ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO
SEQRES 4 A 360 THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE
SEQRES 5 A 360 ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU
SEQRES 6 A 360 PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE
SEQRES 7 A 360 THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU
SEQRES 8 A 360 HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU
SEQRES 9 A 360 TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE
SEQRES 10 A 360 HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN
SEQRES 11 A 360 TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE
SEQRES 12 A 360 CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA
SEQRES 13 A 360 VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER
SEQRES 14 A 360 ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE
SEQRES 15 A 360 MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS
SEQRES 16 A 360 PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY
SEQRES 17 A 360 ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER
SEQRES 18 A 360 SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN
SEQRES 19 A 360 TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN
SEQRES 20 A 360 ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE
SEQRES 21 A 360 GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE
SEQRES 22 A 360 PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR
SEQRES 23 A 360 ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY
SEQRES 24 A 360 PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN
SEQRES 25 A 360 VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN
SEQRES 26 A 360 LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN
SEQRES 27 A 360 PHE PRO LEU ASP LEU ALA SER ALA GLU SER ALA PRO VAL
SEQRES 28 A 360 ALA MET ILE ALA PRO SER ILE ASN GLY
SEQRES 1 B 510 MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE
SEQRES 2 B 510 ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS
SEQRES 3 B 510 THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU
SEQRES 4 B 510 TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU
SEQRES 5 B 510 ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE
SEQRES 6 B 510 MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP
SEQRES 7 B 510 SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP
SEQRES 8 B 510 SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER
SEQRES 9 B 510 GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR
SEQRES 10 B 510 TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU
SEQRES 11 B 510 PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU
SEQRES 12 B 510 PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE
SEQRES 13 B 510 HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER
SEQRES 14 B 510 ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA
SEQRES 15 B 510 PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO
SEQRES 16 B 510 GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL
SEQRES 17 B 510 GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO
SEQRES 18 B 510 PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE
SEQRES 19 B 510 GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE
SEQRES 20 B 510 ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER
SEQRES 21 B 510 ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR
SEQRES 22 B 510 GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG
SEQRES 23 B 510 ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU
SEQRES 24 B 510 GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR
SEQRES 25 B 510 ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE
SEQRES 26 B 510 ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN
SEQRES 27 B 510 ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY
SEQRES 28 B 510 GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU
SEQRES 29 B 510 SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL
SEQRES 30 B 510 LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR
SEQRES 31 B 510 SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY
SEQRES 32 B 510 GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR
SEQRES 33 B 510 VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE
SEQRES 34 B 510 PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE
SEQRES 35 B 510 PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS
SEQRES 36 B 510 ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP
SEQRES 37 B 510 HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY
SEQRES 38 B 510 ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY
SEQRES 39 B 510 PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS
SEQRES 40 B 510 GLU ALA VAL
SEQRES 1 C 473 MET LYS THR LEU SER SER GLN LYS ARG TYR SER PRO VAL
SEQRES 2 C 473 VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN ARG
SEQRES 3 C 473 ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY ASN
SEQRES 4 C 473 ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY ALA
SEQRES 5 C 473 HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA GLY
SEQRES 6 C 473 ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO GLU
SEQRES 7 C 473 LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO HIS
SEQRES 8 C 473 ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY GLU
SEQRES 9 C 473 VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL VAL
SEQRES 10 C 473 HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY VAL
SEQRES 11 C 473 TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU TYR
SEQRES 12 C 473 SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN LYS
SEQRES 13 C 473 MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU GLY
SEQRES 14 C 473 ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE PHE
SEQRES 15 C 473 GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY ASP
SEQRES 16 C 473 VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG VAL
SEQRES 17 C 473 ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY GLU
SEQRES 18 C 473 GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL VAL
SEQRES 19 C 473 GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA GLY
SEQRES 20 C 473 GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP ALA
SEQRES 21 C 473 ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU SER
SEQRES 22 C 473 TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE ALA
SEQRES 23 C 473 THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO SER
SEQRES 24 C 473 GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN ALA
SEQRES 25 C 473 GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU GLY
SEQRES 26 C 473 ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU GLY
SEQRES 27 C 473 LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE PHE
SEQRES 28 C 473 GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY PRO
