HEADER PHOTOSYNTHESIS 15-OCT-16 5H2F
TITLE CRYSTAL STRUCTURE OF THE PSBM-DELETION MUTANT OF PHOTOSYSTEM II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTOSYSTEM II PROTEIN D1 1;
COMPND 3 CHAIN: A, a;
COMPND 4 FRAGMENT: UNP RESIDUES 11-344;
COMPND 5 SYNONYM: PSII D1 PROTEIN 1,PHOTOSYSTEM II Q(B) PROTEIN 1;
COMPND 6 EC: 1.10.3.9;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PHOTOSYSTEM II CP47 REACTION CENTER PROTEIN;
COMPND 9 CHAIN: B, b;
COMPND 10 FRAGMENT: UNP RESIDUES 2-506;
COMPND 11 SYNONYM: PSII 47 KDA PROTEIN,PROTEIN CP-47;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: PHOTOSYSTEM II CP43 REACTION CENTER PROTEIN;
COMPND 14 CHAIN: C, c;
COMPND 15 FRAGMENT: UNP RESIDUES 7-461;
COMPND 16 SYNONYM: PSII 43 KDA PROTEIN,PROTEIN CP-43;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;
COMPND 19 CHAIN: D, d;
COMPND 20 FRAGMENT: UNP RESIDUES 11-352;
COMPND 21 SYNONYM: PSII D2 PROTEIN,PHOTOSYSTEM II Q(A) PROTEIN;
COMPND 22 EC: 1.10.3.9;
COMPND 23 MOL_ID: 5;
COMPND 24 MOLECULE: CYTOCHROME B559 SUBUNIT ALPHA;
COMPND 25 CHAIN: E, e;
COMPND 26 FRAGMENT: UNP RESIDUES 5-84;
COMPND 27 SYNONYM: PSII REACTION CENTER SUBUNIT V;
COMPND 28 MOL_ID: 6;
COMPND 29 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;
COMPND 30 CHAIN: F, f;
COMPND 31 FRAGMENT: UNP RESIDUES 13-45;
COMPND 32 SYNONYM: PSII REACTION CENTER SUBUNIT VI;
COMPND 33 MOL_ID: 7;
COMPND 34 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;
COMPND 35 CHAIN: H, h;
COMPND 36 FRAGMENT: UNP RESIDUES 2-64;
COMPND 37 SYNONYM: PSII-H;
COMPND 38 MOL_ID: 8;
COMPND 39 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;
COMPND 40 CHAIN: I, i;
COMPND 41 FRAGMENT: UNP RESIDUES 1-36;
COMPND 42 SYNONYM: PSII-I,PSII 4.4 KDA PROTEIN;
COMPND 43 MOL_ID: 9;
COMPND 44 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;
COMPND 45 CHAIN: J, j;
COMPND 46 FRAGMENT: UNP RESIDUES 1-40;
COMPND 47 SYNONYM: PSII-J;
COMPND 48 MOL_ID: 10;
COMPND 49 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;
COMPND 50 CHAIN: K, k;
COMPND 51 SYNONYM: PSII-K;
COMPND 52 MOL_ID: 11;
COMPND 53 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;
COMPND 54 CHAIN: L, l;
COMPND 55 FRAGMENT: UNP RESIDUES 3-37;
COMPND 56 SYNONYM: PSII-L;
COMPND 57 MOL_ID: 12;
COMPND 58 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;
COMPND 59 CHAIN: O, o;
COMPND 60 FRAGMENT: UNP RESIDUES 30-272;
COMPND 61 SYNONYM: MSP;
COMPND 62 MOL_ID: 13;
COMPND 63 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;
COMPND 64 CHAIN: T, t;
COMPND 65 FRAGMENT: UNP RESIDUES 1-30;
COMPND 66 SYNONYM: PSII-TC;
COMPND 67 MOL_ID: 14;
COMPND 68 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;
COMPND 69 CHAIN: U, u;
COMPND 70 FRAGMENT: UNP RESIDUES 38-134;
COMPND 71 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN,PSII-U;
COMPND 72 MOL_ID: 15;
COMPND 73 MOLECULE: CYTOCHROME C-550;
COMPND 74 CHAIN: V, v;
COMPND 75 SYNONYM: CYTOCHROME C-549,CYTOCHROME C550,LOW-POTENTIAL CYTOCHROME C;
COMPND 76 MOL_ID: 16;
COMPND 77 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;
COMPND 78 CHAIN: Y, y;
COMPND 79 FRAGMENT: UNP RESIDUES 18-46;
COMPND 80 MOL_ID: 17;
COMPND 81 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;
COMPND 82 CHAIN: X, x;
COMPND 83 FRAGMENT: UNP RESIDUES 2-38;
COMPND 84 MOL_ID: 18;
COMPND 85 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;
COMPND 86 CHAIN: Z, z;
COMPND 87 SYNONYM: PSII-Z
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 3 ORGANISM_TAXID: 197221;
SOURCE 4 STRAIN: BP-1;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 7 ORGANISM_TAXID: 197221;
SOURCE 8 STRAIN: BP-1;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 11 ORGANISM_TAXID: 197221;
SOURCE 12 STRAIN: BP-1;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 15 ORGANISM_TAXID: 197221;
SOURCE 16 STRAIN: BP-1;
SOURCE 17 MOL_ID: 5;
SOURCE 18 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 19 ORGANISM_TAXID: 197221;
SOURCE 20 STRAIN: BP-1;
SOURCE 21 MOL_ID: 6;
SOURCE 22 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 23 ORGANISM_TAXID: 197221;
SOURCE 24 STRAIN: BP-1;
SOURCE 25 MOL_ID: 7;
SOURCE 26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 27 ORGANISM_TAXID: 197221;
SOURCE 28 STRAIN: BP-1;
SOURCE 29 MOL_ID: 8;
SOURCE 30 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 31 ORGANISM_TAXID: 197221;
SOURCE 32 STRAIN: BP-1;
SOURCE 33 MOL_ID: 9;
SOURCE 34 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 35 ORGANISM_TAXID: 197221;
SOURCE 36 STRAIN: BP-1;
SOURCE 37 MOL_ID: 10;
SOURCE 38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 39 ORGANISM_TAXID: 197221;
SOURCE 40 STRAIN: BP-1;
SOURCE 41 MOL_ID: 11;
SOURCE 42 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 43 ORGANISM_TAXID: 197221;
SOURCE 44 STRAIN: BP-1;
SOURCE 45 MOL_ID: 12;
SOURCE 46 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 47 ORGANISM_TAXID: 197221;
SOURCE 48 STRAIN: BP-1;
SOURCE 49 MOL_ID: 13;
SOURCE 50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 51 ORGANISM_TAXID: 197221;
SOURCE 52 STRAIN: BP-1;
SOURCE 53 MOL_ID: 14;
SOURCE 54 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 55 ORGANISM_TAXID: 197221;
SOURCE 56 STRAIN: BP-1;
SOURCE 57 MOL_ID: 15;
SOURCE 58 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 59 ORGANISM_TAXID: 197221;
SOURCE 60 STRAIN: BP-1;
SOURCE 61 MOL_ID: 16;
SOURCE 62 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 63 ORGANISM_TAXID: 197221;
SOURCE 64 STRAIN: BP-1;
SOURCE 65 MOL_ID: 17;
SOURCE 66 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 67 ORGANISM_TAXID: 197221;
SOURCE 68 STRAIN: BP-1;
SOURCE 69 MOL_ID: 18;
SOURCE 70 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 71 ORGANISM_TAXID: 197221;
SOURCE 72 STRAIN: BP-1
KEYWDS PHOTOSYNTHESIS, PHOTOSYSTEM II, MUTANT, PSBM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.UTO,K.KAWAKAMI,Y.UMENA,M.IWAI,M.IKEUCHI,J.R.SHEN,N.KAMIYA
REVDAT 4 29-JUL-20 5H2F 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE
REVDAT 3 02-OCT-19 5H2F 1 COMPND REMARK HET HETNAM
REVDAT 3 2 1 HETSYN FORMUL LINK ATOM
REVDAT 2 30-AUG-17 5H2F 1 JRNL REMARK
REVDAT 1 22-MAR-17 5H2F 0
JRNL AUTH S.UTO,K.KAWAKAMI,Y.UMENA,M.IWAI,M.IKEUCHI,J.R.SHEN,N.KAMIYA
JRNL TITL MUTUAL RELATIONSHIPS BETWEEN STRUCTURAL AND FUNCTIONAL
JRNL TITL 2 CHANGES IN A PSBM-DELETION MUTANT OF PHOTOSYSTEM II.
JRNL REF FARADAY DISCUSS. V. 198 107 2017
JRNL REFN ISSN 1359-6640
JRNL PMID 28272640
JRNL DOI 10.1039/C6FD00213G
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 365283
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 19307
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 25485
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 1291
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 39962
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9423
REMARK 3 SOLVENT ATOMS : 2317
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.00000
REMARK 3 B22 (A**2) : -0.89000
REMARK 3 B33 (A**2) : -2.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.227
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.193
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.142
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.768
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 51170 ; 0.016 ; 0.025
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 70092 ; 2.335 ; 2.534
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 5157 ; 6.068 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1750 ;33.984 ;23.074
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 6098 ;14.763 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 207 ;17.010 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 7217 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 36891 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5H2F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1300001851.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.22
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 385629
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.70500
REMARK 200 R SYM FOR SHELL (I) : 0.70500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP, MOLREP
REMARK 200 STARTING MODEL: 3WU2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG1450, SODIUM CHLORIDE, CALCIUM
REMARK 280 CHLORIDE, MAGNESIUM SULFATE, PH 6.1, MICROBATCH, TEMPERATURE 285K
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 60.97700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 142.94300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 113.49650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 142.94300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 60.97700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 113.49650
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: OCTADECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J, K,
REMARK 350 AND CHAINS: L, O, T, U, V, Y, X, Z
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: OCTADECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: a, b, c, d, e, f, h, i, j, k,
REMARK 350 AND CHAINS: l, o, t, u, v, y, x, z
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 ASN C 19
REMARK 465 SER C 20
REMARK 465 ILE C 21
REMARK 465 PHE C 22
REMARK 465 LYS E 84
REMARK 465 ASP I 36
REMARK 465 MET J 1
REMARK 465 MET J 2
REMARK 465 SER J 3
REMARK 465 GLU J 4
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 GLU d 11
REMARK 465 THR e 5
REMARK 465 TYR f 13
REMARK 465 PRO f 14
REMARK 465 ALA h 64
REMARK 465 GLN x 38
REMARK 465 VAL z 62
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 LEU A 13 CG CD1 CD2
REMARK 470 GLU A 15 CG CD OE1 OE2
REMARK 470 ARG A 16 CG CD NE CZ NH1 NH2
REMARK 470 THR A 228 OG1 CG2
REMARK 470 GLU A 229 CG CD OE1 OE2
REMARK 470 GLU A 231 CG CD OE1 OE2
REMARK 470 GLU A 243 CG CD OE1 OE2
REMARK 470 THR A 286 OG1 CG2
REMARK 470 LYS B 227 CG CD CE NZ
REMARK 470 LYS B 349 CG CD CE NZ
REMARK 470 SER B 480 OG
REMARK 470 GLU B 485 CG CD OE1 OE2
REMARK 470 LEU B 486 CG CD1 CD2
REMARK 470 SER B 487 OG
REMARK 470 GLU B 489 CG CD OE1 OE2
REMARK 470 GLN B 490 CG CD OE1 NE2
REMARK 470 GLU B 492 CG CD OE1 OE2
REMARK 470 GLN B 497 CG CD OE1 NE2
REMARK 470 VAL B 499 CG1 CG2
REMARK 470 VAL B 502 CG1 CG2
REMARK 470 THR B 504 OG1 CG2
REMARK 470 ARG B 505 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 506 CG CD NE CZ NH1 NH2
REMARK 470 THR C 24 OG1 CG2
REMARK 470 ASN C 25 CG OD1 ND2
REMARK 470 SER C 30 OG
REMARK 470 GLU C 142 CG CD OE1 OE2
REMARK 470 ARG C 207 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 11 CG CD OE1 OE2
REMARK 470 ARG D 12 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 61 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 77 CG CD OE1 OE2
REMARK 470 ARG J 7 CG CD NE CZ NH1 NH2
REMARK 470 ARG O 60 CG CD NE CZ NH1 NH2
REMARK 470 GLN O 61 CG CD OE1 NE2
REMARK 470 GLU O 62 CG CD OE1 OE2
REMARK 470 GLU O 98 CG CD OE1 OE2
REMARK 470 ILE T 29 CG1 CG2 CD1
REMARK 470 THR T 30 OG1 CG2
REMARK 470 LYS V 17 CG CD CE NZ
REMARK 470 VAL X 37 CG1 CG2
REMARK 470 GLN X 38 CG CD OE1 NE2
REMARK 470 ILE Z 3 CG1 CG2 CD1
REMARK 470 GLN Z 31 CG CD OE1 NE2
REMARK 470 ASP Z 34 CG OD1 OD2
REMARK 470 ARG Z 35 CG CD NE CZ NH1 NH2
REMARK 470 SER Z 36 OG
REMARK 470 PHE Z 41 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL Z 61 CG1 CG2
REMARK 470 GLU a 15 CG CD OE1 OE2
REMARK 470 LEU a 223 CG CD1 CD2
REMARK 470 ARG a 225 CG CD NE CZ NH1 NH2
REMARK 470 GLU a 226 CG CD OE1 OE2
REMARK 470 THR a 228 OG1 CG2
REMARK 470 GLU a 229 CG CD OE1 OE2
REMARK 470 THR a 230 OG1 CG2
REMARK 470 GLU a 231 CG CD OE1 OE2
REMARK 470 TYR a 235 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU a 242 CG CD OE1 OE2
REMARK 470 GLU a 243 CG CD OE1 OE2
REMARK 470 THR a 245 OG1 CG2
REMARK 470 TYR a 246 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE a 248 CG1 CG2 CD1
REMARK 470 VAL a 249 CG1 CG2
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 THR a 286 OG1 CG2
REMARK 470 ARG b 127 CG CD NE CZ NH1 NH2
REMARK 470 LYS b 227 CG CD CE NZ
REMARK 470 LYS b 349 CD CE NZ
REMARK 470 GLU b 350 CD OE1 OE2
REMARK 470 PHE b 479 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER b 480 OG
REMARK 470 ASN c 19 CG OD1 ND2
REMARK 470 ARG d 24 CG CD NE CZ NH1 NH2
REMARK 470 GLU d 241 CG CD OE1 OE2
REMARK 470 SER e 11 OG
REMARK 470 ARG e 61 CG CD NE CZ NH1 NH2
REMARK 470 LYS e 84 CG CD CE NZ
REMARK 470 GLU i 2 CD OE1 OE2
REMARK 470 MET j 1 CG SD CE
REMARK 470 MET j 2 SD CE
REMARK 470 ARG j 7 CG CD NE CZ NH1 NH2
REMARK 470 LYS k 10 CG CD CE NZ
REMARK 470 ILE k 17 CG1 CG2 CD1
REMARK 470 ARG o 27 CG CD NE CZ NH1 NH2
REMARK 470 SER o 35 OG
REMARK 470 GLU o 54 CG CD OE1 OE2
REMARK 470 LYS o 59 CG CD CE NZ
REMARK 470 ARG o 60 CG CD NE CZ NH1 NH2
REMARK 470 GLU o 62 CG CD OE1 OE2
REMARK 470 ARG o 207 CG CD NE CZ NH1 NH2
REMARK 470 ILE t 29 CG1 CG2 CD1
REMARK 470 THR t 30 OG1 CG2
REMARK 470 GLU u 8 CG CD OE1 OE2
REMARK 470 GLU u 23 CG CD OE1 OE2
REMARK 470 LYS v 17 CG CD CE NZ
REMARK 470 LYS v 24 CG CD CE NZ
REMARK 470 LYS v 110 CG CD CE NZ
REMARK 470 VAL y 18 CG1 CG2
REMARK 470 ILE y 19 CG1 CG2 CD1
REMARK 470 ILE y 25 CG1 CG2 CD1
REMARK 470 LYS x 8 CG CD CE NZ
REMARK 470 GLN x 33 CG CD OE1 NE2
REMARK 470 MET z 1 CG SD CE
REMARK 470 THR z 2 OG1 CG2
REMARK 470 ILE z 3 CG1 CG2 CD1
REMARK 470 LEU z 7 CG CD1 CD2
REMARK 470 GLN z 31 CG CD OE1 NE2
REMARK 470 ASP z 32 CG OD1 OD2
REMARK 470 ASP z 34 CG OD1 OD2
REMARK 470 ARG z 35 CG CD NE CZ NH1 NH2
REMARK 470 LEU z 42 CG CD1 CD2
REMARK 470 LEU z 57 CG CD1 CD2
REMARK 470 VAL z 61 CG1 CG2
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 NH2 ARG B 347 O HOH B 701 2.09
REMARK 500 OH TYR V 136 O HOH V 301 2.10
REMARK 500 OE2 GLU c 413 O HOH c 1001 2.11
REMARK 500 OE2 GLU D 343 O HOH D 501 2.11
REMARK 500 O GLY c 148 NZ LYS c 156 2.14
REMARK 500 OE2 GLU O 74 O HOH O 401 2.16
REMARK 500 O PRO c 191 O HOH c 1002 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 278 CE2 TRP A 278 CD2 0.079
REMARK 500 TRP A 317 CE2 TRP A 317 CD2 0.082
REMARK 500 TRP B 5 CE2 TRP B 5 CD2 0.073
REMARK 500 TRP B 56 CE2 TRP B 56 CD2 0.076
REMARK 500 TRP B 78 CE2 TRP B 78 CD2 0.083
REMARK 500 HIS B 114 CG HIS B 114 CD2 0.058
REMARK 500 HIS C 56 CG HIS C 56 CD2 0.059
REMARK 500 HIS C 91 CG HIS C 91 CD2 0.055
REMARK 500 TRP C 387 CE2 TRP C 387 CD2 0.087
REMARK 500 TRP D 58 CE2 TRP D 58 CD2 0.073
REMARK 500 HIS D 87 CG HIS D 87 CD2 0.088
REMARK 500 HIS V 41 CG HIS V 41 CD2 0.055
REMARK 500 HIS a 118 CG HIS a 118 CD2 0.057
REMARK 500 HIS a 195 CG HIS a 195 CD2 0.064
REMARK 500 HIS a 304 CG HIS a 304 CD2 0.057
REMARK 500 HIS a 332 CG HIS a 332 CD2 0.061
REMARK 500 HIS b 26 CG HIS b 26 CD2 0.058
REMARK 500 TRP b 33 CE2 TRP b 33 CD2 0.077
REMARK 500 TRP b 275 CE2 TRP b 275 CD2 0.077
REMARK 500 TRP c 365 CE2 TRP c 365 CD2 0.080
REMARK 500 TRP d 48 CE2 TRP d 48 CD2 0.075
REMARK 500 HIS d 61 CG HIS d 61 CD2 0.055
REMARK 500 TRP d 93 CE2 TRP d 93 CD2 0.073
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 ASP C 473 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG b 57 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG b 57 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 VAL A 30 -84.79 -96.05
REMARK 500 LEU A 159 -55.35 -120.96
REMARK 500 SER A 167 135.67 -170.13
REMARK 500 ARG A 225 108.88 -55.39
REMARK 500 ILE A 259 -99.19 -103.80
REMARK 500 ASP B 49 80.37 -154.54
REMARK 500 MET B 231 -9.48 -59.03
REMARK 500 ASP B 313 47.99 -88.89
REMARK 500 PHE B 383 -82.25 -94.29
REMARK 500 ARG B 505 137.99 -39.38
REMARK 500 THR C 24 94.64 -56.66
REMARK 500 ASP C 107 114.67 -169.68
REMARK 500 ASN C 201 70.85 -116.41
REMARK 500 TRP C 223 -140.43 52.55
REMARK 500 MET C 356 -36.57 -37.74
REMARK 500 SER C 416 -47.27 173.35
REMARK 500 GLU C 464 108.16 -59.43
REMARK 500 ARG D 12 -116.20 139.98
REMARK 500 VAL D 30 -73.01 -116.00
REMARK 500 SER D 65 9.43 -156.68
REMARK 500 LEU D 158 -60.20 -121.97
REMARK 500 ALA D 234 37.69 -81.87
REMARK 500 ASN D 292 16.41 57.64
REMARK 500 PRO D 309 5.25 -64.80
REMARK 500 ALA D 351 -53.00 76.17
REMARK 500 LYS I 33 -120.92 -101.17
REMARK 500 SER J 39 -1.64 70.25
REMARK 500 ALA O 26 83.59 -64.93
REMARK 500 SER O 34 -3.58 -52.49
REMARK 500 ARG O 42 109.20 -162.81
REMARK 500 LYS O 59 34.42 -89.68
REMARK 500 ARG O 73 -164.09 70.13
REMARK 500 THR O 138 1.93 -59.85
REMARK 500 ASN U 29 -37.19 -137.60
REMARK 500 TYR U 103 -139.51 -114.56
REMARK 500 ASN V 49 79.04 -161.18
REMARK 500 ASP V 67 39.42 -83.81
REMARK 500 ASN V 78 71.07 -152.94
REMARK 500 PHE V 101 74.64 -114.71
REMARK 500 GLN Z 31 -94.87 -68.98
REMARK 500 ASP Z 32 95.02 -49.60
REMARK 500 VAL a 30 -84.41 -89.52
REMARK 500 ASN a 76 -169.56 -109.25
REMARK 500 LEU a 159 -53.52 -126.51
REMARK 500 HIS a 190 -7.42 -142.73
REMARK 500 ARG a 225 97.16 -57.98
REMARK 500 GLU a 229 46.05 -77.24
REMARK 500 THR a 230 -42.32 -154.95
REMARK 500 ILE a 259 -91.82 -108.40
REMARK 500 ASP b 49 83.74 -151.60
REMARK 500
REMARK 500 THIS ENTRY HAS 85 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 956 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH H 239 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH J 215 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH O 561 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH b 950 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH b 951 DISTANCE = 7.60 ANGSTROMS
REMARK 525 HOH c1216 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH h 231 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH o 553 DISTANCE = 6.05 ANGSTROMS
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 406
REMARK 610 LMG A 410
REMARK 610 LHG A 412
REMARK 610 SQD A 413
REMARK 610 CLA B 614
REMARK 610 CLA B 615
REMARK 610 CLA B 617
REMARK 610 BCR B 618
REMARK 610 BCR B 619
REMARK 610 LMG B 621
REMARK 610 LMT B 622
REMARK 610 CLA C 513
REMARK 610 DGD C 517
REMARK 610 DGD C 518
REMARK 610 DGD C 519
REMARK 610 LMG C 520
REMARK 610 LHG C 522
REMARK 610 HTG C 523
REMARK 610 LMG C 531
REMARK 610 DGD D 407
REMARK 610 SQD D 408
REMARK 610 LHG D 411
REMARK 610 LMG D 412
REMARK 610 LMT E 101
REMARK 610 DGD H 102
REMARK 610 LMG J 101
REMARK 610 LHG L 101
REMARK 610 LMT T 102
REMARK 610 HTG V 203
REMARK 610 BCR Y 101
REMARK 610 CLA a 409
REMARK 610 SQD a 418
REMARK 610 LHG a 423
REMARK 610 CLA b 614
REMARK 610 CLA b 615
REMARK 610 CLA b 617
REMARK 610 BCR b 618
REMARK 610 BCR b 619
REMARK 610 SQD b 621
REMARK 610 LMG b 622
REMARK 610 DGD c 917
REMARK 610 DGD c 918
REMARK 610 DGD c 919
REMARK 610 LMG c 920
REMARK 610 LMG c 930
REMARK 610 LMT c 931
REMARK 610 LHG d 401
REMARK 610 DGD d 406
REMARK 610 LHG d 408
REMARK 610 LMG d 409
REMARK 610 SQD f 101
REMARK 610 LMT f 102
REMARK 610 DGD h 102
REMARK 610 LMG i 101
REMARK 610 LMG j 101
REMARK 610 LMT t 101
REMARK 610 HTG v 203
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 OEX A 401 MN4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 170 OD1
REMARK 620 2 OEX A 401 O5 105.8
REMARK 620 3 OEX A 401 O4 93.5 87.8
REMARK 620 4 GLU A 333 OE2 168.8 82.9 93.9
REMARK 620 5 HOH A 522 O 81.2 172.9 93.5 90.0
REMARK 620 6 HOH A 591 O 89.8 84.4 172.1 84.0 94.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 401 CA1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 170 OD2
REMARK 620 2 OEX A 401 O1 155.2
REMARK 620 3 OEX A 401 O2 87.8 67.8
REMARK 620 4 OEX A 401 O5 103.4 74.2 72.2
REMARK 620 5 GLU A 189 OE1 146.5 58.3 124.9 82.9
REMARK 620 6 ALA A 344 O 91.6 75.3 67.2 135.9 106.7
REMARK 620 7 HOH A 521 O 96.4 98.4 136.4 146.2 65.9 69.4
REMARK 620 8 HOH A 604 O 79.4 122.8 143.0 77.2 69.9 146.8 79.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 401 MN1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 189 OE2
REMARK 620 2 OEX A 401 O1 89.2
REMARK 620 3 OEX A 401 O5 99.1 79.2
REMARK 620 4 OEX A 401 O3 168.3 99.0 74.5
REMARK 620 5 HIS A 332 NE2 89.2 176.2 97.7 82.1
REMARK 620 6 ASP A 342 OD2 100.9 96.4 159.5 86.5 87.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 A 402 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 215 NE2
REMARK 620 2 HIS A 272 NE2 96.5
REMARK 620 3 BCT A 421 O2 149.0 100.1
REMARK 620 4 BCT A 421 O2 131.1 80.1 30.5
REMARK 620 5 BCT A 421 O3 99.9 92.6 53.6 32.7
REMARK 620 6 BCT A 421 O3 171.7 91.0 31.0 53.7 83.2
REMARK 620 7 HIS D 214 NE2 106.7 85.9 100.4 121.5 153.3 70.2
REMARK 620 8 HIS D 268 NE2 89.8 173.6 74.7 96.6 87.4 82.6 91.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 401 MN3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 333 OE1
REMARK 620 2 OEX A 401 O2 166.7
REMARK 620 3 OEX A 401 O3 75.8 91.1
REMARK 620 4 OEX A 401 O4 96.1 97.1 171.1
REMARK 620 5 OEX A 401 O5 88.7 91.9 82.4 93.8
REMARK 620 6 GLU C 354 OE2 88.9 88.1 86.9 96.9 169.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX A 401 MN2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 342 OD1
REMARK 620 2 OEX A 401 O1 99.0
REMARK 620 3 OEX A 401 O2 171.4 83.5
REMARK 620 4 OEX A 401 O3 96.0 84.5 92.5
REMARK 620 5 ALA A 344 OXT 87.6 98.6 83.8 174.8
REMARK 620 6 GLU C 354 OE1 87.2 172.9 90.9 91.6 84.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA A 406 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 614 O
REMARK 620 2 CLA A 406 NA 91.6
REMARK 620 3 CLA A 406 NB 103.3 84.9
REMARK 620 4 CLA A 406 NC 106.9 159.6 98.7
REMARK 620 5 CLA A 406 ND 97.2 89.8 158.9 79.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA D 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 578 O
REMARK 620 2 CLA D 401 NA 91.5
REMARK 620 3 CLA D 401 NB 101.2 87.9
REMARK 620 4 CLA D 401 NC 109.1 159.2 90.5
REMARK 620 5 CLA D 401 ND 101.4 90.2 157.4 83.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 438 OD1
REMARK 620 2 HOH B 720 O 100.3
REMARK 620 3 HOH B 850 O 154.0 94.7
REMARK 620 4 HOH B 932 O 100.2 150.9 75.0
REMARK 620 5 HOH O 518 O 144.9 74.0 60.0 77.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 705 O
REMARK 620 2 CLA B 602 NA 81.9
REMARK 620 3 CLA B 602 NB 106.5 81.2
REMARK 620 4 CLA B 602 NC 116.3 161.4 96.1
REMARK 620 5 CLA B 602 ND 90.3 90.8 160.0 85.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B 608 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 855 O
REMARK 620 2 CLA B 608 NA 93.4
REMARK 620 3 CLA B 608 NB 106.0 88.9
REMARK 620 4 CLA B 608 NC 102.8 162.8 92.1
REMARK 620 5 CLA B 608 ND 95.5 85.5 158.0 87.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA B 611 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 710 O
REMARK 620 2 CLA B 611 NA 100.4
REMARK 620 3 CLA B 611 NB 90.8 85.8
REMARK 620 4 CLA B 611 NC 96.8 159.0 81.9
REMARK 620 5 CLA B 611 ND 109.6 103.8 155.0 81.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 512 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 39 OD1