SEQRES 29 C 473 TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP LEU
SEQRES 30 C 473 ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU ARG
SEQRES 31 C 473 ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY SER
SEQRES 32 C 473 LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN SER
SEQRES 33 C 473 VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR SER
SEQRES 34 C 473 HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS LEU
SEQRES 35 C 473 TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY PHE
SEQRES 36 C 473 GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU SER
SEQRES 37 C 473 MET PRO SER LEU ASP
SEQRES 1 D 352 MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY
SEQRES 2 D 352 TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG
SEQRES 3 D 352 PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO
SEQRES 4 D 352 CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR
SEQRES 5 D 352 THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER
SEQRES 6 D 352 SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL
SEQRES 7 D 352 SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU
SEQRES 8 D 352 LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP
SEQRES 9 D 352 CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS
SEQRES 10 D 352 GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE
SEQRES 11 D 352 GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA
SEQRES 12 D 352 ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL
SEQRES 13 D 352 PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE
SEQRES 14 D 352 ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU
SEQRES 15 D 352 LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO
SEQRES 16 D 352 PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA
SEQRES 17 D 352 LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR
SEQRES 18 D 352 LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA
SEQRES 19 D 352 PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL
SEQRES 20 D 352 THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA
SEQRES 21 D 352 PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE
SEQRES 22 D 352 VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL
SEQRES 23 D 352 VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE
SEQRES 24 D 352 SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU
SEQRES 25 D 352 THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE
SEQRES 26 D 352 ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN
SEQRES 27 D 352 PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA
SEQRES 28 D 352 LEU
SEQRES 1 E 84 MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE
SEQRES 2 E 84 ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR
SEQRES 3 E 84 ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER
SEQRES 4 E 84 THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO
SEQRES 5 E 84 ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU
SEQRES 6 E 84 VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR
SEQRES 7 E 84 PHE LEU GLU GLN LEU LYS
SEQRES 1 F 44 THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR PRO
SEQRES 2 F 44 ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU ALA
SEQRES 3 F 44 VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA MET
SEQRES 4 F 44 GLN PHE ILE GLN ARG
SEQRES 1 G 360 MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU
SEQRES 2 G 360 TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN
SEQRES 3 G 360 ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO
SEQRES 4 G 360 THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE
SEQRES 5 G 360 ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU
SEQRES 6 G 360 PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE
SEQRES 7 G 360 THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU
SEQRES 8 G 360 HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU
SEQRES 9 G 360 TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE
SEQRES 10 G 360 HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN
SEQRES 11 G 360 TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE
SEQRES 12 G 360 CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA
SEQRES 13 G 360 VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER
SEQRES 14 G 360 ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE
SEQRES 15 G 360 MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS
SEQRES 16 G 360 PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY
SEQRES 17 G 360 ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER
SEQRES 18 G 360 SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN
SEQRES 19 G 360 TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN
SEQRES 20 G 360 ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE
SEQRES 21 G 360 GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE
SEQRES 22 G 360 PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR
SEQRES 23 G 360 ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY
SEQRES 24 G 360 PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN
SEQRES 25 G 360 VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN
SEQRES 26 G 360 LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN
SEQRES 27 G 360 PHE PRO LEU ASP LEU ALA SER ALA GLU SER ALA PRO VAL
SEQRES 28 G 360 ALA MET ILE ALA PRO SER ILE ASN GLY
SEQRES 1 H 510 MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE
SEQRES 2 H 510 ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS
SEQRES 3 H 510 THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU
SEQRES 4 H 510 TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU
SEQRES 5 H 510 ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE
SEQRES 6 H 510 MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP
SEQRES 7 H 510 SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP
SEQRES 8 H 510 SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER
SEQRES 9 H 510 GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR
SEQRES 10 H 510 TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU
SEQRES 11 H 510 PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU
SEQRES 12 H 510 PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE
SEQRES 13 H 510 HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER
SEQRES 14 H 510 ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA
SEQRES 15 H 510 PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO
SEQRES 16 H 510 GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL
SEQRES 17 H 510 GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO
SEQRES 18 H 510 PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE
SEQRES 19 H 510 GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE
SEQRES 20 H 510 ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER
SEQRES 21 H 510 ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR
SEQRES 22 H 510 GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG
SEQRES 23 H 510 ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU
SEQRES 24 H 510 GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR
SEQRES 25 H 510 ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE
SEQRES 26 H 510 ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN
SEQRES 27 H 510 ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY
SEQRES 28 H 510 GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU
SEQRES 29 H 510 SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL
SEQRES 30 H 510 LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR
SEQRES 31 H 510 SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY
SEQRES 32 H 510 GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR
SEQRES 33 H 510 VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE
SEQRES 34 H 510 PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE
SEQRES 35 H 510 PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS
SEQRES 36 H 510 ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP
SEQRES 37 H 510 HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY
SEQRES 38 H 510 ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY
SEQRES 39 H 510 PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS
SEQRES 40 H 510 GLU ALA VAL
SEQRES 1 I 473 MET LYS THR LEU SER SER GLN LYS ARG TYR SER PRO VAL
SEQRES 2 I 473 VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN ARG
SEQRES 3 I 473 ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY ASN
SEQRES 4 I 473 ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY ALA
SEQRES 5 I 473 HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA GLY
SEQRES 6 I 473 ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO GLU
SEQRES 7 I 473 LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO HIS
SEQRES 8 I 473 ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY GLU
SEQRES 9 I 473 VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL VAL
SEQRES 10 I 473 HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY VAL
SEQRES 11 I 473 TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU TYR
SEQRES 12 I 473 SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN LYS
SEQRES 13 I 473 MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU GLY
SEQRES 14 I 473 ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE PHE
SEQRES 15 I 473 GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY ASP
SEQRES 16 I 473 VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG VAL
SEQRES 17 I 473 ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY GLU
SEQRES 18 I 473 GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL VAL
SEQRES 19 I 473 GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA GLY
SEQRES 20 I 473 GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP ALA
SEQRES 21 I 473 ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU SER
SEQRES 22 I 473 TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE ALA
SEQRES 23 I 473 THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO SER
SEQRES 24 I 473 GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN ALA
SEQRES 25 I 473 GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU GLY
SEQRES 26 I 473 ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU GLY
SEQRES 27 I 473 LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE PHE
SEQRES 28 I 473 GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY PRO
SEQRES 29 I 473 TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP LEU
SEQRES 30 I 473 ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU ARG
SEQRES 31 I 473 ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY SER
SEQRES 32 I 473 LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN SER
SEQRES 33 I 473 VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR SER
SEQRES 34 I 473 HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS LEU
SEQRES 35 I 473 TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY PHE
SEQRES 36 I 473 GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU SER
SEQRES 37 I 473 MET PRO SER LEU ASP
SEQRES 1 J 352 MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY
SEQRES 2 J 352 TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG
SEQRES 3 J 352 PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO
SEQRES 4 J 352 CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR
SEQRES 5 J 352 THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER
SEQRES 6 J 352 SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL
SEQRES 7 J 352 SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU
SEQRES 8 J 352 LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP
SEQRES 9 J 352 CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS
SEQRES 10 J 352 GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE
SEQRES 11 J 352 GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA
SEQRES 12 J 352 ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL
SEQRES 13 J 352 PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE
SEQRES 14 J 352 ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU
SEQRES 15 J 352 LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO
SEQRES 16 J 352 PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA
SEQRES 17 J 352 LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR
SEQRES 18 J 352 LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA
SEQRES 19 J 352 PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL
SEQRES 20 J 352 THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA
SEQRES 21 J 352 PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE
SEQRES 22 J 352 VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL
SEQRES 23 J 352 VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE
SEQRES 24 J 352 SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU
SEQRES 25 J 352 THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE
SEQRES 26 J 352 ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN
SEQRES 27 J 352 PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA
SEQRES 28 J 352 LEU
SEQRES 1 K 84 MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE
SEQRES 2 K 84 ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR
SEQRES 3 K 84 ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER
SEQRES 4 K 84 THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO
SEQRES 5 K 84 ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU
SEQRES 6 K 84 VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR
SEQRES 7 K 84 PHE LEU GLU GLN LEU LYS
SEQRES 1 L 44 THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR PRO
SEQRES 2 L 44 ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU ALA
SEQRES 3 L 44 VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA MET
SEQRES 4 L 44 GLN PHE ILE GLN ARG