REMARK 620 2 CLA C 512 NA 102.8
REMARK 620 3 CLA C 512 NB 102.0 81.0
REMARK 620 4 CLA C 512 NC 104.2 153.0 92.9
REMARK 620 5 CLA C 512 ND 107.0 91.6 150.9 81.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 505 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 722 O
REMARK 620 2 CLA C 505 NA 90.6
REMARK 620 3 CLA C 505 NB 113.8 86.9
REMARK 620 4 CLA C 505 NC 118.3 150.4 86.9
REMARK 620 5 CLA C 505 ND 102.5 85.0 142.8 82.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA C 508 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 607 O
REMARK 620 2 CLA C 508 NA 88.2
REMARK 620 3 CLA C 508 NB 106.4 89.6
REMARK 620 4 CLA C 508 NC 111.4 160.0 88.7
REMARK 620 5 CLA C 508 ND 95.2 90.7 158.4 83.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM E 102 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 23 NE2
REMARK 620 2 HEM E 102 NA 94.8
REMARK 620 3 HEM E 102 NB 90.5 88.9
REMARK 620 4 HEM E 102 NC 87.7 177.4 91.2
REMARK 620 5 HEM E 102 ND 87.6 91.2 178.1 88.8
REMARK 620 6 HIS F 24 NE2 175.9 83.2 93.0 94.3 88.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG J 102 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH F 201 O
REMARK 620 2 GLY J 31 O 157.1
REMARK 620 3 ALA J 34 O 107.9 77.6
REMARK 620 4 LEU J 36 O 92.7 108.7 98.3
REMARK 620 5 LMG J 101 O4 87.5 83.4 160.0 93.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K 102 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP K 19 OD2
REMARK 620 2 ASP K 23 OD2 102.9
REMARK 620 3 HOH K 201 O 69.2 87.2
REMARK 620 4 HOH K 206 O 167.7 75.8 98.5
REMARK 620 5 HOH Y 206 O 99.2 94.0 168.3 93.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA O 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR O 138 O
REMARK 620 2 ASN O 200 OD1 147.9
REMARK 620 3 VAL O 201 O 84.0 74.1
REMARK 620 4 HOH O 459 O 75.4 79.6 85.2
REMARK 620 5 HOH O 533 O 109.9 80.0 147.7 71.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC V 202 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS V 41 NE2
REMARK 620 2 HEC V 202 NA 92.3
REMARK 620 3 HEC V 202 NB 88.1 91.2
REMARK 620 4 HEC V 202 NC 90.1 177.4 87.9
REMARK 620 5 HEC V 202 ND 90.9 90.8 177.8 90.1
REMARK 620 6 HIS V 92 NE2 170.5 97.1 92.0 80.5 88.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 403 CA1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 170 OD1
REMARK 620 2 OEX a 403 O1 144.1
REMARK 620 3 OEX a 403 O2 81.1 63.5
REMARK 620 4 OEX a 403 O5 96.7 80.9 74.8
REMARK 620 5 GLU a 189 OE1 147.3 68.6 131.3 89.6
REMARK 620 6 ALA a 344 O 80.4 75.9 58.7 133.5 117.5
REMARK 620 7 HOH a 506 O 94.0 103.3 129.7 154.7 69.5 71.0
REMARK 620 8 HOH a 599 O 82.8 130.3 145.5 77.0 67.4 146.7 81.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 403 MN4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 170 OD2
REMARK 620 2 OEX a 403 O5 105.6
REMARK 620 3 OEX a 403 O4 98.1 88.4
REMARK 620 4 GLU a 333 OE2 161.5 90.1 91.9
REMARK 620 5 HOH a 544 O 84.9 169.1 87.2 80.1
REMARK 620 6 HOH a 597 O 85.4 86.2 174.2 86.0 97.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 403 MN1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU a 189 OE2
REMARK 620 2 OEX a 403 O1 95.8
REMARK 620 3 OEX a 403 O5 105.2 88.5
REMARK 620 4 OEX a 403 O3 167.5 82.4 62.4
REMARK 620 5 HIS a 332 NE2 93.3 169.8 93.4 89.7
REMARK 620 6 ASP a 342 OD2 93.5 80.7 159.2 98.4 94.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 a 404 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS a 215 NE2
REMARK 620 2 HIS a 272 NE2 93.7
REMARK 620 3 BCT a 422 O2 90.2 90.6
REMARK 620 4 BCT a 422 O3 141.3 94.1 51.9
REMARK 620 5 HIS d 214 NE2 105.3 97.8 161.7 111.1
REMARK 620 6 HIS d 268 NE2 85.8 175.8 85.2 83.9 86.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 403 MN3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU a 333 OE1
REMARK 620 2 OEX a 403 O2 165.5
REMARK 620 3 OEX a 403 O3 83.0 86.2
REMARK 620 4 OEX a 403 O4 94.1 95.2 171.3
REMARK 620 5 OEX a 403 O5 83.6 105.6 88.1 99.7
REMARK 620 6 GLU c 354 OE2 91.5 77.9 84.7 87.2 171.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 OEX a 403 MN2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 342 OD1
REMARK 620 2 OEX a 403 O1 88.5
REMARK 620 3 OEX a 403 O2 159.6 104.2
REMARK 620 4 OEX a 403 O3 109.0 89.1 87.5
REMARK 620 5 ALA a 344 OXT 84.2 90.4 79.8 166.7
REMARK 620 6 GLU c 354 OE1 85.8 174.3 81.1 93.4 88.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA a 408 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH a 567 O
REMARK 620 2 CLA a 408 NA 91.2
REMARK 620 3 CLA a 408 NB 101.7 85.6
REMARK 620 4 CLA a 408 NC 109.2 157.3 80.6
REMARK 620 5 CLA a 408 ND 100.6 95.1 157.7 91.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA a 409 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH a 602 O
REMARK 620 2 CLA a 409 NA 91.8
REMARK 620 3 CLA a 409 NB 106.2 83.1
REMARK 620 4 CLA a 409 NC 110.0 157.8 86.5
REMARK 620 5 CLA a 409 ND 100.1 92.5 153.5 88.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA b 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN b 438 OD1
REMARK 620 2 HOH b 755 O 89.0
REMARK 620 3 HOH b 787 O 93.4 78.4
REMARK 620 4 HOH b 861 O 78.6 78.9 156.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA b 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH b 706 O
REMARK 620 2 CLA b 602 NA 82.5
REMARK 620 3 CLA b 602 NB 108.4 85.9
REMARK 620 4 CLA b 602 NC 115.4 158.8 98.1
REMARK 620 5 CLA b 602 ND 87.0 82.1 159.1 87.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA b 608 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH b 860 O
REMARK 620 2 CLA b 608 NA 96.6
REMARK 620 3 CLA b 608 NB 102.5 88.1
REMARK 620 4 CLA b 608 NC 106.8 156.6 86.9
REMARK 620 5 CLA b 608 ND 100.3 89.8 157.1 86.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA b 611 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH b 737 O
REMARK 620 2 CLA b 611 NA 100.6
REMARK 620 3 CLA b 611 NB 92.5 87.2
REMARK 620 4 CLA b 611 NC 96.3 161.7 85.0
REMARK 620 5 CLA b 611 ND 103.8 99.4 160.8 83.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA c 901 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE c 22 O
REMARK 620 2 THR c 24 O 93.7
REMARK 620 3 ASP c 27 OD1 120.8 99.1
REMARK 620 4 ASP c 27 OD2 74.9 84.4 49.7
REMARK 620 5 SER c 30 OG 158.0 99.1 74.8 124.0
REMARK 620 6 HOH c1158 O 80.0 83.1 158.6 151.1 83.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA c 912 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN c 39 OD1
REMARK 620 2 CLA c 912 NA 100.6
REMARK 620 3 CLA c 912 NB 104.9 85.6
REMARK 620 4 CLA c 912 NC 103.0 156.1 92.0
REMARK 620 5 CLA c 912 ND 101.6 88.0 153.5 83.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA c 905 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH c1166 O
REMARK 620 2 CLA c 905 NA 96.2
REMARK 620 3 CLA c 905 NB 99.5 83.2
REMARK 620 4 CLA c 905 NC 110.8 151.9 84.5
REMARK 620 5 CLA c 905 ND 115.5 89.7 144.9 85.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CLA c 908 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH c1017 O
REMARK 620 2 CLA c 908 NA 83.4
REMARK 620 3 CLA c 908 NB 104.6 87.8
REMARK 620 4 CLA c 908 NC 120.5 154.5 93.7
REMARK 620 5 CLA c 908 ND 96.3 86.2 157.4 82.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM e 101 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS e 23 NE2
REMARK 620 2 HEM e 101 NA 90.6
REMARK 620 3 HEM e 101 NB 85.7 88.7
REMARK 620 4 HEM e 101 NC 90.1 178.6 92.6
REMARK 620 5 HEM e 101 ND 90.7 91.9 176.4 86.8
REMARK 620 6 HIS f 24 NE2 176.4 86.0 95.2 93.3 88.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG j 102 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH f 201 O
REMARK 620 2 GLY j 31 O 156.4
REMARK 620 3 ALA j 34 O 110.3 77.9
REMARK 620 4 LEU j 36 O 97.8 102.8 99.5
REMARK 620 5 LMG j 101 O4 85.6 81.8 158.1 93.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG k 102 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP k 19 OD2
REMARK 620 2 ASP k 23 OD2 98.0
REMARK 620 3 HOH k 201 O 69.3 91.4
REMARK 620 4 HOH k 206 O 162.0 73.1 94.9
REMARK 620 5 HOH k 207 O 104.5 107.9 160.5 93.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA o 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR o 138 O
REMARK 620 2 ASN o 200 OD1 151.3
REMARK 620 3 VAL o 201 O 73.4 85.9
REMARK 620 4 HOH o 416 O 80.9 77.8 85.5
REMARK 620 5 HOH o 441 O 132.8 67.3 94.6 144.9
REMARK 620 6 HOH o 447 O 69.7 136.5 104.8 143.9 69.8
REMARK 620 7 HOH o 489 O 110.0 79.2 151.5 67.7 101.7 102.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC v 202 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS v 41 NE2
REMARK 620 2 HEC v 202 NA 91.2
REMARK 620 3 HEC v 202 NB 82.0 83.7
REMARK 620 4 HEC v 202 NC 87.4 177.7 94.3
REMARK 620 5 HEC v 202 ND 95.4 97.1 177.3 84.8
REMARK 620 6 HIS v 92 NE2 168.8 99.9 97.9 81.5 84.5
REMARK 620 N 1 2 3 4 5
DBREF 5H2F A 11 344 UNP P0A444 PSBA1_THEEB 11 344
DBREF 5H2F B 2 506 UNP Q8DIQ1 PSBB_THEEB 2 506
DBREF 5H2F C 19 473 UNP Q8DIF8 PSBC_THEEB 7 461
DBREF 5H2F D 11 352 UNP Q8CM25 PSBD_THEEB 11 352
DBREF 5H2F E 5 84 UNP Q8DIP0 PSBE_THEEB 5 84
DBREF 5H2F F 13 45 UNP Q8DIN9 PSBF_THEEB 13 45
DBREF 5H2F H 2 64 UNP Q8DJ43 PSBH_THEEB 2 64
DBREF 5H2F I 1 36 UNP Q8DJZ6 PSBI_THEEB 1 36
DBREF 5H2F J 1 40 UNP P59087 PSBJ_THEEB 1 40
DBREF 5H2F K 10 46 UNP Q9F1K9 PSBK_THEEB 10 46
DBREF 5H2F L 3 37 UNP Q8DIN8 PSBL_THEEB 3 37
DBREF 5H2F O 4 246 UNP P0A431 PSBO_THEEB 30 272
DBREF 5H2F T 1 30 UNP Q8DIQ0 PSBT_THEEB 1 30
DBREF 5H2F U 8 104 UNP Q9F1L5 PSBU_THEEB 38 134
DBREF 5H2F V 1 137 UNP P0A386 CY550_THEEB 27 163
DBREF 5H2F Y 18 46 UNP Q8DJI1 YCF12_THEEB 18 46
DBREF 5H2F X 2 38 UNP Q9F1R6 PSBX_THEEB 2 38
DBREF 5H2F Z 1 62 UNP Q8DHJ2 PSBZ_THEEB 1 62
DBREF 5H2F a 11 344 UNP P0A444 PSBA1_THEEB 11 344
DBREF 5H2F b 2 506 UNP Q8DIQ1 PSBB_THEEB 2 506
DBREF 5H2F c 19 473 UNP Q8DIF8 PSBC_THEEB 7 461
DBREF 5H2F d 11 352 UNP Q8CM25 PSBD_THEEB 11 352
DBREF 5H2F e 5 84 UNP Q8DIP0 PSBE_THEEB 5 84
DBREF 5H2F f 13 45 UNP Q8DIN9 PSBF_THEEB 13 45
DBREF 5H2F h 2 64 UNP Q8DJ43 PSBH_THEEB 2 64
DBREF 5H2F i 1 36 UNP Q8DJZ6 PSBI_THEEB 1 36
DBREF 5H2F j 1 40 UNP P59087 PSBJ_THEEB 1 40
DBREF 5H2F k 10 46 UNP Q9F1K9 PSBK_THEEB 10 46
DBREF 5H2F l 3 37 UNP Q8DIN8 PSBL_THEEB 3 37
DBREF 5H2F o 4 246 UNP P0A431 PSBO_THEEB 30 272
DBREF 5H2F t 1 30 UNP Q8DIQ0 PSBT_THEEB 1 30
DBREF 5H2F u 8 104 UNP Q9F1L5 PSBU_THEEB 38 134
DBREF 5H2F v 1 137 UNP P0A386 CY550_THEEB 27 163
DBREF 5H2F y 18 46 UNP Q8DJI1 YCF12_THEEB 18 46
DBREF 5H2F x 2 38 UNP Q9F1R6 PSBX_THEEB 2 38
DBREF 5H2F z 1 62 UNP Q8DHJ2 PSBZ_THEEB 1 62
SEQRES 1 A 334 ALA ASN LEU TRP GLU ARG PHE CYS ASN TRP VAL THR SER
SEQRES 2 A 334 THR ASP ASN ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE
SEQRES 3 A 334 MET ILE PRO THR LEU LEU ALA ALA THR ILE CYS PHE VAL
SEQRES 4 A 334 ILE ALA PHE ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY
SEQRES 5 A 334 ILE ARG GLU PRO VAL SER GLY SER LEU LEU TYR GLY ASN
SEQRES 6 A 334 ASN ILE ILE THR GLY ALA VAL VAL PRO SER SER ASN ALA
SEQRES 7 A 334 ILE GLY LEU HIS PHE TYR PRO ILE TRP GLU ALA ALA SER
SEQRES 8 A 334 LEU ASP GLU TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU
SEQRES 9 A 334 ILE ILE PHE HIS PHE LEU LEU GLY ALA SER CYS TYR MET
SEQRES 10 A 334 GLY ARG GLN TRP GLU LEU SER TYR ARG LEU GLY MET ARG
SEQRES 11 A 334 PRO TRP ILE CYS VAL ALA TYR SER ALA PRO LEU ALA SER
SEQRES 12 A 334 ALA PHE ALA VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY
SEQRES 13 A 334 SER PHE SER ASP GLY MET PRO LEU GLY ILE SER GLY THR
SEQRES 14 A 334 PHE ASN PHE MET ILE VAL PHE GLN ALA GLU HIS ASN ILE
SEQRES 15 A 334 LEU MET HIS PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL
SEQRES 16 A 334 PHE GLY GLY ALA LEU PHE CYS ALA MET HIS GLY SER LEU
SEQRES 17 A 334 VAL THR SER SER LEU ILE ARG GLU THR THR GLU THR GLU
SEQRES 18 A 334 SER ALA ASN TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU
SEQRES 19 A 334 THR TYR ASN ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG
SEQRES 20 A 334 LEU ILE PHE GLN TYR ALA SER PHE ASN ASN SER ARG SER
SEQRES 21 A 334 LEU HIS PHE PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL
SEQRES 22 A 334 TRP PHE THR ALA LEU GLY ILE SER THR MET ALA PHE ASN
SEQRES 23 A 334 LEU ASN GLY PHE ASN PHE ASN HIS SER VAL ILE ASP ALA
SEQRES 24 A 334 LYS GLY ASN VAL ILE ASN THR TRP ALA ASP ILE ILE ASN
SEQRES 25 A 334 ARG ALA ASN LEU GLY MET GLU VAL MET HIS GLU ARG ASN
SEQRES 26 A 334 ALA HIS ASN PHE PRO LEU ASP LEU ALA
SEQRES 1 B 505 GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE ASN
SEQRES 2 B 505 ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS THR
SEQRES 3 B 505 ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU TYR
SEQRES 4 B 505 GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU ASN
SEQRES 5 B 505 PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE MET
SEQRES 6 B 505 ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP SER
SEQRES 7 B 505 ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP SER
SEQRES 8 B 505 PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER GLY
SEQRES 9 B 505 LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR TRP
SEQRES 10 B 505 ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU PRO
SEQRES 11 B 505 ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU PHE
SEQRES 12 B 505 LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE HIS
SEQRES 13 B 505 LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER ASP
SEQRES 14 B 505 PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA PRO
SEQRES 15 B 505 GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO GLY
SEQRES 16 B 505 GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL GLY
SEQRES 17 B 505 ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO PRO
SEQRES 18 B 505 GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE GLU
SEQRES 19 B 505 THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE ALA
SEQRES 20 B 505 ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER ALA
SEQRES 21 B 505 THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR GLN
SEQRES 22 B 505 TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG ARG
SEQRES 23 B 505 VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU GLU
SEQRES 24 B 505 ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR ASP
SEQRES 25 B 505 TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE ARG
SEQRES 26 B 505 THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN ALA
SEQRES 27 B 505 TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY GLU
SEQRES 28 B 505 GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU SER
SEQRES 29 B 505 PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL LYS
SEQRES 30 B 505 ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR SER
SEQRES 31 B 505 PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY GLY
SEQRES 32 B 505 GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR VAL
SEQRES 33 B 505 LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE PHE
SEQRES 34 B 505 GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE PHE
SEQRES 35 B 505 ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS ALA
SEQRES 36 B 505 VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP HIS
SEQRES 37 B 505 GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY ILE
SEQRES 38 B 505 ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY PHE
SEQRES 39 B 505 TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG
SEQRES 1 C 455 ASN SER ILE PHE ALA THR ASN ARG ASP GLN GLU SER SER
SEQRES 2 C 455 GLY PHE ALA TRP TRP ALA GLY ASN ALA ARG LEU ILE ASN
SEQRES 3 C 455 LEU SER GLY LYS LEU LEU GLY ALA HIS VAL ALA HIS ALA
SEQRES 4 C 455 GLY LEU ILE VAL PHE TRP ALA GLY ALA MET THR LEU PHE
SEQRES 5 C 455 GLU LEU ALA HIS PHE ILE PRO GLU LYS PRO MET TYR GLU
SEQRES 6 C 455 GLN GLY LEU ILE LEU ILE PRO HIS ILE ALA THR LEU GLY
SEQRES 7 C 455 TRP GLY VAL GLY PRO GLY GLY GLU VAL VAL ASP THR PHE
SEQRES 8 C 455 PRO PHE PHE VAL VAL GLY VAL VAL HIS LEU ILE SER SER
SEQRES 9 C 455 ALA VAL LEU GLY PHE GLY GLY VAL TYR HIS ALA ILE ARG
SEQRES 10 C 455 GLY PRO GLU THR LEU GLU GLU TYR SER SER PHE PHE GLY
SEQRES 11 C 455 TYR ASP TRP LYS ASP LYS ASN LYS MET THR THR ILE LEU
SEQRES 12 C 455 GLY PHE HIS LEU ILE VAL LEU GLY ILE GLY ALA LEU LEU
SEQRES 13 C 455 LEU VAL ALA LYS ALA MET PHE PHE GLY GLY LEU TYR ASP
SEQRES 14 C 455 THR TRP ALA PRO GLY GLY GLY ASP VAL ARG VAL ILE THR
SEQRES 15 C 455 ASN PRO THR LEU ASP PRO ARG VAL ILE PHE GLY TYR LEU
SEQRES 16 C 455 LEU LYS SER PRO PHE GLY GLY GLU GLY TRP ILE VAL SER
SEQRES 17 C 455 VAL ASN ASN LEU GLU ASP VAL VAL GLY GLY HIS ILE TRP
SEQRES 18 C 455 ILE GLY LEU ILE CYS ILE ALA GLY GLY ILE TRP HIS ILE
SEQRES 19 C 455 LEU THR THR PRO PHE GLY TRP ALA ARG ARG ALA PHE ILE
SEQRES 20 C 455 TRP SER GLY GLU ALA TYR LEU SER TYR SER LEU GLY ALA
SEQRES 21 C 455 LEU SER MET MET GLY PHE ILE ALA THR CYS PHE VAL TRP
SEQRES 22 C 455 PHE ASN ASN THR VAL TYR PRO SER GLU PHE TYR GLY PRO
SEQRES 23 C 455 THR GLY PRO GLU ALA SER GLN ALA GLN ALA MET THR PHE
SEQRES 24 C 455 LEU ILE ARG ASP GLN LYS LEU GLY ALA ASN VAL GLY SER
SEQRES 25 C 455 ALA GLN GLY PRO THR GLY LEU GLY LYS TYR LEU MET ARG
SEQRES 26 C 455 SER PRO THR GLY GLU ILE ILE PHE GLY GLY GLU THR MET
SEQRES 27 C 455 ARG PHE TRP ASP PHE ARG GLY PRO TRP LEU GLU PRO LEU
SEQRES 28 C 455 ARG GLY PRO ASN GLY LEU ASP LEU ASN LYS ILE LYS ASN
SEQRES 29 C 455 ASP ILE GLN PRO TRP GLN GLU ARG ARG ALA ALA GLU TYR
SEQRES 30 C 455 MET THR HIS ALA PRO LEU GLY SER LEU ASN SER VAL GLY
SEQRES 31 C 455 GLY VAL ALA THR GLU ILE ASN SER VAL ASN PHE VAL SER
SEQRES 32 C 455 PRO ARG SER TRP LEU ALA THR SER HIS PHE VAL LEU ALA
SEQRES 33 C 455 PHE PHE PHE LEU VAL GLY HIS LEU TRP HIS ALA GLY ARG
SEQRES 34 C 455 ALA ARG ALA ALA ALA ALA GLY PHE GLU LYS GLY ILE ASP
SEQRES 35 C 455 ARG GLU SER GLU PRO VAL LEU SER MET PRO SER LEU ASP
SEQRES 1 D 342 GLU ARG GLY TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS
SEQRES 2 D 342 ARG ASP ARG PHE VAL PHE VAL GLY TRP SER GLY ILE LEU
SEQRES 3 D 342 LEU PHE PRO CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU
SEQRES 4 D 342 THR GLY THR THR PHE VAL THR SER TRP TYR THR HIS GLY
SEQRES 5 D 342 LEU ALA SER SER TYR LEU GLU GLY CYS ASN PHE LEU THR
SEQRES 6 D 342 VAL ALA VAL SER THR PRO ALA ASN SER MET GLY HIS SER
SEQRES 7 D 342 LEU LEU LEU LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE
SEQRES 8 D 342 THR ARG TRP CYS GLN LEU GLY GLY LEU TRP THR PHE ILE
SEQRES 9 D 342 ALA LEU HIS GLY ALA PHE GLY LEU ILE GLY PHE MET LEU
SEQRES 10 D 342 ARG GLN PHE GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO
SEQRES 11 D 342 TYR ASN ALA ILE ALA PHE SER ALA PRO ILE ALA VAL PHE
SEQRES 12 D 342 VAL SER VAL PHE LEU ILE TYR PRO LEU GLY GLN SER SER
SEQRES 13 D 342 TRP PHE PHE ALA PRO SER PHE GLY VAL ALA ALA ILE PHE
SEQRES 14 D 342 ARG PHE LEU LEU PHE PHE GLN GLY PHE HIS ASN TRP THR
SEQRES 15 D 342 LEU ASN PRO PHE HIS MET MET GLY VAL ALA GLY VAL LEU
SEQRES 16 D 342 GLY GLY ALA LEU LEU CYS ALA ILE HIS GLY ALA THR VAL
SEQRES 17 D 342 GLU ASN THR LEU PHE GLN ASP GLY GLU GLY ALA SER THR
SEQRES 18 D 342 PHE ARG ALA PHE ASN PRO THR GLN ALA GLU GLU THR TYR
SEQRES 19 D 342 SER MET VAL THR ALA ASN ARG PHE TRP SER GLN ILE PHE
SEQRES 20 D 342 GLY ILE ALA PHE SER ASN LYS ARG TRP LEU HIS PHE PHE
SEQRES 21 D 342 MET LEU PHE VAL PRO VAL THR GLY LEU TRP MET SER ALA
SEQRES 22 D 342 ILE GLY VAL VAL GLY LEU ALA LEU ASN LEU ARG SER TYR
SEQRES 23 D 342 ASP PHE ILE SER GLN GLU ILE ARG ALA ALA GLU ASP PRO
SEQRES 24 D 342 GLU PHE GLU THR PHE TYR THR LYS ASN LEU LEU LEU ASN
SEQRES 25 D 342 GLU GLY ILE ARG ALA TRP MET ALA PRO GLN ASP GLN PRO
SEQRES 26 D 342 HIS GLU ASN PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG
SEQRES 27 D 342 GLY ASN ALA LEU
SEQRES 1 E 80 THR GLY GLU ARG PRO PHE SER ASP ILE ILE THR SER VAL
SEQRES 2 E 80 ARG TYR TRP VAL ILE HIS SER ILE THR ILE PRO ALA LEU
SEQRES 3 E 80 PHE ILE ALA GLY TRP LEU PHE VAL SER THR GLY LEU ALA
SEQRES 4 E 80 TYR ASP VAL PHE GLY THR PRO ARG PRO ASP SER TYR TYR
SEQRES 5 E 80 ALA GLN GLU GLN ARG SER ILE PRO LEU VAL THR ASP ARG
SEQRES 6 E 80 PHE GLU ALA LYS GLN GLN VAL GLU THR PHE LEU GLU GLN
SEQRES 7 E 80 LEU LYS
SEQRES 1 F 33 TYR PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR
SEQRES 2 F 33 LEU ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA
SEQRES 3 F 33 ALA MET GLN PHE ILE GLN ARG
SEQRES 1 H 63 ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU
SEQRES 2 H 63 ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR
SEQRES 3 H 63 THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL
SEQRES 4 H 63 PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU
SEQRES 5 H 63 ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA
SEQRES 1 I 36 FME GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR
SEQRES 2 I 36 PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY
SEQRES 3 I 36 ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP
SEQRES 1 J 40 MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL
SEQRES 2 J 40 ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY
SEQRES 3 J 40 LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER
SEQRES 4 J 40 LEU
SEQRES 1 K 37 LYS LEU PRO GLU ALA TYR ALA ILE PHE ASP PRO LEU VAL
SEQRES 2 K 37 ASP VAL LEU PRO VAL ILE PRO VAL LEU PHE LEU ALA LEU
SEQRES 3 K 37 ALA PHE VAL TRP GLN ALA ALA VAL GLY PHE ARG
SEQRES 1 L 35 PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN ARG THR
SEQRES 2 L 35 SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL LEU ALA
SEQRES 3 L 35 LEU LEU PHE SER SER TYR PHE PHE ASN
SEQRES 1 O 243 THR LEU THR TYR ASP ASP ILE VAL GLY THR GLY LEU ALA
SEQRES 2 O 243 ASN LYS CYS PRO THR LEU ASP ASP THR ALA ARG GLY ALA
SEQRES 3 O 243 TYR PRO ILE ASP SER SER GLN THR TYR ARG ILE ALA ARG
SEQRES 4 O 243 LEU CYS LEU GLN PRO THR THR PHE LEU VAL LYS GLU GLU
SEQRES 5 O 243 PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE VAL PRO THR
SEQRES 6 O 243 LYS LEU VAL THR ARG GLU THR THR SER LEU ASP GLN ILE
SEQRES 7 O 243 GLN GLY GLU LEU LYS VAL ASN SER ASP GLY SER LEU THR
SEQRES 8 O 243 PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN PRO VAL THR
SEQRES 9 O 243 VAL GLN MET ALA GLY GLY GLU ARG ILE PRO LEU LEU PHE
SEQRES 10 O 243 THR VAL LYS ASN LEU VAL ALA SER THR GLN PRO ASN VAL
SEQRES 11 O 243 THR SER ILE THR THR SER THR ASP PHE LYS GLY GLU PHE
SEQRES 12 O 243 ASN VAL PRO SER TYR ARG THR ALA ASN PHE LEU ASP PRO
SEQRES 13 O 243 LYS GLY ARG GLY LEU ALA SER GLY TYR ASP SER ALA ILE
SEQRES 14 O 243 ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU ALA ARG ALA
SEQRES 15 O 243 ASN VAL LYS ARG PHE SER LEU THR LYS GLY GLN ILE SER
SEQRES 16 O 243 LEU ASN VAL ALA LYS VAL ASP GLY ARG THR GLY GLU ILE