SEQRES 1 O 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 O 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 O 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 4 O 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 5 O 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 6 O 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 O 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 O 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 9 O 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 10 O 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 11 O 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 12 O 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 13 O 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 14 O 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 1 P 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 P 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 P 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 4 P 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 5 P 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 6 P 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 P 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 P 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 9 P 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 10 P 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 11 P 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 12 P 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 13 P 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 14 P 179 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 1 S 100 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 S 100 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 S 100 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 4 S 100 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 5 S 100 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 6 S 100 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 S 100 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 S 100 UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 1 T 163 MET LEU LYS LYS CYS VAL TRP LEU ALA VAL ALA LEU CYS
SEQRES 2 T 163 LEU CYS LEU TRP GLN PHE THR MET GLY THR ALA LEU ALA
SEQRES 3 T 163 ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN
SEQRES 4 T 163 SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR
SEQRES 5 T 163 LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER
SEQRES 6 T 163 CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU
SEQRES 7 T 163 ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO
SEQRES 8 T 163 ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN
SEQRES 9 T 163 PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL
SEQRES 10 T 163 HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET
SEQRES 11 T 163 ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY
SEQRES 12 T 163 HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP
SEQRES 13 T 163 GLY GLY GLY LYS VAL TYR TYR
SEQRES 1 U 100 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 U 100 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 U 100 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 4 U 100 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 5 U 100 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 6 U 100 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 U 100 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 U 100 UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 1 V 163 MET LEU LYS LYS CYS VAL TRP LEU ALA VAL ALA LEU CYS
SEQRES 2 V 163 LEU CYS LEU TRP GLN PHE THR MET GLY THR ALA LEU ALA
SEQRES 3 V 163 ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN
SEQRES 4 V 163 SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR
SEQRES 5 V 163 LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER
SEQRES 6 V 163 CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU
SEQRES 7 V 163 ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO
SEQRES 8 V 163 ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN
SEQRES 9 V 163 PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL
SEQRES 10 V 163 HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET
SEQRES 11 V 163 ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY
SEQRES 12 V 163 HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP
SEQRES 13 V 163 GLY GLY GLY LYS VAL TYR TYR
SEQRES 1 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 4 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 5 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 6 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 9 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 10 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 11 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 12 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 13 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 14 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 15 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 16 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 17 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 18 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 19 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 20 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 21 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 22 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 23 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 24 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 25 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 26 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 27 X 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 28 X 359 UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 1 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 4 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 5 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 6 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 7 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 8 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 9 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 10 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 11 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 12 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 13 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 14 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 15 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 16 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 17 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 18 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 19 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 20 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 21 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 22 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 23 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 24 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 25 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 26 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 27 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 28 Y 359 UNK UNK UNK UNK UNK UNK UNK UNK