SEQRES 17 O 243 ALA GLY THR PHE GLU SER GLU GLN LEU SER ASP ASP ASP
SEQRES 18 O 243 MET GLY ALA HIS GLU PRO HIS GLU VAL LYS ILE GLN GLY
SEQRES 19 O 243 VAL PHE TYR ALA SER ILE GLU PRO ALA
SEQRES 1 T 30 FME GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE
SEQRES 2 T 30 ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO
SEQRES 3 T 30 PRO ARG ILE THR
SEQRES 1 U 97 GLU LEU VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA
SEQRES 2 U 97 TYR GLY GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA
SEQRES 3 U 97 ALA PHE ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA
SEQRES 4 U 97 LYS LEU ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU
SEQRES 5 U 97 ASP VAL LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS
SEQRES 6 U 97 GLN ILE LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR
SEQRES 7 U 97 GLU VAL GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR
SEQRES 8 U 97 ASN ASN GLY LEU TYR LYS
SEQRES 1 V 137 ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN
SEQRES 2 V 137 SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR
SEQRES 3 V 137 LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER
SEQRES 4 V 137 CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU
SEQRES 5 V 137 ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO
SEQRES 6 V 137 ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN
SEQRES 7 V 137 PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL
SEQRES 8 V 137 HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET
SEQRES 9 V 137 ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY
SEQRES 10 V 137 HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP
SEQRES 11 V 137 GLY GLY GLY LYS VAL TYR TYR
SEQRES 1 Y 29 VAL ILE ALA GLN LEU THR MET ILE ALA MET ILE GLY ILE
SEQRES 2 Y 29 ALA GLY PRO MET ILE ILE PHE LEU LEU ALA VAL ARG ARG
SEQRES 3 Y 29 GLY ASN LEU
SEQRES 1 X 37 THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU
SEQRES 2 X 37 LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL
SEQRES 3 X 37 LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN
SEQRES 1 Z 62 MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL
SEQRES 2 Z 62 ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA
SEQRES 3 Z 62 TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU
SEQRES 4 Z 62 ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU
SEQRES 5 Z 62 VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL
SEQRES 1 a 334 ALA ASN LEU TRP GLU ARG PHE CYS ASN TRP VAL THR SER
SEQRES 2 a 334 THR ASP ASN ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE
SEQRES 3 a 334 MET ILE PRO THR LEU LEU ALA ALA THR ILE CYS PHE VAL
SEQRES 4 a 334 ILE ALA PHE ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY
SEQRES 5 a 334 ILE ARG GLU PRO VAL SER GLY SER LEU LEU TYR GLY ASN
SEQRES 6 a 334 ASN ILE ILE THR GLY ALA VAL VAL PRO SER SER ASN ALA
SEQRES 7 a 334 ILE GLY LEU HIS PHE TYR PRO ILE TRP GLU ALA ALA SER
SEQRES 8 a 334 LEU ASP GLU TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU
SEQRES 9 a 334 ILE ILE PHE HIS PHE LEU LEU GLY ALA SER CYS TYR MET
SEQRES 10 a 334 GLY ARG GLN TRP GLU LEU SER TYR ARG LEU GLY MET ARG
SEQRES 11 a 334 PRO TRP ILE CYS VAL ALA TYR SER ALA PRO LEU ALA SER
SEQRES 12 a 334 ALA PHE ALA VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY
SEQRES 13 a 334 SER PHE SER ASP GLY MET PRO LEU GLY ILE SER GLY THR
SEQRES 14 a 334 PHE ASN PHE MET ILE VAL PHE GLN ALA GLU HIS ASN ILE
SEQRES 15 a 334 LEU MET HIS PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL
SEQRES 16 a 334 PHE GLY GLY ALA LEU PHE CYS ALA MET HIS GLY SER LEU
SEQRES 17 a 334 VAL THR SER SER LEU ILE ARG GLU THR THR GLU THR GLU
SEQRES 18 a 334 SER ALA ASN TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU
SEQRES 19 a 334 THR TYR ASN ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG
SEQRES 20 a 334 LEU ILE PHE GLN TYR ALA SER PHE ASN ASN SER ARG SER
SEQRES 21 a 334 LEU HIS PHE PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL
SEQRES 22 a 334 TRP PHE THR ALA LEU GLY ILE SER THR MET ALA PHE ASN
SEQRES 23 a 334 LEU ASN GLY PHE ASN PHE ASN HIS SER VAL ILE ASP ALA
SEQRES 24 a 334 LYS GLY ASN VAL ILE ASN THR TRP ALA ASP ILE ILE ASN
SEQRES 25 a 334 ARG ALA ASN LEU GLY MET GLU VAL MET HIS GLU ARG ASN
SEQRES 26 a 334 ALA HIS ASN PHE PRO LEU ASP LEU ALA
SEQRES 1 b 505 GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE ASN
SEQRES 2 b 505 ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS THR
SEQRES 3 b 505 ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU TYR
SEQRES 4 b 505 GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU ASN
SEQRES 5 b 505 PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE MET
SEQRES 6 b 505 ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP SER
SEQRES 7 b 505 ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP SER
SEQRES 8 b 505 PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER GLY
SEQRES 9 b 505 LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR TRP
SEQRES 10 b 505 ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU PRO
SEQRES 11 b 505 ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU PHE
SEQRES 12 b 505 LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE HIS
SEQRES 13 b 505 LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER ASP
SEQRES 14 b 505 PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA PRO
SEQRES 15 b 505 GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO GLY
SEQRES 16 b 505 GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL GLY
SEQRES 17 b 505 ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO PRO
SEQRES 18 b 505 GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE GLU
SEQRES 19 b 505 THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE ALA
SEQRES 20 b 505 ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER ALA
SEQRES 21 b 505 THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR GLN
SEQRES 22 b 505 TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG ARG
SEQRES 23 b 505 VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU GLU
SEQRES 24 b 505 ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR ASP
SEQRES 25 b 505 TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE ARG
SEQRES 26 b 505 THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN ALA
SEQRES 27 b 505 TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY GLU
SEQRES 28 b 505 GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU SER
SEQRES 29 b 505 PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL LYS
SEQRES 30 b 505 ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR SER
SEQRES 31 b 505 PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY GLY
SEQRES 32 b 505 GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR VAL
SEQRES 33 b 505 LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE PHE
SEQRES 34 b 505 GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE PHE
SEQRES 35 b 505 ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS ALA
SEQRES 36 b 505 VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP HIS
SEQRES 37 b 505 GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY ILE
SEQRES 38 b 505 ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY PHE
SEQRES 39 b 505 TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG
SEQRES 1 c 455 ASN SER ILE PHE ALA THR ASN ARG ASP GLN GLU SER SER
SEQRES 2 c 455 GLY PHE ALA TRP TRP ALA GLY ASN ALA ARG LEU ILE ASN
SEQRES 3 c 455 LEU SER GLY LYS LEU LEU GLY ALA HIS VAL ALA HIS ALA
SEQRES 4 c 455 GLY LEU ILE VAL PHE TRP ALA GLY ALA MET THR LEU PHE
SEQRES 5 c 455 GLU LEU ALA HIS PHE ILE PRO GLU LYS PRO MET TYR GLU
SEQRES 6 c 455 GLN GLY LEU ILE LEU ILE PRO HIS ILE ALA THR LEU GLY
SEQRES 7 c 455 TRP GLY VAL GLY PRO GLY GLY GLU VAL VAL ASP THR PHE
SEQRES 8 c 455 PRO PHE PHE VAL VAL GLY VAL VAL HIS LEU ILE SER SER
SEQRES 9 c 455 ALA VAL LEU GLY PHE GLY GLY VAL TYR HIS ALA ILE ARG
SEQRES 10 c 455 GLY PRO GLU THR LEU GLU GLU TYR SER SER PHE PHE GLY
SEQRES 11 c 455 TYR ASP TRP LYS ASP LYS ASN LYS MET THR THR ILE LEU
SEQRES 12 c 455 GLY PHE HIS LEU ILE VAL LEU GLY ILE GLY ALA LEU LEU
SEQRES 13 c 455 LEU VAL ALA LYS ALA MET PHE PHE GLY GLY LEU TYR ASP
SEQRES 14 c 455 THR TRP ALA PRO GLY GLY GLY ASP VAL ARG VAL ILE THR
SEQRES 15 c 455 ASN PRO THR LEU ASP PRO ARG VAL ILE PHE GLY TYR LEU
SEQRES 16 c 455 LEU LYS SER PRO PHE GLY GLY GLU GLY TRP ILE VAL SER
SEQRES 17 c 455 VAL ASN ASN LEU GLU ASP VAL VAL GLY GLY HIS ILE TRP
SEQRES 18 c 455 ILE GLY LEU ILE CYS ILE ALA GLY GLY ILE TRP HIS ILE
SEQRES 19 c 455 LEU THR THR PRO PHE GLY TRP ALA ARG ARG ALA PHE ILE
SEQRES 20 c 455 TRP SER GLY GLU ALA TYR LEU SER TYR SER LEU GLY ALA
SEQRES 21 c 455 LEU SER MET MET GLY PHE ILE ALA THR CYS PHE VAL TRP
SEQRES 22 c 455 PHE ASN ASN THR VAL TYR PRO SER GLU PHE TYR GLY PRO
SEQRES 23 c 455 THR GLY PRO GLU ALA SER GLN ALA GLN ALA MET THR PHE
SEQRES 24 c 455 LEU ILE ARG ASP GLN LYS LEU GLY ALA ASN VAL GLY SER
SEQRES 25 c 455 ALA GLN GLY PRO THR GLY LEU GLY LYS TYR LEU MET ARG
SEQRES 26 c 455 SER PRO THR GLY GLU ILE ILE PHE GLY GLY GLU THR MET
SEQRES 27 c 455 ARG PHE TRP ASP PHE ARG GLY PRO TRP LEU GLU PRO LEU
SEQRES 28 c 455 ARG GLY PRO ASN GLY LEU ASP LEU ASN LYS ILE LYS ASN
SEQRES 29 c 455 ASP ILE GLN PRO TRP GLN GLU ARG ARG ALA ALA GLU TYR
SEQRES 30 c 455 MET THR HIS ALA PRO LEU GLY SER LEU ASN SER VAL GLY
SEQRES 31 c 455 GLY VAL ALA THR GLU ILE ASN SER VAL ASN PHE VAL SER
SEQRES 32 c 455 PRO ARG SER TRP LEU ALA THR SER HIS PHE VAL LEU ALA
SEQRES 33 c 455 PHE PHE PHE LEU VAL GLY HIS LEU TRP HIS ALA GLY ARG
SEQRES 34 c 455 ALA ARG ALA ALA ALA ALA GLY PHE GLU LYS GLY ILE ASP
SEQRES 35 c 455 ARG GLU SER GLU PRO VAL LEU SER MET PRO SER LEU ASP
SEQRES 1 d 342 GLU ARG GLY TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS
SEQRES 2 d 342 ARG ASP ARG PHE VAL PHE VAL GLY TRP SER GLY ILE LEU
SEQRES 3 d 342 LEU PHE PRO CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU
SEQRES 4 d 342 THR GLY THR THR PHE VAL THR SER TRP TYR THR HIS GLY
SEQRES 5 d 342 LEU ALA SER SER TYR LEU GLU GLY CYS ASN PHE LEU THR
SEQRES 6 d 342 VAL ALA VAL SER THR PRO ALA ASN SER MET GLY HIS SER
SEQRES 7 d 342 LEU LEU LEU LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE
SEQRES 8 d 342 THR ARG TRP CYS GLN LEU GLY GLY LEU TRP THR PHE ILE
SEQRES 9 d 342 ALA LEU HIS GLY ALA PHE GLY LEU ILE GLY PHE MET LEU
SEQRES 10 d 342 ARG GLN PHE GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO
SEQRES 11 d 342 TYR ASN ALA ILE ALA PHE SER ALA PRO ILE ALA VAL PHE
SEQRES 12 d 342 VAL SER VAL PHE LEU ILE TYR PRO LEU GLY GLN SER SER
SEQRES 13 d 342 TRP PHE PHE ALA PRO SER PHE GLY VAL ALA ALA ILE PHE
SEQRES 14 d 342 ARG PHE LEU LEU PHE PHE GLN GLY PHE HIS ASN TRP THR
SEQRES 15 d 342 LEU ASN PRO PHE HIS MET MET GLY VAL ALA GLY VAL LEU
SEQRES 16 d 342 GLY GLY ALA LEU LEU CYS ALA ILE HIS GLY ALA THR VAL
SEQRES 17 d 342 GLU ASN THR LEU PHE GLN ASP GLY GLU GLY ALA SER THR
SEQRES 18 d 342 PHE ARG ALA PHE ASN PRO THR GLN ALA GLU GLU THR TYR
SEQRES 19 d 342 SER MET VAL THR ALA ASN ARG PHE TRP SER GLN ILE PHE
SEQRES 20 d 342 GLY ILE ALA PHE SER ASN LYS ARG TRP LEU HIS PHE PHE
SEQRES 21 d 342 MET LEU PHE VAL PRO VAL THR GLY LEU TRP MET SER ALA
SEQRES 22 d 342 ILE GLY VAL VAL GLY LEU ALA LEU ASN LEU ARG SER TYR
SEQRES 23 d 342 ASP PHE ILE SER GLN GLU ILE ARG ALA ALA GLU ASP PRO
SEQRES 24 d 342 GLU PHE GLU THR PHE TYR THR LYS ASN LEU LEU LEU ASN
SEQRES 25 d 342 GLU GLY ILE ARG ALA TRP MET ALA PRO GLN ASP GLN PRO
SEQRES 26 d 342 HIS GLU ASN PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG
SEQRES 27 d 342 GLY ASN ALA LEU
SEQRES 1 e 80 THR GLY GLU ARG PRO PHE SER ASP ILE ILE THR SER VAL
SEQRES 2 e 80 ARG TYR TRP VAL ILE HIS SER ILE THR ILE PRO ALA LEU
SEQRES 3 e 80 PHE ILE ALA GLY TRP LEU PHE VAL SER THR GLY LEU ALA
SEQRES 4 e 80 TYR ASP VAL PHE GLY THR PRO ARG PRO ASP SER TYR TYR
SEQRES 5 e 80 ALA GLN GLU GLN ARG SER ILE PRO LEU VAL THR ASP ARG
SEQRES 6 e 80 PHE GLU ALA LYS GLN GLN VAL GLU THR PHE LEU GLU GLN
SEQRES 7 e 80 LEU LYS
SEQRES 1 f 33 TYR PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR
SEQRES 2 f 33 LEU ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA
SEQRES 3 f 33 ALA MET GLN PHE ILE GLN ARG
SEQRES 1 h 63 ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU
SEQRES 2 h 63 ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR
SEQRES 3 h 63 THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL
SEQRES 4 h 63 PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU
SEQRES 5 h 63 ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA
SEQRES 1 i 36 FME GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR
SEQRES 2 i 36 PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY
SEQRES 3 i 36 ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP
SEQRES 1 j 40 MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL
SEQRES 2 j 40 ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY
SEQRES 3 j 40 LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER
SEQRES 4 j 40 LEU
SEQRES 1 k 37 LYS LEU PRO GLU ALA TYR ALA ILE PHE ASP PRO LEU VAL
SEQRES 2 k 37 ASP VAL LEU PRO VAL ILE PRO VAL LEU PHE LEU ALA LEU
SEQRES 3 k 37 ALA PHE VAL TRP GLN ALA ALA VAL GLY PHE ARG
SEQRES 1 l 35 PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN ARG THR
SEQRES 2 l 35 SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL LEU ALA
SEQRES 3 l 35 LEU LEU PHE SER SER TYR PHE PHE ASN
SEQRES 1 o 243 THR LEU THR TYR ASP ASP ILE VAL GLY THR GLY LEU ALA
SEQRES 2 o 243 ASN LYS CYS PRO THR LEU ASP ASP THR ALA ARG GLY ALA
SEQRES 3 o 243 TYR PRO ILE ASP SER SER GLN THR TYR ARG ILE ALA ARG
SEQRES 4 o 243 LEU CYS LEU GLN PRO THR THR PHE LEU VAL LYS GLU GLU
SEQRES 5 o 243 PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE VAL PRO THR
SEQRES 6 o 243 LYS LEU VAL THR ARG GLU THR THR SER LEU ASP GLN ILE
SEQRES 7 o 243 GLN GLY GLU LEU LYS VAL ASN SER ASP GLY SER LEU THR
SEQRES 8 o 243 PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN PRO VAL THR
SEQRES 9 o 243 VAL GLN MET ALA GLY GLY GLU ARG ILE PRO LEU LEU PHE
SEQRES 10 o 243 THR VAL LYS ASN LEU VAL ALA SER THR GLN PRO ASN VAL
SEQRES 11 o 243 THR SER ILE THR THR SER THR ASP PHE LYS GLY GLU PHE
SEQRES 12 o 243 ASN VAL PRO SER TYR ARG THR ALA ASN PHE LEU ASP PRO
SEQRES 13 o 243 LYS GLY ARG GLY LEU ALA SER GLY TYR ASP SER ALA ILE
SEQRES 14 o 243 ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU ALA ARG ALA
SEQRES 15 o 243 ASN VAL LYS ARG PHE SER LEU THR LYS GLY GLN ILE SER
SEQRES 16 o 243 LEU ASN VAL ALA LYS VAL ASP GLY ARG THR GLY GLU ILE
SEQRES 17 o 243 ALA GLY THR PHE GLU SER GLU GLN LEU SER ASP ASP ASP
SEQRES 18 o 243 MET GLY ALA HIS GLU PRO HIS GLU VAL LYS ILE GLN GLY
SEQRES 19 o 243 VAL PHE TYR ALA SER ILE GLU PRO ALA
SEQRES 1 t 30 FME GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE
SEQRES 2 t 30 ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO
SEQRES 3 t 30 PRO ARG ILE THR
SEQRES 1 u 97 GLU LEU VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA
SEQRES 2 u 97 TYR GLY GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA
SEQRES 3 u 97 ALA PHE ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA
SEQRES 4 u 97 LYS LEU ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU
SEQRES 5 u 97 ASP VAL LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS
SEQRES 6 u 97 GLN ILE LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR
SEQRES 7 u 97 GLU VAL GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR
SEQRES 8 u 97 ASN ASN GLY LEU TYR LYS
SEQRES 1 v 137 ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN
SEQRES 2 v 137 SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR
SEQRES 3 v 137 LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER
SEQRES 4 v 137 CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU
SEQRES 5 v 137 ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO
SEQRES 6 v 137 ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN
SEQRES 7 v 137 PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL
SEQRES 8 v 137 HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET
SEQRES 9 v 137 ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY
SEQRES 10 v 137 HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP
SEQRES 11 v 137 GLY GLY GLY LYS VAL TYR TYR
SEQRES 1 y 29 VAL ILE ALA GLN LEU THR MET ILE ALA MET ILE GLY ILE
SEQRES 2 y 29 ALA GLY PRO MET ILE ILE PHE LEU LEU ALA VAL ARG ARG
SEQRES 3 y 29 GLY ASN LEU
SEQRES 1 x 37 THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU
SEQRES 2 x 37 LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL
SEQRES 3 x 37 LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN
SEQRES 1 z 62 MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL
SEQRES 2 z 62 ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA
SEQRES 3 z 62 TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU
SEQRES 4 z 62 ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU
SEQRES 5 z 62 VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL
MODRES 5H2F FME I 1 MET MODIFIED RESIDUE
MODRES 5H2F FME T 1 MET MODIFIED RESIDUE
MODRES 5H2F FME i 1 MET MODIFIED RESIDUE
MODRES 5H2F FME t 1 MET MODIFIED RESIDUE
HET FME I 1 10
HET FME T 1 10
HET FME i 1 10
HET FME t 1 10
HET OEX A 401 10
HET FE2 A 402 1
HET CL A 403 1
HET CL A 404 1
HET CLA A 405 65
HET CLA A 406 55
HET PHO A 407 64
HET CLA A 408 65
HET BCR A 409 40
HET LMG A 410 51
HET PL9 A 411 55
HET LHG A 412 31
HET SQD A 413 49
HET LMT A 414 35
HET UNL A 415 5
HET DMS A 416 4
HET DMS A 417 4
HET DMS A 418 4
HET DMS A 419 4
HET DMS A 420 4
HET BCT A 421 8
HET CA B 601 1
HET CLA B 602 65
HET CLA B 603 65
HET CLA B 604 65
HET CLA B 605 65
HET CLA B 606 65
HET CLA B 607 65
HET CLA B 608 65
HET CLA B 609 65
HET CLA B 610 65
HET CLA B 611 65
HET CLA B 612 65
HET CLA B 613 65
HET CLA B 614 61
HET CLA B 615 53
HET CLA B 616 65
HET CLA B 617 55
HET BCR B 618 19
HET BCR B 619 30
HET BCR B 620 40
HET LMG B 621 40
HET LMT B 622 24
HET HTG B 623 19
HET UNL B 624 7
HET UNL B 625 16
HET HTG B 626 19
HET HTG B 627 19
HET DMS B 628 4
HET DMS B 629 4
HET DMS B 630 4
HET DMS B 631 4
HET DMS B 632 4
HET DMS B 633 4
HET DMS B 634 4
HET DMS B 635 4
HET DMS B 636 4
HET DMS B 637 4
HET DMS B 638 4
HET DMS B 639 4
HET DMS B 640 4
HET DMS B 641 4
HET DMS B 642 4
HET SQD C 501 54
HET CLA C 502 65
HET CLA C 503 65
HET CLA C 504 65
HET CLA C 505 65
HET CLA C 506 65
HET CLA C 507 65
HET CLA C 508 65
HET CLA C 509 65
HET CLA C 510 65
HET CLA C 511 65
HET CLA C 512 65
HET CLA C 513 56
HET CLA C 514 65
HET BCR C 515 40
HET BCR C 516 40
HET DGD C 517 62
HET DGD C 518 62
HET DGD C 519 62
HET LMG C 520 51
HET HTG C 521 19
HET LHG C 522 30
HET HTG C 523 9
HET DMS C 524 4
HET DMS C 525 4
HET DMS C 526 4
HET DMS C 527 4
HET DMS C 528 4
HET DMS C 529 4
HET DMS C 530 4
HET LMG C 531 40
HET HTG C 532 19
HET DMS C 533 4
HET DMS C 534 4
HET DMS C 535 4
HET DMS C 536 4
HET DMS C 537 4
HET DMS C 538 4
HET DMS C 539 4
HET DMS C 540 4
HET CLA D 401 65
HET PHO D 402 64
HET CLA D 403 65
HET CLA D 404 65
HET BCR D 405 40
HET PL9 D 406 55
HET DGD D 407 50
HET SQD D 408 20
HET LHG D 409 49
HET LHG D 410 49
HET LHG D 411 45
HET LMG D 412 46
HET UNL D 413 16
HET HTG D 414 19
HET HTG D 415 19
HET DMS D 416 4
HET DMS D 417 4
HET DMS D 418 4
HET LMT E 101 24
HET HEM E 102 43
HET DMS F 101 4
HET RRX H 101 41
HET DGD H 102 62
HET DMS H 103 4
HET DMS I 101 4
HET LMT I 102 35
HET UNL I 103 13
HET UNL I 104 16
HET UNL I 105 16
HET DMS I 106 4
HET LMG J 101 45
HET MG J 102 1
HET UNL J 103 16
HET BCR K 101 40
HET MG K 102 1
HET LHG L 101 40
HET DMS L 102 4
HET UNL O 301 16
HET CA O 302 1
HET DMS O 303 4
HET DMS O 304 4
HET DMS O 305 4
HET DMS O 306 4
HET DMS O 307 4
HET DMS O 308 4
HET DMS O 309 4
HET DMS O 310 4
HET DMS O 311 4
HET DMS O 312 4
HET DMS O 313 4
HET DMS O 314 4
HET UNL T 101 13
HET LMT T 102 24
HET UNL U 201 14
HET DMS U 202 4
HET DMS U 203 4
HET DMS V 201 4
HET HEC V 202 43
HET HTG V 203 14
HET DMS V 204 4
HET DMS V 205 4
HET DMS V 206 4
HET DMS V 207 4
HET DMS V 208 4
HET DMS V 209 4
HET DMS V 210 4
HET DMS V 211 4
HET DMS V 212 4
HET BCR Y 101 39
HET UNL X 101 16
HET LMT Z 101 35
HET UNL Z 102 9
HET DMS a 401 4
HET DMS a 402 4
HET OEX a 403 10
HET FE2 a 404 1
HET CL a 405 1
HET CL a 406 1
HET CLA a 407 65
HET CLA a 408 65
HET CLA a 409 61
HET PHO a 410 64
HET PHO a 411 64
HET CLA a 412 65
HET BCR a 413 40
HET SQD a 414 54
HET PL9 a 415 55
HET LHG a 416 49
HET UNL a 417 10
HET SQD a 418 51
HET LMT a 419 35
HET UNL a 420 6
HET DMS a 421 4
HET BCT a 422 4
HET LHG a 423 45
HET DMS a 424 4
HET DMS a 425 4
HET CA b 601 1
HET CLA b 602 65
HET CLA b 603 65
HET CLA b 604 65
HET CLA b 605 65
HET CLA b 606 65
HET CLA b 607 65
HET CLA b 608 65
HET CLA b 609 65
HET CLA b 610 65
HET CLA b 611 65
HET CLA b 612 65
HET CLA b 613 65
HET CLA b 614 59
HET CLA b 615 52
HET CLA b 616 65
HET CLA b 617 60
HET BCR b 618 20
HET BCR b 619 31
HET BCR b 620 40
HET SQD b 621 38
HET LMG b 622 43
HET HTG b 623 19
HET HTG b 624 19
HET UNL b 625 16
HET HTG b 626 19
HET HTG b 627 19
HET UNL b 628 11
HET DMS b 629 4
HET DMS b 630 4
HET DMS b 631 4
HET HTG b 632 19
HET DMS b 633 4
HET DMS b 634 4
HET DMS b 635 4
HET DMS b 636 4
HET DMS b 637 4
HET DMS b 638 4
HET CA c 901 1
HET CLA c 902 65
HET CLA c 903 65
HET CLA c 904 65
HET CLA c 905 65
HET CLA c 906 65
HET CLA c 907 65
HET CLA c 908 65
HET CLA c 909 65
HET CLA c 910 65
HET CLA c 911 65
HET CLA c 912 65
HET CLA c 913 65
HET CLA c 914 65
HET BCR c 915 40
HET BCR c 916 40
HET DGD c 917 62
HET DGD c 918 62
HET DGD c 919 62
HET LMG c 920 51
HET LMT c 921 35
HET HTG c 922 19
HET DMS c 923 4
HET DMS c 924 4
HET DMS c 925 4
HET DMS c 926 4
HET DMS c 927 4
HET DMS c 928 4
HET DMS c 929 4
HET LMG c 930 49
HET LMT c 931 24
HET UNL c 932 10
HET DMS c 933 4
HET DMS c 934 4
HET DMS c 935 4
HET DMS c 936 4
HET DMS c 937 4
HET DMS c 938 4
HET DMS c 939 4
HET DMS c 940 4
HET DMS c 941 4
HET DMS c 942 4
HET DMS c 943 4
HET DMS c 944 4
HET LHG d 401 33
HET CLA d 402 65
HET CLA d 403 65
HET BCR d 404 40
HET PL9 d 405 55
HET DGD d 406 43
HET LHG d 407 49
HET LHG d 408 46
HET LMG d 409 47
HET UNL d 410 16
HET DMS d 411 4
HET DMS d 412 4
HET DMS d 413 4
HET DMS d 414 4
HET DMS d 415 4
HET HEM e 101 43
HET SQD f 101 14
HET LMT f 102 25
HET DMS f 103 4
HET RRX h 101 41
HET DGD h 102 62
HET LMG i 101 51
HET UNL i 102 16
HET UNL i 103 16
HET UNL i 104 16
HET UNL i 105 10
HET DMS i 106 4
HET LMG j 101 47
HET MG j 102 1
HET UNL j 103 16
HET BCR k 101 40
HET MG k 102 1
HET SQD l 101 54
HET LHG l 102 49
HET DMS l 103 4
HET DMS l 104 4
HET DMS l 105 4
HET HTG l 106 19
HET CA o 301 1
HET DMS o 302 4
HET DMS o 303 4
HET DMS o 304 4