HET CLA A1342 65
HET CLA A1343 61
HET CLA A1344 45
HET PHO A1345 64
HET CLA A1346 51
HET MN A1347 1
HET MN A1348 1
HET MN A1349 1
HET FE2 A1350 1
HET MN A1354 1
HET CLA B1482 65
HET CLA B1483 60
HET CLA B1484 45
HET CLA B1485 47
HET CLA B1486 41
HET CLA B1487 65
HET CLA B1488 65
HET CLA B1489 50
HET CLA B1490 45
HET CLA B1491 27
HET CLA B1492 65
HET CLA B1493 45
HET CLA B1494 65
HET CLA B1495 55
HET CLA B1496 65
HET CLA B1497 41
HET CLA C1459 45
HET CLA C1460 47
HET CLA C1461 27
HET CLA C1462 56
HET CLA C1463 55
HET CLA C1464 56
HET CLA C1465 65
HET CLA C1466 50
HET CLA C1467 47
HET CLA C1468 27
HET CLA C1469 41
HET CLA C1470 41
HET CLA C1471 41
HET CLA D1351 65
HET PHO D1352 54
HET CLA D1353 50
HET PL9 D1354 6
HET HEM E1085 25
HET BCR F1046 40
HET CLA G1342 65
HET CLA G1343 61
HET CLA G1344 45
HET PHO G1345 64
HET CLA G1346 51
HET MN G1347 1
HET MN G1348 1
HET MN G1349 1
HET FE2 G1350 1
HET MN G5054 1
HET CLA H1482 65
HET CLA H1483 60
HET CLA H1484 45
HET CLA H1485 47
HET CLA H1486 41
HET CLA H1487 65
HET CLA H1488 65
HET CLA H1489 50
HET CLA H1490 45
HET CLA H1491 27
HET CLA H1492 65
HET CLA H1493 45
HET CLA H1494 65
HET CLA H1495 55
HET CLA H1496 65
HET CLA H1497 41
HET CLA I1459 45
HET CLA I1460 47
HET CLA I1461 27
HET CLA I1462 56
HET CLA I1463 55
HET CLA I1464 56
HET CLA I1465 65
HET CLA I1466 50
HET CLA I1467 47
HET CLA I1468 27
HET CLA I1469 41
HET CLA I1470 41
HET CLA I1471 41
HET CLA J1351 65
HET PHO J1352 54
HET CLA J1353 50
HET PL9 J1354 6
HET HEM L1046 25
HET BCR L1047 40
HET HEC T1138 43
HET HEC V1138 43
HETNAM CLA CHLOROPHYLL A
HETNAM PHO PHEOPHYTIN A
HETNAM MN MANGANESE (II) ION
HETNAM FE2 FE (II) ION
HETNAM PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-
HETNAM 2 PL9 NONAMETHYL-2,6,10,14,18,22,26,30,34-
HETNAM 3 PL9 HEXATRIACONTANONAENYL-2,5-CYCLOHEXADIENE-1,4-DIONE-2,3-
HETNAM 4 PL9 DIMETHYL-5-SOLANESYL-1,4-BENZOQUINONE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM BCR BETA-CAROTENE
HETNAM HEC HEME C
HETSYN PL9 PLASTOQUINONE 9
HETSYN HEM HEME
FORMUL 21 CLA 70(C22 H15 N4 O1 MG1)
FORMUL 22 PHO 4(C55 H74 N4 O5)
FORMUL 23 MN 8(MN 2+)
FORMUL 24 FE2 2(FE 2+)
FORMUL 25 PL9 2(C53 H80 O2)
FORMUL 26 HEM 2(C34 H32 FE N4 O4)
FORMUL 27 BCR 2(C40 H56)
FORMUL 28 HEC 2(C34 H34 FE N4 O4)
HELIX 1 1 ALA A 11 THR A 24 1 14
HELIX 2 2 PHE A 33 ALA A 54 1 22
HELIX 3 3 LEU A 102 ASN A 108 1 7
HELIX 4 4 GLY A 110 LEU A 133 1 24
HELIX 5 5 SER A 134 LEU A 137 5 4
HELIX 6 6 TRP A 142 TYR A 147 1 6
HELIX 7 7 TYR A 147 VAL A 157 1 11
HELIX 8 8 LEU A 159 GLY A 166 1 8
HELIX 9 9 GLY A 175 ASN A 191 1 17
HELIX 10 10 ILE A 192 MET A 194 5 3
HELIX 11 11 HIS A 195 SER A 221 1 27
HELIX 12 12 VAL A 249 PHE A 260 1 12
HELIX 13 13 ASN A 266 HIS A 272 1 7
HELIX 14 14 HIS A 272 PHE A 295 1 24
HELIX 15 15 THR A 316 VAL A 330 1 15
HELIX 16 16 PRO B 16 ALA B 43 1 28
HELIX 17 17 VAL B 62 LEU B 69 1 8
HELIX 18 18 PHE B 93 TYR B 117 1 25
HELIX 19 19 ASP B 134 PRO B 136 5 3
HELIX 20 20 LYS B 137 HIS B 157 1 21
HELIX 21 21 PRO B 195 VAL B 219 1 25
HELIX 22 22 PRO B 222 LEU B 229 1 8
HELIX 23 23 ILE B 234 TYR B 258 1 25
HELIX 24 24 THR B 271 SER B 277 1 7
HELIX 25 25 PHE B 280 ALA B 293 1 14
HELIX 26 26 GLU B 307 ASP B 313 1 7
HELIX 27 27 TYR B 314 ASN B 318 5 5
HELIX 28 28 ASP B 413 ILE B 425 1 13
HELIX 29 29 SER B 446 PHE B 475 1 30
HELIX 30 30 ARG B 476 GLY B 481 1 6
HELIX 31 31 ASN C 39 ASN C 44 5 6
HELIX 32 32 LEU C 45 HIS C 74 1 30
HELIX 33 33 MET C 81 GLY C 85 5 5
HELIX 34 34 LEU C 88 TRP C 97 1 10
HELIX 35 35 THR C 108 TYR C 131 1 24
HELIX 36 36 ASP C 153 MET C 180 1 28
HELIX 37 37 ASN C 229 THR C 254 1 26
HELIX 38 38 TRP C 259 PHE C 264 1 6
HELIX 39 39 SER C 267 ASN C 293 1 27
HELIX 40 40 THR C 305 LYS C 323 1 19
HELIX 41 41 ASP C 376 ASN C 382 1 7
HELIX 42 42 GLN C 385 HIS C 398 1 14
HELIX 43 43 SER C 421 ARG C 447 1 27
HELIX 44 44 ARG C 447 ALA C 452 1 6
HELIX 45 45 TRP D 14 ARG D 24 1 11
HELIX 46 46 GLY D 31 VAL D 55 1 25
HELIX 47 47 ALA D 82 GLY D 86 5 5
HELIX 48 48 ASP D 100 GLY D 108 1 9
HELIX 49 49 GLY D 108 GLY D 137 1 30
HELIX 50 50 PRO D 140 LEU D 158 1 19
HELIX 51 51 LEU D 158 GLN D 164 1 7
HELIX 52 52 ALA D 176 ASN D 190 1 15
HELIX 53 53 ASN D 194 LEU D 222 1 29
HELIX 54 54 SER D 245 GLN D 255 1 11
HELIX 55 55 ASN D 263 ALA D 290 1 28
HELIX 56 56 SER D 300 ALA D 305 1 6
HELIX 57 57 THR D 313 ALA D 330 1 18
HELIX 58 58 PRO D 331 ASP D 333 5 3
HELIX 59 59 ASP E 12 VAL E 17 1 6
HELIX 60 60 VAL E 17 GLY E 41 1 25
HELIX 61 61 GLY E 41 GLY E 48 1 8
HELIX 62 62 ARG E 51 TYR E 55 5 5
HELIX 63 63 ALA E 72 LYS E 84 1 13
HELIX 64 64 THR F 17 GLN F 41 1 25
HELIX 65 65 ALA G 11 THR G 24 1 14
HELIX 66 66 PHE G 33 ALA G 54 1 22
HELIX 67 67 LEU G 102 ASN G 108 1 7
HELIX 68 68 GLY G 110 LEU G 133 1 24
HELIX 69 69 SER G 134 LEU G 137 5 4
HELIX 70 70 TRP G 142 TYR G 147 1 6
HELIX 71 71 TYR G 147 VAL G 157 1 11
HELIX 72 72 LEU G 159 GLY G 166 1 8
HELIX 73 73 GLY G 175 ASN G 191 1 17
HELIX 74 74 ILE G 192 MET G 194 5 3
HELIX 75 75 HIS G 195 SER G 221 1 27
HELIX 76 76 ASN G 247 PHE G 260 1 14
HELIX 77 77 ASN G 266 HIS G 272 1 7
HELIX 78 78 HIS G 272 PHE G 295 1 24
HELIX 79 79 THR G 316 VAL G 330 1 15
HELIX 80 80 PRO H 16 ALA H 43 1 28
HELIX 81 81 VAL H 62 LEU H 69 1 8
HELIX 82 82 SER H 92 TYR H 117 1 26
HELIX 83 83 ASP H 134 PRO H 136 5 3
HELIX 84 84 LYS H 137 ALA H 155 1 19
HELIX 85 85 PRO H 195 VAL H 219 1 25
HELIX 86 86 PRO H 222 LEU H 229 1 8
HELIX 87 87 ILE H 234 TYR H 258 1 25
HELIX 88 88 THR H 271 SER H 277 1 7
HELIX 89 89 PHE H 280 ALA H 293 1 14
HELIX 90 90 GLU H 307 ASP H 313 1 7
HELIX 91 91 TYR H 314 ASN H 318 5 5
HELIX 92 92 ASP H 413 ILE H 425 1 13
HELIX 93 93 SER H 446 PHE H 475 1 30
HELIX 94 94 ARG H 476 GLY H 481 1 6
HELIX 95 95 ALA I 40 LEU I 45 1 6
HELIX 96 96 LEU I 45 HIS I 74 1 30
HELIX 97 97 MET I 81 GLY I 85 5 5
HELIX 98 98 LEU I 88 TRP I 97 1 10
HELIX 99 99 THR I 108 ILE I 134 1 27
HELIX 100 100 ASP I 153 MET I 180 1 28
HELIX 101 101 ASN I 229 THR I 254 1 26
HELIX 102 102 TRP I 259 PHE I 264 1 6
HELIX 103 103 SER I 267 ASN I 293 1 27
HELIX 104 104 THR I 305 LYS I 323 1 19
HELIX 105 105 ASP I 376 ASN I 382 1 7
HELIX 106 106 GLN I 385 HIS I 398 1 14
HELIX 107 107 SER I 421 ALA I 452 1 32
HELIX 108 108 TRP J 14 ARG J 24 1 11
HELIX 109 109 GLY J 31 VAL J 55 1 25
HELIX 110 110 ALA J 82 GLY J 86 5 5
HELIX 111 111 ASP J 100 GLY J 108 1 9
HELIX 112 112 GLY J 109 GLY J 137 1 29
HELIX 113 113 PRO J 140 LEU J 158 1 19
HELIX 114 114 LEU J 158 GLN J 164 1 7
HELIX 115 115 ALA J 176 ASN J 190 1 15
HELIX 116 116 ASN J 194 LEU J 222 1 29
HELIX 117 117 SER J 245 ILE J 256 1 12
HELIX 118 118 ASN J 263 ALA J 290 1 28
HELIX 119 119 SER J 300 ALA J 305 1 6
HELIX 120 120 THR J 313 ALA J 330 1 18
HELIX 121 121 PRO J 331 ASP J 333 5 3
HELIX 122 122 ASP K 12 VAL K 17 1 6
HELIX 123 123 VAL K 17 GLY K 41 1 25
HELIX 124 124 GLY K 41 GLY K 48 1 8
HELIX 125 125 ARG K 51 TYR K 55 5 5
HELIX 126 126 ALA K 72 LYS K 84 1 13
HELIX 127 127 THR L 17 GLN L 41 1 25
HELIX 128 128 UNK O 123 UNK O 128 1 6
HELIX 129 129 UNK P 123 UNK P 128 1 6
HELIX 130 130 UNK S 10 UNK S 16 1 7
HELIX 131 131 UNK S 29 UNK S 35 5 7
HELIX 132 132 UNK S 39 UNK S 50 1 12
HELIX 133 133 UNK S 55 UNK S 61 5 7
HELIX 134 134 UNK S 66 UNK S 76 1 11
HELIX 135 135 UNK S 86 UNK S 91 1 6
HELIX 136 136 THR T 4 LEU T 8 1 5
HELIX 137 137 THR T 22 CYS T 37 1 16
HELIX 138 138 CYS T 37 VAL T 42 1 6
HELIX 139 139 GLY T 43 ILE T 45 5 3
HELIX 140 140 ARG T 55 LEU T 61 1 7
HELIX 141 141 ASN T 68 ASN T 78 1 11
HELIX 142 142 PHE T 101 ARG T 105 5 5
HELIX 143 143 THR T 108 GLY T 127 1 20
HELIX 144 144 ASP T 128 GLY T 131 5 4
HELIX 145 145 UNK U 10 UNK U 16 1 7
HELIX 146 146 UNK U 29 UNK U 35 5 7
HELIX 147 147 UNK U 39 UNK U 50 1 12
HELIX 148 148 UNK U 55 UNK U 61 5 7
HELIX 149 149 UNK U 66 UNK U 76 1 11
HELIX 150 150 UNK U 86 UNK U 91 1 6
HELIX 151 151 THR V 4 LEU V 8 1 5
HELIX 152 152 THR V 22 CYS V 37 1 16
HELIX 153 153 CYS V 37 VAL V 42 1 6
HELIX 154 154 GLY V 43 ILE V 45 5 3
HELIX 155 155 ARG V 55 LEU V 61 1 7
HELIX 156 156 ASN V 68 ASN V 78 1 11
HELIX 157 157 PHE V 101 ARG V 105 5 5
HELIX 158 158 THR V 108 GLY V 127 1 20
HELIX 159 159 ASP V 128 GLY V 131 5 4
HELIX 160 160 UNK X 3 UNK X 21 1 19
HELIX 161 161 UNK X 53 UNK X 72 1 20
HELIX 162 162 UNK X 107 UNK X 124 1 18
HELIX 163 163 UNK X 124 UNK X 129 1 6
HELIX 164 164 UNK X 157 UNK X 182 1 26
HELIX 165 165 UNK X 200 UNK X 227 1 28
HELIX 166 166 UNK X 252 UNK X 278 1 27
HELIX 167 167 UNK X 311 UNK X 326 1 16
HELIX 168 168 UNK X 328 UNK X 333 1 6
HELIX 169 169 UNK X 355 UNK X 374 1 20
HELIX 170 170 UNK X 405 UNK X 440 1 36
HELIX 171 171 UNK X 455 UNK X 474 1 20
HELIX 172 172 UNK X 503 UNK X 508 5 6
HELIX 173 173 UNK X 509 UNK X 517 1 9
HELIX 174 174 UNK X 518 UNK X 533 1 16
HELIX 175 175 UNK X 552 UNK X 562 1 11
HELIX 176 176 UNK X 563 UNK X 584 1 22
HELIX 177 177 UNK Y 3 UNK Y 21 1 19
HELIX 178 178 UNK Y 53 UNK Y 72 1 20
HELIX 179 179 UNK Y 107 UNK Y 124 1 18
HELIX 180 180 UNK Y 124 UNK Y 129 1 6
HELIX 181 181 UNK Y 157 UNK Y 182 1 26
HELIX 182 182 UNK Y 200 UNK Y 227 1 28
HELIX 183 183 UNK Y 252 UNK Y 278 1 27
HELIX 184 184 UNK Y 311 UNK Y 326 1 16
HELIX 185 185 UNK Y 328 UNK Y 333 1 6
HELIX 186 186 UNK Y 355 UNK Y 374 1 20
HELIX 187 187 UNK Y 405 UNK Y 439 1 35
HELIX 188 188 UNK Y 455 UNK Y 474 1 20
HELIX 189 189 UNK Y 503 UNK Y 508 5 6
HELIX 190 190 UNK Y 509 UNK Y 517 1 9
HELIX 191 191 UNK Y 518 UNK Y 533 1 16
HELIX 192 192 UNK Y 552 UNK Y 562 1 11
HELIX 193 193 UNK Y 563 UNK Y 584 1 22
SHEET 1 AA 2 SER A 305 VAL A 306 0
SHEET 2 AA 2 VAL A 313 ILE A 314 -1 O ILE A 314 N SER A 305
SHEET 1 BA 2 MET B 166 VAL B 168 0
SHEET 2 BA 2 SER B 177 GLN B 179 -1 O SER B 177 N VAL B 168
SHEET 1 BB 2 GLN B 338 TRP B 340 0
SHEET 2 BB 2 PHE B 430 GLU B 431 -1 O GLU B 431 N GLN B 338
SHEET 1 HA 2 MET H 166 VAL H 168 0
SHEET 2 HA 2 SER H 177 GLN H 179 -1 O SER H 177 N VAL H 168
SHEET 1 HB 2 GLN H 338 TRP H 340 0
SHEET 2 HB 2 PHE H 430 GLU H 431 -1 O GLU H 431 N GLN H 338
SHEET 1 OA 5 UNK O 29 UNK O 30 0
SHEET 2 OA 5 UNK O 7 UNK O 16 -1 O UNK O 16 N UNK O 29
SHEET 3 OA 5 UNK O 168 UNK O 177 -1 O UNK O 170 N UNK O 15
SHEET 4 OA 5 UNK O 149 UNK O 156 -1 O UNK O 149 N UNK O 175
SHEET 5 OA 5 UNK O 141 UNK O 142 -1 O UNK O 141 N UNK O 150
SHEET 1 OB 3 UNK O 32 UNK O 33 0
SHEET 2 OB 3 UNK O 62 UNK O 64 -1 O UNK O 64 N UNK O 32
SHEET 3 OB 3 UNK O 71 UNK O 73 -1 O UNK O 72 N UNK O 63
SHEET 1 OC 2 UNK O 49 UNK O 51 0
SHEET 2 OC 2 UNK O 83 UNK O 85 -1 O UNK O 83 N UNK O 51
SHEET 1 OD 2 UNK O 90 UNK O 94 0
SHEET 2 OD 2 UNK O 134 UNK O 138 -1 O UNK O 134 N UNK O 94
SHEET 1 PA 5 UNK P 29 UNK P 30 0
SHEET 2 PA 5 UNK P 7 UNK P 16 -1 O UNK P 16 N UNK P 29
SHEET 3 PA 5 UNK P 168 UNK P 177 -1 O UNK P 170 N UNK P 15
SHEET 4 PA 5 UNK P 149 UNK P 156 -1 O UNK P 149 N UNK P 175
SHEET 5 PA 5 UNK P 141 UNK P 142 -1 O UNK P 141 N UNK P 150
SHEET 1 PB 3 UNK P 32 UNK P 33 0
SHEET 2 PB 3 UNK P 62 UNK P 64 -1 O UNK P 64 N UNK P 32
SHEET 3 PB 3 UNK P 71 UNK P 73 -1 O UNK P 72 N UNK P 63
SHEET 1 PC 2 UNK P 49 UNK P 51 0
SHEET 2 PC 2 UNK P 83 UNK P 85 -1 O UNK P 83 N UNK P 51
SHEET 1 PD 2 UNK P 90 UNK P 94 0
SHEET 2 PD 2 UNK P 134 UNK P 138 -1 O UNK P 134 N UNK P 94
SHEET 1 SA 2 UNK S 23 UNK S 24 0
SHEET 2 SA 2 UNK S 80 UNK S 81 1 N UNK S 81 O UNK S 23
SHEET 1 TA 2 THR T 9 PRO T 11 0
SHEET 2 TA 2 THR T 18 THR T 20 -1 O ILE T 19 N VAL T 10
SHEET 1 UA 2 UNK U 23 UNK U 24 0
SHEET 2 UA 2 UNK U 80 UNK U 81 1 N UNK U 81 O UNK U 23
SHEET 1 VA 2 THR V 9 PRO V 11 0
SHEET 2 VA 2 THR V 18 THR V 20 -1 O ILE V 19 N VAL V 10
LINK NE2 HIS A 198 MG CLA A1342 1555 1555 2.22
LINK MN MN A1347 OD1 ASP A 170 1555 1555 2.38
LINK MN MN A1347 OE1 GLU A 333 1555 1555 2.03
LINK MN MN A1347 OE2 GLU A 333 1555 1555 2.17
LINK MN MN A1347 MN MN A1349 1555 1555 2.88
LINK FE FE2 A1350 NE2 HIS A 215 1555 1555 1.98
LINK FE FE2 A1350 NE2 HIS A 272 1555 1555 2.08
LINK FE FE2 A1350 NE2 HIS D 214 1555 1555 2.09
LINK FE FE2 A1350 NE2 HIS D 268 1555 1555 2.29
LINK NE2 HIS B 100 MG CLA B1486 1555 1555 2.58
LINK NE2 HIS B 114 MG CLA B1497 1555 1555 2.36
LINK ND1 HIS B 201 MG CLA B1483 1555 1555 2.05
LINK NE2 HIS B 216 MG CLA B1490 1555 1555 2.24
LINK NE2 HIS B 455 MG CLA B1485 1555 1555 2.14
LINK NE2 HIS B 466 MG CLA B1489 1555 1555 2.15
LINK NE2 HIS B 469 MG CLA B1492 1555 1555 2.00
LINK OD1 ASN C 39 MG CLA C1469 1555 1555 2.70
LINK NE2 HIS C 53 MG CLA C1467 1555 1555 2.53
LINK NE2 HIS C 56 MG CLA C1468 1555 1555 2.37
LINK NE2 HIS C 118 MG CLA C1461 1555 1555 2.41
LINK NE2 HIS C 237 MG CLA C1459 1555 1555 1.94
LINK NE2 HIS C 251 MG CLA C1464 1555 1555 2.45
LINK NE2 HIS C 430 MG CLA C1460 1555 1555 2.46
LINK NE2 HIS C 441 MG CLA C1463 1555 1555 2.12
LINK NE2 HIS C 444 MG CLA C1466 1555 1555 2.28
LINK NE2 HIS D 117 MG CLA D1353 1555 1555 2.47
LINK NE2 HIS D 197 MG CLA D1351 1555 1555 2.22
LINK NE2 HIS E 23 FE HEM E1085 1555 1555 2.21
LINK NE2 HIS F 24 FE HEM E1085 1555 1555 1.87
LINK NE2 HIS G 198 MG CLA G1342 1555 1555 2.13
LINK MN MN G1347 OE2 GLU G 333 1555 1555 2.02
LINK MN MN G1347 OD1 ASP G 170 1555 1555 2.32
LINK MN MN G1347 OE1 GLU G 333 1555 1555 1.97
LINK MN MN G1347 OD2 ASP G 170 1555 1555 2.57
LINK MN MN G1348 NE2 HIS G 332 1555 1555 2.43
LINK FE FE2 G1350 NE2 HIS G 215 1555 1555 1.99
LINK FE FE2 G1350 NE2 HIS G 272 1555 1555 2.15
LINK FE FE2 G1350 NE2 HIS J 214 1555 1555 2.08
LINK FE FE2 G1350 NE2 HIS J 268 1555 1555 2.19