HET DMS o 305 4
HET DMS o 306 4
HET DMS o 307 4
HET DMS o 308 4
HET LMT t 101 24
HET UNL t 102 16
HET DMS t 103 4
HET DMS t 104 4
HET DMS t 105 4
HET UNL u 201 11
HET DMS u 202 4
HET DMS u 203 4
HET DMS u 204 4
HET DMS u 205 4
HET DMS v 201 4
HET HEC v 202 43
HET HTG v 203 16
HET DMS v 204 4
HET DMS v 205 4
HET DMS v 206 4
HET DMS v 207 4
HET DMS v 208 4
HET DMS v 209 4
HET DMS v 210 4
HET DMS v 211 4
HET BCR y 101 40
HET UNL x 101 15
HETNAM FME N-FORMYLMETHIONINE
HETNAM OEX CA-MN4-O5 CLUSTER
HETNAM FE2 FE (II) ION
HETNAM CL CHLORIDE ION
HETNAM CLA CHLOROPHYLL A
HETNAM PHO PHEOPHYTIN A
HETNAM BCR BETA-CAROTENE
HETNAM LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE
HETNAM PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,
HETNAM 2 PL9 6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-
HETNAM 3 PL9 CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-
HETNAM 4 PL9 BENZOQUINONE
HETNAM LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE
HETNAM SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-
HETNAM 2 SQD GLUCOPYRANOSYL]-SN-GLYCEROL
HETNAM LMT DODECYL-BETA-D-MALTOSIDE
HETNAM UNL UNKNOWN LIGAND
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM BCT BICARBONATE ION
HETNAM CA CALCIUM ION
HETNAM HTG HEPTYL 1-THIO-BETA-D-GLUCOPYRANOSIDE
HETNAM DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM RRX (3R)-BETA,BETA-CAROTEN-3-OL
HETNAM MG MAGNESIUM ION
HETNAM HEC HEME C
HETSYN PL9 PLASTOQUINONE 9
HETSYN SQD SULFOQUINOVOSYLDIACYLGLYCEROL
HETSYN HEM HEME
HETSYN RRX BETA-CRYPTOXANTHIN
FORMUL 8 FME 4(C6 H11 N O3 S)
FORMUL 37 OEX 2(CA MN4 O5)
FORMUL 38 FE2 2(FE 2+)
FORMUL 39 CL 4(CL 1-)
FORMUL 41 CLA 70(C55 H72 MG N4 O5 2+)
FORMUL 43 PHO 4(C55 H74 N4 O5)
FORMUL 45 BCR 18(C40 H56)
FORMUL 46 LMG 12(C45 H86 O10)
FORMUL 47 PL9 4(C53 H80 O2)
FORMUL 48 LHG 12(C38 H75 O10 P)
FORMUL 49 SQD 8(C41 H78 O12 S)
FORMUL 50 LMT 11(C24 H46 O11)
FORMUL 52 DMS 133(C2 H6 O S)
FORMUL 57 BCT 2(C H O3 1-)
FORMUL 58 CA 5(CA 2+)
FORMUL 80 HTG 17(C13 H26 O5 S)
FORMUL 16 DGD 10(C51 H96 O15)
FORMUL 59 HEM 2(C34 H32 FE N4 O4)
FORMUL 61 RRX 2(C40 H56 O)
FORMUL 71 MG 4(MG 2+)
FORMUL 97 HEC 2(C34 H34 FE N4 O4)
FORMUL 88 HOH *2317(H2 O)
HELIX 1 AA1 ASN A 12 THR A 22 1 11
HELIX 2 AA2 VAL A 30 ALA A 55 1 26
HELIX 3 AA3 PRO A 95 ALA A 99 5 5
HELIX 4 AA4 SER A 101 ASN A 108 1 8
HELIX 5 AA5 GLY A 109 LEU A 137 1 29
HELIX 6 AA6 TRP A 142 LEU A 159 1 18
HELIX 7 AA7 LEU A 159 GLY A 166 1 8
HELIX 8 AA8 SER A 167 GLY A 171 5 5
HELIX 9 AA9 ILE A 176 ASN A 191 1 16
HELIX 10 AB1 ILE A 192 MET A 194 5 3
HELIX 11 AB2 HIS A 195 SER A 222 1 28
HELIX 12 AB3 SER A 232 TYR A 237 5 6
HELIX 13 AB4 ASN A 247 ILE A 259 1 13
HELIX 14 AB5 PHE A 260 SER A 264 5 5
HELIX 15 AB6 ASN A 267 ALA A 294 1 28
HELIX 16 AB7 THR A 316 HIS A 332 1 17
HELIX 17 AB8 TYR B 6 ILE B 13 5 8
HELIX 18 AB9 ASP B 15 PHE B 45 1 31
HELIX 19 AC1 PRO B 54 GLN B 58 5 5
HELIX 20 AC2 VAL B 62 LEU B 69 1 8
HELIX 21 AC3 SER B 92 TYR B 117 1 26
HELIX 22 AC4 LEU B 120 ARG B 124 5 5
HELIX 23 AC5 ASP B 134 PHE B 156 1 23
HELIX 24 AC6 GLY B 186 ASN B 191 5 6
HELIX 25 AC7 ASN B 194 VAL B 219 1 26
HELIX 26 AC8 PRO B 222 LEU B 229 1 8
HELIX 27 AC9 ASN B 233 GLY B 259 1 27
HELIX 28 AD1 PRO B 264 GLY B 269 1 6
HELIX 29 AD2 THR B 271 SER B 277 1 7
HELIX 30 AD3 SER B 278 SER B 294 1 17
HELIX 31 AD4 THR B 297 ALA B 304 1 8
HELIX 32 AD5 PRO B 306 ASP B 313 1 8
HELIX 33 AD6 TYR B 314 ASN B 318 5 5
HELIX 34 AD7 PRO B 329 GLY B 333 5 5
HELIX 35 AD8 SER B 391 GLY B 396 1 6
HELIX 36 AD9 ASP B 413 ILE B 425 1 13
HELIX 37 AE1 SER B 446 PHE B 475 1 30
HELIX 38 AE2 ARG B 476 PHE B 479 5 4
HELIX 39 AE3 SER B 487 VAL B 491 5 5
HELIX 40 AE4 ASP B 501 ARG B 505 5 5
HELIX 41 AE5 ASP C 27 GLY C 32 1 6
HELIX 42 AE6 ALA C 34 ILE C 43 5 10
HELIX 43 AE7 LEU C 45 PHE C 75 1 31
HELIX 44 AE8 PRO C 80 GLN C 84 5 5
HELIX 45 AE9 LEU C 88 LEU C 95 1 8
HELIX 46 AF1 GLY C 100 GLU C 104 5 5
HELIX 47 AF2 THR C 108 ARG C 135 1 28
HELIX 48 AF3 ASP C 153 PHE C 182 1 30
HELIX 49 AF4 ASP C 205 PHE C 210 1 6
HELIX 50 AF5 GLY C 211 LYS C 215 5 5
HELIX 51 AF6 GLY C 222 VAL C 227 5 6
HELIX 52 AF7 ASN C 229 THR C 254 1 26
HELIX 53 AF8 PHE C 257 PHE C 264 1 8
HELIX 54 AF9 SER C 267 ASN C 293 1 27
HELIX 55 AG1 PRO C 298 GLY C 303 1 6
HELIX 56 AG2 THR C 305 LEU C 324 1 20
HELIX 57 AG3 GLY C 353 TRP C 359 5 7
HELIX 58 AG4 LEU C 366 PRO C 368 5 3
HELIX 59 AG5 ASP C 376 ASP C 383 1 8
HELIX 60 AG6 GLN C 385 THR C 397 1 13
HELIX 61 AG7 SER C 421 ALA C 453 1 33
HELIX 62 AG8 GLU C 464 MET C 469 5 6
HELIX 63 AG9 GLY D 13 LYS D 23 1 11
HELIX 64 AH1 TRP D 32 VAL D 55 1 24
HELIX 65 AH2 SER D 57 GLY D 62 1 6
HELIX 66 AH3 SER D 66 GLY D 70 5 5
HELIX 67 AH4 ALA D 82 GLY D 86 5 5
HELIX 68 AH5 ASP D 100 LEU D 107 1 8
HELIX 69 AH6 GLY D 108 GLY D 137 1 30
HELIX 70 AH7 PRO D 140 LEU D 158 1 19
HELIX 71 AH8 LEU D 158 GLN D 164 1 7
HELIX 72 AH9 SER D 166 ALA D 170 5 5
HELIX 73 AI1 VAL D 175 ASN D 190 1 16
HELIX 74 AI2 TRP D 191 LEU D 193 5 3
HELIX 75 AI3 ASN D 194 THR D 221 1 28
HELIX 76 AI4 SER D 245 PHE D 257 1 13
HELIX 77 AI5 ASN D 263 ALA D 290 1 28
HELIX 78 AI6 PHE D 298 ASP D 308 1 11
HELIX 79 AI7 THR D 313 GLN D 334 1 22
HELIX 80 AI8 PRO D 335 ASN D 338 5 4
HELIX 81 AI9 PRO D 342 LEU D 346 5 5
HELIX 82 AJ1 PRO E 9 SER E 16 1 8
HELIX 83 AJ2 SER E 16 THR E 40 1 25
HELIX 84 AJ3 GLY E 41 GLY E 48 1 8
HELIX 85 AJ4 GLU E 71 GLN E 82 1 12
HELIX 86 AJ5 THR F 17 GLN F 41 1 25
HELIX 87 AJ6 THR H 5 ARG H 12 1 8
HELIX 88 AJ7 PRO H 13 SER H 16 5 4
HELIX 89 AJ8 THR H 27 ASN H 50 1 24
HELIX 90 AJ9 GLU I 2 SER I 25 1 24
HELIX 91 AK1 GLY I 26 ARG I 30 5 5
HELIX 92 AK2 PRO J 9 TYR J 33 1 25
HELIX 93 AK3 PRO K 12 ILE K 17 5 6
HELIX 94 AK4 PHE K 18 LEU K 25 1 8
HELIX 95 AK5 VAL K 27 VAL K 43 1 17
HELIX 96 AK6 ASN L 13 ASN L 37 1 25
HELIX 97 AK7 THR O 6 VAL O 11 1 6
HELIX 98 AK8 GLY O 14 LYS O 18 5 5
HELIX 99 AK9 GLU O 179 GLU O 181 5 3
HELIX 100 AL1 LEU O 182 VAL O 187 1 6
HELIX 101 AL2 ASP O 223 ALA O 227 5 5
HELIX 102 AL3 GLU T 2 PHE T 23 1 22
HELIX 103 AL4 ASN U 11 LEU U 17 1 7
HELIX 104 AL5 GLY U 18 GLU U 23 5 6
HELIX 105 AL6 ASN U 31 TYR U 38 5 8
HELIX 106 AL7 PRO U 43 ASN U 52 1 10
HELIX 107 AL8 SER U 57 ILE U 64 5 8
HELIX 108 AL9 THR U 68 LEU U 79 1 12
HELIX 109 AM1 GLU U 88 GLU U 93 1 6
HELIX 110 AM2 GLY U 94 ASP U 96 5 3
HELIX 111 AM3 THR V 22 CYS V 37 1 16
HELIX 112 AM4 CYS V 37 VAL V 42 1 6
HELIX 113 AM5 GLY V 43 ILE V 45 5 3
HELIX 114 AM6 ARG V 55 ALA V 62 1 8
HELIX 115 AM7 ASN V 68 ASN V 78 1 11
HELIX 116 AM8 SER V 94 ALA V 98 5 5
HELIX 117 AM9 PHE V 101 ARG V 105 5 5
HELIX 118 AN1 THR V 108 GLY V 127 1 20
HELIX 119 AN2 ASP V 128 TRP V 130 5 3
HELIX 120 AN3 GLY V 133 TYR V 137 5 5
HELIX 121 AN4 ILE Y 19 ARG Y 42 1 24
HELIX 122 AN5 THR X 4 ASP X 35 1 32
HELIX 123 AN6 THR Z 2 ALA Z 28 1 27
HELIX 124 AN7 TRP Z 33 VAL Z 62 1 30
HELIX 125 AN8 ASN a 12 THR a 22 1 11
HELIX 126 AN9 VAL a 30 ALA a 55 1 26
HELIX 127 AO1 PRO a 95 ALA a 99 5 5
HELIX 128 AO2 SER a 101 ASN a 108 1 8
HELIX 129 AO3 GLY a 109 LEU a 137 1 29
HELIX 130 AO4 TRP a 142 LEU a 159 1 18
HELIX 131 AO5 LEU a 159 GLY a 166 1 8
HELIX 132 AO6 SER a 167 GLY a 171 5 5
HELIX 133 AO7 ILE a 176 ASN a 191 1 16
HELIX 134 AO8 ILE a 192 MET a 194 5 3
HELIX 135 AO9 HIS a 195 SER a 222 1 28
HELIX 136 AP1 SER a 232 TYR a 237 5 6
HELIX 137 AP2 ASN a 247 ILE a 259 1 13
HELIX 138 AP3 ASN a 267 ALA a 294 1 28
HELIX 139 AP4 THR a 316 HIS a 332 1 17
HELIX 140 AP5 TYR b 6 ILE b 13 5 8
HELIX 141 AP6 ASP b 15 PHE b 45 1 31
HELIX 142 AP7 PRO b 54 GLN b 58 5 5
HELIX 143 AP8 VAL b 62 LEU b 69 1 8
HELIX 144 AP9 SER b 92 TYR b 117 1 26
HELIX 145 AQ1 LEU b 120 ARG b 124 5 5
HELIX 146 AQ2 ASP b 134 PHE b 156 1 23
HELIX 147 AQ3 GLY b 186 ASN b 191 5 6
HELIX 148 AQ4 ASN b 194 VAL b 219 1 26
HELIX 149 AQ5 PRO b 222 LEU b 229 1 8
HELIX 150 AQ6 ASN b 233 GLY b 259 1 27
HELIX 151 AQ7 PRO b 264 GLY b 269 1 6
HELIX 152 AQ8 THR b 271 SER b 277 1 7
HELIX 153 AQ9 SER b 278 SER b 294 1 17
HELIX 154 AR1 THR b 297 ALA b 304 1 8
HELIX 155 AR2 PRO b 306 ASP b 313 1 8
HELIX 156 AR3 TYR b 314 ASN b 318 5 5
HELIX 157 AR4 PRO b 329 GLY b 333 5 5
HELIX 158 AR5 ASP b 413 ILE b 425 1 13
HELIX 159 AR6 SER b 446 PHE b 475 1 30
HELIX 160 AR7 ARG b 476 PHE b 479 5 4
HELIX 161 AR8 ASP c 27 GLY c 32 1 6
HELIX 162 AR9 ALA c 34 ILE c 43 5 10
HELIX 163 AS1 LEU c 45 PHE c 75 1 31
HELIX 164 AS2 PRO c 80 GLN c 84 5 5
HELIX 165 AS3 ILE c 87 LEU c 95 1 9
HELIX 166 AS4 GLY c 100 GLU c 104 5 5
HELIX 167 AS5 THR c 108 ARG c 135 1 28
HELIX 168 AS6 ASP c 153 PHE c 182 1 30
HELIX 169 AS7 ASP c 205 PHE c 210 1 6
HELIX 170 AS8 GLY c 211 LYS c 215 5 5
HELIX 171 AS9 GLY c 222 VAL c 227 5 6
HELIX 172 AT1 ASN c 229 LEU c 253 1 25
HELIX 173 AT2 PHE c 257 PHE c 264 1 8
HELIX 174 AT3 SER c 267 ASN c 293 1 27
HELIX 175 AT4 PRO c 298 GLY c 303 1 6
HELIX 176 AT5 THR c 305 LEU c 324 1 20
HELIX 177 AT6 GLY c 353 TRP c 359 5 7
HELIX 178 AT7 LEU c 366 PRO c 368 5 3
HELIX 179 AT8 ASP c 376 ASP c 383 1 8
HELIX 180 AT9 GLN c 385 THR c 397 1 13
HELIX 181 AU1 SER c 421 ALA c 453 1 33
HELIX 182 AU2 ASP c 460 MET c 469 5 10
HELIX 183 AU3 GLY d 13 LYS d 23 1 11
HELIX 184 AU4 VAL d 30 VAL d 55 1 26
HELIX 185 AU5 SER d 57 GLY d 62 1 6
HELIX 186 AU6 SER d 66 GLY d 70 5 5
HELIX 187 AU7 ALA d 82 GLY d 86 5 5
HELIX 188 AU8 ASP d 100 GLY d 108 1 9
HELIX 189 AU9 GLY d 108 GLY d 137 1 30
HELIX 190 AV1 PRO d 140 LEU d 158 1 19
HELIX 191 AV2 LEU d 158 GLN d 164 1 7
HELIX 192 AV3 SER d 166 ALA d 170 5 5
HELIX 193 AV4 VAL d 175 ASN d 190 1 16
HELIX 194 AV5 TRP d 191 LEU d 193 5 3
HELIX 195 AV6 ASN d 194 ASN d 220 1 27
HELIX 196 AV7 SER d 245 PHE d 257 1 13
HELIX 197 AV8 ASN d 263 LEU d 291 1 29
HELIX 198 AV9 PHE d 298 ASP d 308 1 11
HELIX 199 AW1 THR d 313 GLN d 334 1 22
HELIX 200 AW2 PRO d 335 ASN d 338 5 4
HELIX 201 AW3 PRO d 342 LEU d 346 5 5
HELIX 202 AW4 PRO e 9 ILE e 14 1 6
HELIX 203 AW5 SER e 16 THR e 40 1 25
HELIX 204 AW6 GLY e 41 GLY e 48 1 8
HELIX 205 AW7 GLU e 71 GLN e 82 1 12
HELIX 206 AW8 THR f 17 GLN f 41 1 25
HELIX 207 AW9 THR h 5 ARG h 12 1 8
HELIX 208 AX1 PRO h 13 SER h 16 5 4
HELIX 209 AX2 THR h 27 ASN h 50 1 24
HELIX 210 AX3 GLU i 2 SER i 25 1 24
HELIX 211 AX4 GLY i 26 ARG i 30 5 5
HELIX 212 AX5 PRO j 9 TYR j 33 1 25
HELIX 213 AX6 PRO k 12 ILE k 17 5 6
HELIX 214 AX7 PHE k 18 ASP k 23 1 6
HELIX 215 AX8 VAL k 24 PRO k 26 5 3
HELIX 216 AX9 VAL k 27 VAL k 43 1 17
HELIX 217 AY1 ASN l 13 ASN l 37 1 25
HELIX 218 AY2 THR o 6 VAL o 11 1 6
HELIX 219 AY3 GLY o 14 LYS o 18 5 5
HELIX 220 AY4 GLU o 179 GLU o 181 5 3
HELIX 221 AY5 LEU o 182 VAL o 187 1 6
HELIX 222 AY6 GLU t 2 PHE t 23 1 22
HELIX 223 AY7 ASN u 11 LEU u 17 1 7
HELIX 224 AY8 GLY u 18 GLU u 23 5 6
HELIX 225 AY9 ASN u 31 TYR u 38 5 8
HELIX 226 AZ1 PRO u 43 ALA u 53 1 11
HELIX 227 AZ2 SER u 57 ILE u 64 5 8
HELIX 228 AZ3 THR u 68 LEU u 79 1 12
HELIX 229 AZ4 GLU u 88 GLU u 93 1 6
HELIX 230 AZ5 GLY u 94 ASP u 96 5 3
HELIX 231 AZ6 THR v 22 CYS v 37 1 16
HELIX 232 AZ7 CYS v 37 VAL v 42 1 6
HELIX 233 AZ8 GLY v 43 ILE v 45 5 3
HELIX 234 AZ9 ARG v 55 LEU v 61 1 7
HELIX 235 BA1 ASN v 68 ASN v 78 1 11
HELIX 236 BA2 SER v 94 ALA v 98 5 5
HELIX 237 BA3 PHE v 101 ARG v 105 5 5
HELIX 238 BA4 THR v 108 GLY v 127 1 20
HELIX 239 BA5 ASP v 128 TRP v 130 5 3
HELIX 240 BA6 GLY v 133 TYR v 137 5 5
HELIX 241 BA7 ILE y 19 ARG y 42 1 24
HELIX 242 BA8 THR x 4 ASP x 35 1 32
HELIX 243 BA9 THR z 2 ALA z 28 1 27
HELIX 244 BB1 ASP z 32 PHE z 59 1 28