LINK NE2 HIS H 100 MG CLA H1486 1555 1555 2.53
LINK NE2 HIS H 114 MG CLA H1497 1555 1555 2.42
LINK ND1 HIS H 201 MG CLA H1483 1555 1555 2.05
LINK NE2 HIS H 216 MG CLA H1490 1555 1555 2.27
LINK NE2 HIS H 455 MG CLA H1485 1555 1555 2.13
LINK NE2 HIS H 466 MG CLA H1489 1555 1555 2.16
LINK NE2 HIS H 469 MG CLA H1492 1555 1555 1.98
LINK OD1 ASN I 39 MG CLA I1469 1555 1555 2.70
LINK NE2 HIS I 53 MG CLA I1467 1555 1555 2.50
LINK NE2 HIS I 56 MG CLA I1468 1555 1555 2.33
LINK NE2 HIS I 118 MG CLA I1461 1555 1555 2.37
LINK NE2 HIS I 237 MG CLA I1459 1555 1555 1.97
LINK NE2 HIS I 251 MG CLA I1464 1555 1555 2.45
LINK NE2 HIS I 430 MG CLA I1460 1555 1555 2.49
LINK NE2 HIS I 441 MG CLA I1463 1555 1555 2.08
LINK NE2 HIS I 444 MG CLA I1466 1555 1555 2.25
LINK NE2 HIS J 117 MG CLA J1353 1555 1555 2.45
LINK NE2 HIS J 197 MG CLA J1351 1555 1555 2.19
LINK NE2 HIS L 24 FE HEM L1046 1555 1555 1.78
LINK FE HEM L1046 NE2 HIS K 23 1555 1555 2.31
LINK SG CYS T 37 CAB HEC T1138 1555 1555 1.73
LINK NE2 HIS T 41 FE HEC T1138 1555 1555 2.09
LINK NE2 HIS T 92 FE HEC T1138 1555 1555 2.04
LINK SG CYS V 37 CAB HEC V1138 1555 1555 1.51
LINK NE2 HIS V 41 FE HEC V1138 1555 1555 2.09
LINK NE2 HIS V 92 FE HEC V1138 1555 1555 2.05
CISPEP 1 THR T 63 PRO T 64 0 -0.03
CISPEP 2 THR V 63 PRO V 64 0 0.08
SITE 1 AC1 22 PHE A 119 TYR A 147 PRO A 150 SER A 153
SITE 2 AC1 22 MET A 183 ILE A 184 PHE A 186 GLN A 187
SITE 3 AC1 22 ILE A 192 LEU A 193 HIS A 198 GLY A 201
SITE 4 AC1 22 VAL A 205 PHE A 206 VAL A 283 THR A 286
SITE 5 AC1 22 ILE A 290 CLA A1343 CLA A1344 PHO A1345
SITE 6 AC1 22 LEU D 205 CLA D1351
SITE 1 AC2 11 VAL A 157 PHE A 158 MET A 172 ILE A 176
SITE 2 AC2 11 PHE A 180 MET A 183 CLA A1342 MET D 198
SITE 3 AC2 11 VAL D 201 ALA D 202 CLA D1351
SITE 1 AC3 11 GLN A 199 VAL A 202 ALA A 203 CLA A1342
SITE 2 AC3 11 PHE D 157 VAL D 175 ILE D 178 PHE D 179
SITE 3 AC3 11 LEU D 182 CLA D1351 PHO D1352
SITE 1 AC4 20 LEU A 41 ALA A 44 THR A 45 ILE A 115
SITE 2 AC4 20 PHE A 119 TYR A 126 GLN A 130 ALA A 146
SITE 3 AC4 20 TYR A 147 PRO A 150 LEU A 174 GLY A 175
SITE 4 AC4 20 PRO A 279 VAL A 283 CLA A1342 LEU D 205
SITE 5 AC4 20 ALA D 208 ALA D 212 ILE D 213 PHE D 257
SITE 1 AC5 8 PRO A 39 THR A 40 PRO A 95 ILE A 96
SITE 2 AC5 8 TRP A 97 GLN A 113 LEU A 114 HIS A 118
SITE 1 AC6 3 ASP A 170 GLU A 333 MN A1349
SITE 1 AC7 4 GLU A 189 HIS A 332 MN A1349 MN A1354
SITE 1 AC8 5 GLU A 189 GLU A 333 MN A1347 MN A1348
SITE 2 AC8 5 MN A1354
SITE 1 AC9 4 HIS A 215 HIS A 272 HIS D 214 HIS D 268
SITE 1 BC1 2 MN A1348 MN A1349
SITE 1 BC2 2 ASP B 188 PHE B 190
SITE 1 BC3 8 PHE B 190 PRO B 192 ALA B 200 HIS B 201
SITE 2 BC3 8 ALA B 204 VAL B 208 PHE B 247 CLA B1484
SITE 1 BC4 14 ARG B 68 LEU B 69 ALA B 146 LEU B 149
SITE 2 BC4 14 CYS B 150 PHE B 153 LEU B 158 HIS B 201
SITE 3 BC4 14 HIS B 202 VAL B 252 THR B 262 CLA B1483
SITE 4 BC4 14 CLA B1485 CLA B1487
SITE 1 BC5 18 TRP B 33 PHE B 61 PHE B 65 ARG B 68
SITE 2 BC5 18 LEU B 69 VAL B 245 ALA B 248 ALA B 249
SITE 3 BC5 18 VAL B 252 PHE B 451 HIS B 455 PHE B 458
SITE 4 BC5 18 ALA B 459 CLA B1484 CLA B1486 CLA B1488
SITE 5 BC5 18 CLA B1492 CLA B1494
SITE 1 BC6 10 THR B 27 VAL B 30 ALA B 31 ALA B 34
SITE 2 BC6 10 VAL B 62 PHE B 65 MET B 66 VAL B 96
SITE 3 BC6 10 HIS B 100 CLA B1485
SITE 1 BC7 9 LEU B 69 GLY B 70 GLY B 152 PHE B 153
SITE 2 BC7 9 PHE B 156 HIS B 157 PHE B 162 PRO B 164
SITE 3 BC7 9 CLA B1484
SITE 1 BC8 10 TRP B 33 TYR B 40 GLY B 59 PHE B 61
SITE 2 BC8 10 ARG B 326 TRP B 450 PHE B 451 CLA B1485
SITE 3 BC8 10 CLA B1494 MET D 281
SITE 1 BC9 14 SER B 239 SER B 240 ALA B 243 PHE B 246
SITE 2 BC9 14 PHE B 247 PHE B 463 HIS B 466 ILE B 467
SITE 3 BC9 14 THR B 473 LEU B 474 CLA B1490 ILE D 123
SITE 4 BC9 14 MET D 126 PHE D 130
SITE 1 CC1 6 PHE B 139 PHE B 215 HIS B 216 PRO B 221
SITE 2 CC1 6 CLA B1489 CLA B1491
SITE 1 CC2 6 PHE B 139 HIS B 142 VAL B 237 SER B 240
SITE 2 CC2 6 SER B 241 CLA B1490
SITE 1 CC3 13 LEU B 238 ILE B 242 LEU B 461 PHE B 462
SITE 2 CC3 13 PHE B 464 GLY B 465 TRP B 468 HIS B 469
SITE 3 CC3 13 ARG B 472 CLA B1485 CLA B1493 CLA B1494
SITE 4 CC3 13 CLA B1495
SITE 1 CC4 10 LEU B 19 ALA B 22 HIS B 23 HIS B 26
SITE 2 CC4 10 GLU B 235 VAL B 237 LEU B 238 SER B 241
SITE 3 CC4 10 CLA B1492 CLA B1496
SITE 1 CC5 8 HIS B 26 VAL B 30 PHE B 458 PHE B 462
SITE 2 CC5 8 CLA B1485 CLA B1488 CLA B1492 CLA B1495
SITE 1 CC6 4 ALA B 22 LEU B 29 CLA B1492 CLA B1494
SITE 1 CC7 12 HIS B 23 LEU B 24 LEU B 106 LEU B 109
SITE 2 CC7 12 ALA B 110 TRP B 113 MET B 138 ILE B 141
SITE 3 CC7 12 HIS B 142 LEU B 145 CLA B1493 CLA B1497
SITE 1 CC8 6 LEU B 24 LEU B 107 ALA B 110 TRP B 113
SITE 2 CC8 6 HIS B 114 CLA B1496
SITE 1 CC9 11 THR C 94 LEU C 95 LEU C 168 GLY C 171
SITE 2 CC9 11 ALA C 172 VAL C 233 HIS C 237 PHE C 289
SITE 3 CC9 11 VAL C 296 TYR C 297 CLA C1460
SITE 1 DC1 13 TRP C 63 HIS C 91 GLY C 283 ALA C 286
SITE 2 DC1 13 VAL C 290 TYR C 297 HIS C 430 LEU C 433
SITE 3 DC1 13 ALA C 434 PHE C 437 CLA C1459 CLA C1462
SITE 4 DC1 13 CLA C1468
SITE 1 DC2 1 HIS C 118
SITE 1 DC3 8 PHE A 300 TRP C 63 MET C 67 PHE C 70
SITE 2 DC3 8 GLY C 85 TRP C 425 SER C 429 CLA C1460
SITE 1 DC4 11 TRP A 131 SER C 273 TYR C 274 GLY C 277
SITE 2 DC4 11 ALA C 278 HIS C 441 LEU C 442 ALA C 445
SITE 3 DC4 11 ARG C 449 CLA C1464 CLA C1465
SITE 1 DC5 11 ILE C 243 CYS C 244 TRP C 250 HIS C 251
SITE 2 DC5 11 PRO C 256 PHE C 257 TRP C 259 ALA C 260
SITE 3 DC5 11 PHE C 264 CLA C1463 CLA C1465
SITE 1 DC6 16 MET C 157 THR C 158 LEU C 161 HIS C 164
SITE 2 DC6 16 LEU C 168 ILE C 240 PHE C 264 TRP C 266
SITE 3 DC6 16 TYR C 271 TYR C 274 SER C 275 LEU C 279
SITE 4 DC6 16 MET C 282 CLA C1463 CLA C1464 CLA C1467
SITE 1 DC7 13 TRP C 36 ALA C 37 ASN C 39 ALA C 40
SITE 2 DC7 13 LEU C 272 LEU C 276 PHE C 437 VAL C 439
SITE 3 DC7 13 GLY C 440 TRP C 443 HIS C 444 ARG C 447
SITE 4 DC7 13 CLA C1467
SITE 1 DC8 12 ASN C 39 ILE C 43 HIS C 53 HIS C 56
SITE 2 DC8 12 GLY C 268 GLU C 269 TYR C 271 LEU C 272
SITE 3 DC8 12 SER C 275 CLA C1465 CLA C1466 CLA C1468
SITE 1 DC9 3 HIS C 56 CLA C1460 CLA C1467
SITE 1 EC1 6 ARG C 26 GLY C 38 ASN C 39 ARG C 41
SITE 2 EC1 6 LYS C 48 ALA C 52
SITE 1 EC2 6 HIS C 53 ALA C 57 ILE C 160 PHE C 163
SITE 2 EC2 6 HIS C 164 VAL C 167
SITE 1 EC3 6 VAL C 124 PHE C 127 GLY C 128 TYR C 131
SITE 2 EC3 6 HIS C 132 PRO C 137
SITE 1 EC4 18 MET A 183 PHE A 206 CLA A1342 CLA A1343
SITE 2 EC4 18 CLA A1344 LEU D 122 VAL D 152 SER D 155
SITE 3 EC4 18 VAL D 156 LEU D 182 PHE D 185 GLN D 186
SITE 4 EC4 18 TRP D 191 HIS D 197 VAL D 201 VAL D 204
SITE 5 EC4 18 LEU D 279 PHO D1352
SITE 1 EC5 17 PHE A 206 LEU A 210 ALA A 213 MET A 214
SITE 2 EC5 17 ILE A 259 CLA A1344 GLY D 118 PHE D 125
SITE 3 EC5 17 ASN D 142 ALA D 145 PHE D 146 PRO D 149
SITE 4 EC5 17 PHE D 153 PHE D 173 PRO D 275 LEU D 279
SITE 5 EC5 17 CLA D1351
SITE 1 EC6 10 LEU D 36 LEU D 43 LEU D 89 LEU D 90
SITE 2 EC6 10 LEU D 91 LEU D 92 TRP D 93 THR D 112