SHEET 1 AA1 2 ALA A 81 VAL A 82 0
SHEET 2 AA1 2 LEU A 174 GLY A 175 -1 O LEU A 174 N VAL A 82
SHEET 1 AA2 2 LEU A 297 ASN A 298 0
SHEET 2 AA2 2 GLY C 402 SER C 403 1 O GLY C 402 N ASN A 298
SHEET 1 AA3 2 LEU B 3 PRO B 4 0
SHEET 2 AA3 2 VAL L 10 GLU L 11 1 O GLU L 11 N LEU B 3
SHEET 1 AA4 2 MET B 166 VAL B 168 0
SHEET 2 AA4 2 SER B 177 GLN B 179 -1 O SER B 177 N VAL B 168
SHEET 1 AA5 6 VAL B 377 ASP B 380 0
SHEET 2 AA5 6 ILE B 369 THR B 371 -1 N LEU B 370 O ALA B 379
SHEET 3 AA5 6 GLU B 353 VAL B 356 -1 N PHE B 355 O THR B 371
SHEET 4 AA5 6 ILE B 336 ARG B 347 -1 N PHE B 346 O LEU B 354
SHEET 5 AA5 6 THR B 398 TYR B 402 -1 O TYR B 402 N HIS B 343
SHEET 6 AA5 6 THR B 410 PHE B 411 -1 O PHE B 411 N VAL B 399
SHEET 1 AA6 5 VAL B 377 ASP B 380 0
SHEET 2 AA6 5 ILE B 369 THR B 371 -1 N LEU B 370 O ALA B 379
SHEET 3 AA6 5 GLU B 353 VAL B 356 -1 N PHE B 355 O THR B 371
SHEET 4 AA6 5 ILE B 336 ARG B 347 -1 N PHE B 346 O LEU B 354
SHEET 5 AA6 5 ILE B 429 ASP B 433 -1 O GLU B 431 N GLN B 338
SHEET 1 AA7 2 LEU C 185 ASP C 187 0
SHEET 2 AA7 2 ASP C 195 ARG C 197 -1 O ASP C 195 N ASP C 187
SHEET 1 AA8 2 LEU C 341 ARG C 343 0
SHEET 2 AA8 2 ILE C 349 PHE C 351 -1 O ILE C 350 N MET C 342
SHEET 1 AA9 2 ARG C 370 GLY C 371 0
SHEET 2 AA9 2 GLY C 374 LEU C 375 -1 O GLY C 374 N GLY C 371
SHEET 1 AB1 2 ALA D 77 VAL D 78 0
SHEET 2 AB1 2 PHE D 173 GLY D 174 -1 O PHE D 173 N VAL D 78
SHEET 1 AB2 2 TYR O 30 PRO O 31 0
SHEET 2 AB2 2 SER O 135 ILE O 136 -1 O ILE O 136 N TYR O 30
SHEET 1 AB310 PHE O 65 PRO O 67 0
SHEET 2 AB310 TYR O 38 LYS O 53 -1 N VAL O 52 O VAL O 66
SHEET 3 AB310 GLU O 232 PRO O 245 -1 O LYS O 234 N LEU O 51
SHEET 4 AB310 GLU O 210 LEU O 220 -1 N GLN O 219 O VAL O 233
SHEET 5 AB310 LEU O 192 VAL O 204 -1 N ASN O 200 O THR O 214
SHEET 6 AB310 ASP O 141 PRO O 149 -1 N GLY O 144 O ILE O 197
SHEET 7 AB310 VAL O 126 SER O 128 -1 N SER O 128 O LYS O 143
SHEET 8 AB310 LEU O 93 ILE O 101 -1 N PHE O 95 O ALA O 127
SHEET 9 AB310 LEU O 78 VAL O 87 -1 N GLN O 82 O GLU O 98
SHEET 10 AB310 TYR O 38 LYS O 53 -1 N LEU O 45 O LEU O 78
SHEET 1 AB4 3 LYS O 69 LEU O 70 0
SHEET 2 AB4 3 PHE O 103 GLN O 109 -1 O GLN O 109 N LYS O 69
SHEET 3 AB4 3 ARG O 115 THR O 121 -1 O ILE O 116 N VAL O 108
SHEET 1 AB5 2 ILE U 25 ASP U 26 0
SHEET 2 AB5 2 PHE U 82 THR U 83 1 O THR U 83 N ILE U 25
SHEET 1 AB6 2 THR V 9 PRO V 11 0
SHEET 2 AB6 2 THR V 18 THR V 20 -1 O ILE V 19 N VAL V 10
SHEET 1 AB7 2 ALA a 81 VAL a 82 0
SHEET 2 AB7 2 LEU a 174 GLY a 175 -1 O LEU a 174 N VAL a 82
SHEET 1 AB8 2 LEU a 297 ASN a 298 0
SHEET 2 AB8 2 GLY c 402 SER c 403 1 O GLY c 402 N ASN a 298
SHEET 1 AB9 2 LEU b 3 PRO b 4 0
SHEET 2 AB9 2 VAL l 10 GLU l 11 1 O GLU l 11 N LEU b 3
SHEET 1 AC1 2 MET b 166 VAL b 168 0
SHEET 2 AC1 2 SER b 177 GLN b 179 -1 O GLN b 179 N MET b 166
SHEET 1 AC2 6 VAL b 377 ASP b 380 0
SHEET 2 AC2 6 ILE b 369 THR b 371 -1 N LEU b 370 O ALA b 379
SHEET 3 AC2 6 GLU b 353 VAL b 356 -1 N PHE b 355 O THR b 371
SHEET 4 AC2 6 ILE b 336 ARG b 347 -1 N PHE b 346 O LEU b 354
SHEET 5 AC2 6 THR b 398 TYR b 402 -1 O SER b 400 N VAL b 345
SHEET 6 AC2 6 THR b 410 PHE b 411 -1 O PHE b 411 N VAL b 399
SHEET 1 AC3 5 VAL b 377 ASP b 380 0
SHEET 2 AC3 5 ILE b 369 THR b 371 -1 N LEU b 370 O ALA b 379
SHEET 3 AC3 5 GLU b 353 VAL b 356 -1 N PHE b 355 O THR b 371
SHEET 4 AC3 5 ILE b 336 ARG b 347 -1 N PHE b 346 O LEU b 354
SHEET 5 AC3 5 ILE b 429 ASP b 433 -1 O GLU b 431 N GLN b 338
SHEET 1 AC4 2 LEU c 185 ASP c 187 0
SHEET 2 AC4 2 ASP c 195 ARG c 197 -1 O ARG c 197 N LEU c 185
SHEET 1 AC5 2 LEU c 341 ARG c 343 0
SHEET 2 AC5 2 ILE c 349 PHE c 351 -1 O ILE c 350 N MET c 342
SHEET 1 AC6 2 ARG c 370 GLY c 371 0
SHEET 2 AC6 2 GLY c 374 LEU c 375 -1 O GLY c 374 N GLY c 371
SHEET 1 AC7 2 ALA d 77 VAL d 78 0
SHEET 2 AC7 2 PHE d 173 GLY d 174 -1 O PHE d 173 N VAL d 78
SHEET 1 AC8 2 TYR o 30 PRO o 31 0
SHEET 2 AC8 2 SER o 135 ILE o 136 -1 O ILE o 136 N TYR o 30
SHEET 1 AC9 4 PHE o 65 PRO o 67 0
SHEET 2 AC9 4 TYR o 38 LYS o 53 -1 N VAL o 52 O VAL o 66
SHEET 3 AC9 4 LEU o 78 VAL o 87 -1 O LEU o 78 N LEU o 45
SHEET 4 AC9 4 ASP o 99 ILE o 101 -1 O ASP o 99 N GLN o 82
SHEET 1 AD110 PHE o 65 PRO o 67 0
SHEET 2 AD110 TYR o 38 LYS o 53 -1 N VAL o 52 O VAL o 66
SHEET 3 AD110 GLU o 232 PRO o 245 -1 O LYS o 234 N LEU o 51
SHEET 4 AD110 GLU o 210 LEU o 220 -1 N SER o 217 O ILE o 235
SHEET 5 AD110 LEU o 192 ASP o 205 -1 N ASP o 205 O GLU o 210
SHEET 6 AD110 ASP o 141 PRO o 149 -1 N VAL o 148 O THR o 193
SHEET 7 AD110 VAL o 126 SER o 128 -1 N SER o 128 O LYS o 143
SHEET 8 AD110 LEU o 93 VAL o 96 -1 N PHE o 95 O ALA o 127
SHEET 9 AD110 LEU o 78 VAL o 87 -1 N GLU o 84 O VAL o 96
SHEET 10 AD110 ASP o 99 ILE o 101 -1 O ASP o 99 N GLN o 82
SHEET 1 AD2 3 LYS o 69 LEU o 70 0
SHEET 2 AD2 3 PHE o 103 GLN o 109 -1 O GLN o 109 N LYS o 69
SHEET 3 AD2 3 ARG o 115 THR o 121 -1 O ILE o 116 N VAL o 108
SHEET 1 AD3 2 ILE u 25 ASP u 26 0
SHEET 2 AD3 2 PHE u 82 THR u 83 1 O THR u 83 N ILE u 25
SSBOND 1 CYS O 19 CYS O 44 1555 1555 2.03
SSBOND 2 CYS o 19 CYS o 44 1555 1555 1.98
LINK C FME I 1 N GLU I 2 1555 1555 1.34
LINK C FME T 1 N GLU T 2 1555 1555 1.34
LINK SG CYS V 37 CAB HEC V 202 1555 1555 1.84
LINK SG CYS V 40 CAC HEC V 202 1555 1555 1.94
LINK C FME i 1 N GLU i 2 1555 1555 1.35
LINK C FME t 1 N GLU t 2 1555 1555 1.34
LINK SG CYS v 37 CAB HEC v 202 1555 1555 1.82
LINK SG CYS v 40 CAC HEC v 202 1555 1555 1.97
LINK OD1 ASP A 170 MN4 OEX A 401 1555 1555 1.98
LINK OD2 ASP A 170 CA1 OEX A 401 1555 1555 2.41
LINK OE1 GLU A 189 CA1 OEX A 401 1555 1555 2.96
LINK OE2 GLU A 189 MN1 OEX A 401 1555 1555 1.87
LINK NE2 HIS A 215 FE FE2 A 402 1555 1555 2.05
LINK NE2 HIS A 272 FE FE2 A 402 1555 1555 2.32
LINK NE2 HIS A 332 MN1 OEX A 401 1555 1555 2.03
LINK OE1 GLU A 333 MN3 OEX A 401 1555 1555 1.97
LINK OE2 GLU A 333 MN4 OEX A 401 1555 1555 2.13
LINK OD1 ASP A 342 MN2 OEX A 401 1555 1555 2.04
LINK OD2 ASP A 342 MN1 OEX A 401 1555 1555 2.20
LINK O ALA A 344 CA1 OEX A 401 1555 1555 2.31
LINK OXT ALA A 344 MN2 OEX A 401 1555 1555 1.97
LINK CA1 OEX A 401 O HOH A 521 1555 1555 2.30
LINK MN4 OEX A 401 O HOH A 522 1555 1555 2.16
LINK MN4 OEX A 401 O HOH A 591 1555 1555 2.15
LINK CA1 OEX A 401 O HOH A 604 1555 1555 2.41
LINK MN2 OEX A 401 OE1 GLU C 354 1555 1555 2.08
LINK MN3 OEX A 401 OE2 GLU C 354 1555 1555 2.14
LINK FE FE2 A 402 O2 ABCT A 421 1555 1555 2.54
LINK FE FE2 A 402 O2 BBCT A 421 1555 1555 2.46
LINK FE FE2 A 402 O3 ABCT A 421 1555 1555 2.35
LINK FE FE2 A 402 O3 BBCT A 421 1555 1555 2.29
LINK FE FE2 A 402 NE2 HIS D 214 1555 1555 2.17
LINK FE FE2 A 402 NE2 HIS D 268 1555 1555 2.38
LINK MG CLA A 406 O HOH A 614 1555 1555 2.12
LINK O HOH A 578 MG CLA D 401 1555 1555 2.02
LINK OD1 ASN B 438 CA CA B 601 1555 1555 2.59
LINK CA CA B 601 O HOH B 720 1555 1555 2.69
LINK CA CA B 601 O HOH B 850 1555 1555 2.62
LINK CA CA B 601 O HOH B 932 1555 1555 2.34
LINK CA CA B 601 O HOH O 518 1555 1555 2.59
LINK MG CLA B 602 O HOH B 705 1555 1555 1.97
LINK MG CLA B 608 O HOH B 855 1555 1555 1.93
LINK MG CLA B 611 O HOH B 710 1555 1555 2.11
LINK OD1 ASN C 39 MG CLA C 512 1555 1555 1.97
LINK MG CLA C 505 O HOH C 722 1555 1555 2.06
LINK MG CLA C 508 O HOH C 607 1555 1555 2.08
LINK NE2 HIS E 23 FE HEM E 102 1555 1555 2.04
LINK FE HEM E 102 NE2 HIS F 24 1555 1555 2.10
LINK O HOH F 201 MG MG J 102 1555 1555 2.50
LINK O GLY J 31 MG MG J 102 1555 1555 2.25
LINK O ALA J 34 MG MG J 102 1555 1555 2.31
LINK O LEU J 36 MG MG J 102 1555 1555 2.39
LINK O4 LMG J 101 MG MG J 102 1555 1555 2.40
LINK OD2 ASP K 19 MG MG K 102 1555 1555 2.38
LINK OD2 ASP K 23 MG MG K 102 1555 1555 2.51
LINK MG MG K 102 O HOH K 201 1555 1555 2.15
LINK MG MG K 102 O HOH K 206 1555 1555 2.81
LINK MG MG K 102 O HOH Y 206 1555 1555 2.79
LINK O THR O 138 CA CA O 302 1555 1555 2.46
LINK OD1 ASN O 200 CA CA O 302 1555 1555 2.49
LINK O VAL O 201 CA CA O 302 1555 1555 2.33
LINK CA CA O 302 O HOH O 459 1555 1555 2.19
LINK CA CA O 302 O HOH O 533 1555 1555 2.93
LINK NE2 HIS V 41 FE HEC V 202 1555 1555 2.00
LINK NE2 HIS V 92 FE HEC V 202 1555 1555 2.02
LINK OD1 ASP a 170 CA1 OEX a 403 1555 1555 2.53
LINK OD2 ASP a 170 MN4 OEX a 403 1555 1555 2.10
LINK OE1 GLU a 189 CA1 OEX a 403 1555 1555 2.85
LINK OE2 GLU a 189 MN1 OEX a 403 1555 1555 1.78
LINK NE2 HIS a 215 FE FE2 a 404 1555 1555 1.98
LINK NE2 HIS a 272 FE FE2 a 404 1555 1555 2.30
LINK NE2 HIS a 332 MN1 OEX a 403 1555 1555 2.05
LINK OE1 GLU a 333 MN3 OEX a 403 1555 1555 2.06
LINK OE2 GLU a 333 MN4 OEX a 403 1555 1555 2.05
LINK OD1 ASP a 342 MN2 OEX a 403 1555 1555 2.00
LINK OD2 ASP a 342 MN1 OEX a 403 1555 1555 2.19
LINK O ALA a 344 CA1 OEX a 403 1555 1555 2.60
LINK OXT ALA a 344 MN2 OEX a 403 1555 1555 1.96
LINK CA1 OEX a 403 O HOH a 506 1555 1555 2.40
LINK MN4 OEX a 403 O HOH a 544 1555 1555 2.21
LINK MN4 OEX a 403 O HOH a 597 1555 1555 2.33
LINK CA1 OEX a 403 O HOH a 599 1555 1555 2.62
LINK MN2 OEX a 403 OE1 GLU c 354 1555 1555 2.11
LINK MN3 OEX a 403 OE2 GLU c 354 1555 1555 2.29
LINK FE FE2 a 404 O2 BCT a 422 1555 1555 2.35
LINK FE FE2 a 404 O3 BCT a 422 1555 1555 2.59
LINK FE FE2 a 404 NE2 HIS d 214 1555 1555 2.08
LINK FE FE2 a 404 NE2 HIS d 268 1555 1555 2.33
LINK MG CLA a 408 O HOH a 567 1555 1555 2.15
LINK MG CLA a 409 O HOH a 602 1555 1555 2.13
LINK OD1 ASN b 438 CA CA b 601 1555 1555 2.41
LINK CA CA b 601 O HOH b 755 1555 1555 2.64
LINK CA CA b 601 O HOH b 787 1555 1555 2.12
LINK CA CA b 601 O HOH b 861 1555 1555 2.45
LINK MG CLA b 602 O HOH b 706 1555 1555 2.16
LINK MG CLA b 608 O HOH b 860 1555 1555 1.96
LINK MG CLA b 611 O HOH b 737 1555 1555 2.01
LINK O PHE c 22 CA CA c 901 1555 1555 2.38
LINK O THR c 24 CA CA c 901 1555 1555 2.18
LINK OD1 ASP c 27 CA CA c 901 1555 1555 2.76
LINK OD2 ASP c 27 CA CA c 901 1555 1555 2.52
LINK OG SER c 30 CA CA c 901 1555 1555 2.30
LINK OD1 ASN c 39 MG CLA c 912 1555 1555 2.04
LINK CA CA c 901 O HOH c1158 1555 1555 2.52
LINK MG CLA c 905 O HOH c1166 1555 1555 2.10
LINK MG CLA c 908 O HOH c1017 1555 1555 2.04
LINK NE2 HIS e 23 FE HEM e 101 1555 1555 2.11
LINK FE HEM e 101 NE2 HIS f 24 1555 1555 2.06
LINK O HOH f 201 MG MG j 102 1555 1555 2.54
LINK O GLY j 31 MG MG j 102 1555 1555 2.21
LINK O ALA j 34 MG MG j 102 1555 1555 2.49
LINK O LEU j 36 MG MG j 102 1555 1555 2.25
LINK O4 LMG j 101 MG MG j 102 1555 1555 2.52
LINK OD2 ASP k 19 MG MG k 102 1555 1555 2.21
LINK OD2 ASP k 23 MG MG k 102 1555 1555 2.40
LINK MG MG k 102 O HOH k 201 1555 1555 2.12
LINK MG MG k 102 O HOH k 206 1555 1555 2.96
LINK MG MG k 102 O HOH k 207 1555 1555 2.51
LINK O THR o 138 CA CA o 301 1555 1555 2.47
LINK OD1 ASN o 200 CA CA o 301 1555 1555 2.32
LINK O VAL o 201 CA CA o 301 1555 1555 2.35
LINK CA CA o 301 O HOH o 416 1555 1555 2.49
LINK CA CA o 301 O HOH o 441 1555 1555 2.60
LINK CA CA o 301 O HOH o 447 1555 1555 2.37
LINK CA CA o 301 O HOH o 489 1555 1555 2.32
LINK NE2 HIS v 41 FE HEC v 202 1555 1555 1.99
LINK NE2 HIS v 92 FE HEC v 202 1555 1555 1.92
CISPEP 1 TYR U 42 PRO U 43 0 4.19
CISPEP 2 ALA U 53 PRO U 54 0 1.68
CISPEP 3 THR V 63 PRO V 64 0 -11.67
CISPEP 4 TYR u 42 PRO u 43 0 3.47
CISPEP 5 ALA u 53 PRO u 54 0 -1.22
CISPEP 6 THR v 63 PRO v 64 0 -4.57
CRYST1 121.954 226.993 285.886 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 0.008200 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004405 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003498 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