SITE 3 EC6 10 PHE D 113 HIS D 117
SITE 1 EC7 4 THR D 217 TRP D 253 PHE D 261 LEU D 267
SITE 1 EC8 6 TYR E 19 HIS E 23 THR E 26 TRP F 20
SITE 2 EC8 6 HIS F 24 ALA F 27
SITE 1 EC9 7 TYR D 42 LEU D 49 PHE D 101 PHE D 113
SITE 2 EC9 7 PRO F 29 THR F 30 PHE F 33
SITE 1 FC1 22 PHE G 119 TYR G 147 PRO G 150 SER G 153
SITE 2 FC1 22 MET G 183 ILE G 184 PHE G 186 GLN G 187
SITE 3 FC1 22 ILE G 192 LEU G 193 HIS G 198 GLY G 201
SITE 4 FC1 22 VAL G 205 PHE G 206 VAL G 283 THR G 286
SITE 5 FC1 22 ILE G 290 CLA G1343 CLA G1344 PHO G1345
SITE 6 FC1 22 LEU J 205 CLA J1351
SITE 1 FC2 12 VAL G 157 PHE G 158 MET G 172 ILE G 176
SITE 2 FC2 12 PHE G 180 MET G 183 CLA G1342 MET J 198
SITE 3 FC2 12 VAL J 201 ALA J 202 LEU J 209 CLA J1351
SITE 1 FC3 11 GLN G 199 VAL G 202 ALA G 203 CLA G1342
SITE 2 FC3 11 PHE J 157 VAL J 175 ILE J 178 PHE J 179
SITE 3 FC3 11 LEU J 182 CLA J1351 PHO J1352
SITE 1 FC4 21 LEU G 41 ALA G 44 THR G 45 PHE G 48
SITE 2 FC4 21 ILE G 115 PHE G 119 TYR G 126 GLN G 130
SITE 3 FC4 21 ALA G 146 TYR G 147 PRO G 150 LEU G 174
SITE 4 FC4 21 GLY G 175 PRO G 279 VAL G 283 CLA G1342
SITE 5 FC4 21 LEU J 205 ALA J 208 ALA J 212 ILE J 213
SITE 6 FC4 21 PHE J 257
SITE 1 FC5 9 PRO G 39 THR G 40 PHE G 93 PRO G 95
SITE 2 FC5 9 ILE G 96 TRP G 97 GLN G 113 LEU G 114
SITE 3 FC5 9 HIS G 118
SITE 1 FC6 3 ASP G 170 GLU G 333 MN G1349
SITE 1 FC7 4 GLU G 189 HIS G 332 MN G1349 MN G5054
SITE 1 FC8 6 ASP G 170 GLU G 189 GLU G 333 MN G1347
SITE 2 FC8 6 MN G1348 MN G5054
SITE 1 FC9 4 HIS G 215 HIS G 272 HIS J 214 HIS J 268
SITE 1 GC1 2 MN G1348 MN G1349
SITE 1 GC2 2 ASP H 188 PHE H 190
SITE 1 GC3 9 PHE H 190 PRO H 192 ALA H 200 HIS H 201
SITE 2 GC3 9 ALA H 204 VAL H 208 PHE H 247 THR H 255
SITE 3 GC3 9 CLA H1484
SITE 1 GC4 14 ARG H 68 LEU H 69 ALA H 146 LEU H 149
SITE 2 GC4 14 CYS H 150 PHE H 153 MET H 166 HIS H 201
SITE 3 GC4 14 HIS H 202 VAL H 252 THR H 262 CLA H1483
SITE 4 GC4 14 CLA H1485 CLA H1487
SITE 1 GC5 17 TRP H 33 PHE H 61 PHE H 65 ARG H 68
SITE 2 GC5 17 VAL H 245 ALA H 248 ALA H 249 VAL H 252
SITE 3 GC5 17 PHE H 451 HIS H 455 PHE H 458 ALA H 459
SITE 4 GC5 17 CLA H1484 CLA H1486 CLA H1488 CLA H1492
SITE 5 GC5 17 CLA H1494
SITE 1 GC6 10 THR H 27 VAL H 30 ALA H 31 ALA H 34
SITE 2 GC6 10 VAL H 62 PHE H 65 MET H 66 VAL H 96
SITE 3 GC6 10 HIS H 100 CLA H1485
SITE 1 GC7 9 LEU H 69 GLY H 70 GLY H 152 PHE H 153
SITE 2 GC7 9 PHE H 156 HIS H 157 PHE H 162 PRO H 164
SITE 3 GC7 9 CLA H1484
SITE 1 GC8 10 TRP H 33 TYR H 40 GLY H 59 PHE H 61
SITE 2 GC8 10 ARG H 326 TRP H 450 PHE H 451 CLA H1485
SITE 3 GC8 10 CLA H1494 MET J 281
SITE 1 GC9 15 THR H 236 SER H 240 ALA H 243 PHE H 246
SITE 2 GC9 15 PHE H 247 PHE H 463 HIS H 466 ILE H 467
SITE 3 GC9 15 THR H 473 LEU H 474 CLA H1490 ILE J 123
SITE 4 GC9 15 MET J 126 LEU J 127 PHE J 130
SITE 1 HC1 6 PHE H 139 PHE H 215 HIS H 216 PRO H 221
SITE 2 HC1 6 CLA H1489 CLA H1491
SITE 1 HC2 6 PHE H 139 HIS H 142 VAL H 237 SER H 240
SITE 2 HC2 6 SER H 241 CLA H1490
SITE 1 HC3 13 LEU H 238 ILE H 242 LEU H 461 PHE H 462
SITE 2 HC3 13 PHE H 464 GLY H 465 TRP H 468 HIS H 469
SITE 3 HC3 13 ARG H 472 CLA H1485 CLA H1493 CLA H1494
SITE 4 HC3 13 CLA H1495
SITE 1 HC4 10 LEU H 19 ALA H 22 HIS H 23 HIS H 26
SITE 2 HC4 10 GLU H 235 VAL H 237 LEU H 238 SER H 241
SITE 3 HC4 10 CLA H1492 CLA H1496
SITE 1 HC5 8 HIS H 26 VAL H 30 PHE H 458 PHE H 462
SITE 2 HC5 8 CLA H1485 CLA H1488 CLA H1492 CLA H1495
SITE 1 HC6 4 ALA H 22 LEU H 29 CLA H1492 CLA H1494
SITE 1 HC7 12 HIS H 23 LEU H 24 LEU H 106 LEU H 109
SITE 2 HC7 12 ALA H 110 TRP H 113 MET H 138 ILE H 141
SITE 3 HC7 12 HIS H 142 LEU H 145 CLA H1493 CLA H1497
SITE 1 HC8 6 LEU H 24 LEU H 107 ALA H 110 TRP H 113
SITE 2 HC8 6 HIS H 114 CLA H1496
SITE 1 HC9 11 THR I 94 LEU I 95 LEU I 168 GLY I 171
SITE 2 HC9 11 ALA I 172 VAL I 233 HIS I 237 PHE I 289
SITE 3 HC9 11 VAL I 296 TYR I 297 CLA I1460
SITE 1 IC1 14 TRP I 63 HIS I 91 GLY I 283 ALA I 286
SITE 2 IC1 14 VAL I 290 TYR I 297 HIS I 430 LEU I 433
SITE 3 IC1 14 ALA I 434 PHE I 437 CLA I1459 CLA I1461
SITE 4 IC1 14 CLA I1462 CLA I1468
SITE 1 IC2 3 VAL I 61 HIS I 118 CLA I1460
SITE 1 IC3 8 PHE G 300 TRP I 63 MET I 67 PHE I 70
SITE 2 IC3 8 GLY I 85 TRP I 425 SER I 429 CLA I1460
SITE 1 IC4 11 TRP G 131 SER I 273 TYR I 274 GLY I 277
SITE 2 IC4 11 ALA I 278 HIS I 441 LEU I 442 ALA I 445
SITE 3 IC4 11 ARG I 449 CLA I1464 CLA I1465
SITE 1 IC5 11 ILE I 243 CYS I 244 TRP I 250 HIS I 251
SITE 2 IC5 11 PRO I 256 PHE I 257 TRP I 259 ALA I 260
SITE 3 IC5 11 PHE I 264 CLA I1463 CLA I1465
SITE 1 IC6 15 MET I 157 THR I 158 LEU I 161 HIS I 164
SITE 2 IC6 15 LEU I 168 ILE I 240 PHE I 264 TRP I 266
SITE 3 IC6 15 TYR I 271 TYR I 274 SER I 275 MET I 282
SITE 4 IC6 15 CLA I1463 CLA I1464 CLA I1467
SITE 1 IC7 13 TRP I 36 ALA I 37 ASN I 39 ALA I 40
SITE 2 IC7 13 LEU I 272 LEU I 276 PHE I 437 VAL I 439
SITE 3 IC7 13 GLY I 440 TRP I 443 HIS I 444 ARG I 447
SITE 4 IC7 13 CLA I1467
SITE 1 IC8 13 ASN I 39 ILE I 43 ALA I 52 HIS I 53
SITE 2 IC8 13 HIS I 56 GLY I 268 GLU I 269 TYR I 271
SITE 3 IC8 13 LEU I 272 SER I 275 CLA I1465 CLA I1466
SITE 4 IC8 13 CLA I1468
SITE 1 IC9 3 HIS I 56 CLA I1460 CLA I1467
SITE 1 JC1 6 ARG I 26 GLY I 38 ASN I 39 ARG I 41
SITE 2 JC1 6 LYS I 48 ALA I 52
SITE 1 JC2 6 HIS I 53 ALA I 57 ILE I 160 PHE I 163
SITE 2 JC2 6 HIS I 164 VAL I 167
SITE 1 JC3 5 VAL I 124 PHE I 127 GLY I 128 TYR I 131
SITE 2 JC3 5 HIS I 132
SITE 1 JC4 18 MET G 183 PHE G 206 CLA G1342 CLA G1343
SITE 2 JC4 18 CLA G1344 LEU J 122 VAL J 152 SER J 155
SITE 3 JC4 18 VAL J 156 LEU J 182 PHE J 185 GLN J 186
SITE 4 JC4 18 TRP J 191 HIS J 197 VAL J 201 VAL J 204
SITE 5 JC4 18 LEU J 279 PHO J1352
SITE 1 JC5 17 PHE G 206 LEU G 210 ALA G 213 MET G 214
SITE 2 JC5 17 ILE G 259 CLA G1344 GLY J 118 PHE J 125
SITE 3 JC5 17 ASN J 142 ALA J 145 PHE J 146 PRO J 149
SITE 4 JC5 17 PHE J 153 PHE J 173 PRO J 275 LEU J 279
SITE 5 JC5 17 CLA J1351
SITE 1 JC6 10 LEU J 36 LEU J 43 LEU J 89 LEU J 90
SITE 2 JC6 10 LEU J 91 LEU J 92 TRP J 93 THR J 112
SITE 3 JC6 10 PHE J 113 HIS J 117
SITE 1 JC7 3 TRP J 253 PHE J 261 LEU J 267
SITE 1 JC8 6 TYR K 19 HIS K 23 THR K 26 TRP L 20
SITE 2 JC8 6 HIS L 24 ALA L 27
SITE 1 JC9 7 TYR J 42 LEU J 49 PHE J 101 PHE J 113
SITE 2 JC9 7 PRO L 29 THR L 30 PHE L 33
SITE 1 KC1 16 ALA T 36 CYS T 37 CYS T 40 HIS T 41
SITE 2 KC1 16 THR T 48 LEU T 52 ASP T 53 THR T 58
SITE 3 KC1 16 LEU T 59 ALA T 62 LEU T 72 TYR T 75
SITE 4 KC1 16 MET T 76 TYR T 82 HIS T 92 ILE T 115
SITE 1 KC2 15 ALA V 36 CYS V 37 CYS V 40 HIS V 41
SITE 2 KC2 15 THR V 48 LEU V 52 ASP V 53 THR V 58
SITE 3 KC2 15 LEU V 59 ALA V 62 LEU V 72 TYR V 75
SITE 4 KC2 15 TYR V 82 HIS V 92 ILE V 115
CRYST1 127.517 224.612 305.632 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 0.007842 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004452 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003272 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
