HEADER METAL TRANSPORT 11-DEC-06 2O7U
TITLE CRYSTAL STRUCTURE OF K206E/K296E MUTANT OF THE N-TERMINAL HALF
TITLE 2 MOLECULE OF HUMAN TRANSFERRIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEROTRANSFERRIN;
COMPND 3 CHAIN: B, A, C, D, E, F, G, H, I;
COMPND 4 FRAGMENT: N-LOBE;
COMPND 5 SYNONYM: TRANSFERRIN, SIDEROPHILIN, BETA-1-METAL-BINDING GLOBULIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: MESOCRICETUS AURATUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: GOLDEN HAMSTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10036;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: BHK;
SOURCE 9 EXPRESSION_SYSTEM_ORGAN: KIDNEY;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PNUT
KEYWDS HUMAN TRANSFERRIN, IRON BINDING PROTEIN, DILYSINE PAIR, METAL
KEYWDS 2 TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR H.M.BAKER,D.NURIZZO,A.B.MASON,E.N.BAKER
REVDAT 7 30-AUG-23 2O7U 1 REMARK
REVDAT 6 20-OCT-21 2O7U 1 REMARK SEQADV LINK
REVDAT 5 18-OCT-17 2O7U 1 REMARK
REVDAT 4 13-JUL-11 2O7U 1 VERSN
REVDAT 3 24-FEB-09 2O7U 1 VERSN
REVDAT 2 17-APR-07 2O7U 1 JRNL
REVDAT 1 23-JAN-07 2O7U 0
JRNL AUTH H.M.BAKER,D.NURIZZO,A.B.MASON,E.N.BAKER
JRNL TITL STRUCTURES OF TWO MUTANTS THAT PROBE THE ROLE IN IRON
JRNL TITL 2 RELEASE OF THE DILYSINE PAIR IN THE N-LOBE OF HUMAN
JRNL TITL 3 TRANSFERRIN.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 63 408 2007
JRNL REFN ISSN 0907-4449
JRNL PMID 17327678
JRNL DOI 10.1107/S0907444907000182
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 78012
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) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4132
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5706
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.3810
REMARK 3 BIN FREE R VALUE SET COUNT : 312
REMARK 3 BIN FREE R VALUE : 0.4080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 22950
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 72
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.14000
REMARK 3 B22 (A**2) : -0.28000
REMARK 3 B33 (A**2) : 0.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.20000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.405
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.373
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 41.761
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.921
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.893
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 23607 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 31977 ; 1.323 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2952 ; 5.993 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1080 ;37.160 ;24.500
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3897 ;17.550 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 108 ;18.612 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3375 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 18180 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 10736 ; 0.222 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 16095 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 751 ; 0.148 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 19 ; 0.084 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 130 ; 0.317 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.286 ; 0.200
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): 15124 ; 0.440 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23580 ; 0.854 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9615 ; 1.299 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 8397 ; 2.313 ; 4.500
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 3 A 600 1
REMARK 3 2 B 3 B 600 1
REMARK 3 3 C 3 C 600 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2556 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 2556 ; 0.02 ; 0.00
REMARK 3 TIGHT POSITIONAL 1 C (A): 2556 ; 0.02 ; 0.00
REMARK 3 TIGHT THERMAL 1 A (A**2): 2556 ; 0.05 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 2556 ; 0.05 ; 0.00
REMARK 3 TIGHT THERMAL 1 C (A**2): 2556 ; 0.05 ; 0.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : D E F G H I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 6
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 D 3 D 600 1
REMARK 3 2 E 3 E 600 1
REMARK 3 3 F 3 F 600 1
REMARK 3 4 G 3 G 600 1
REMARK 3 5 H 3 H 600 1
REMARK 3 6 I 3 I 600 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 D (A): 2556 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 E (A): 2556 ; 0.04 ; 0.00
REMARK 3 TIGHT POSITIONAL 2 F (A): 2556 ; 0.04 ; 0.00
REMARK 3 TIGHT POSITIONAL 2 G (A): 2556 ; 0.03 ; 0.00
REMARK 3 TIGHT POSITIONAL 2 H (A): 2556 ; 0.03 ; 0.00
REMARK 3 TIGHT POSITIONAL 2 I (A): 2556 ; 0.03 ; 0.00
REMARK 3 TIGHT THERMAL 2 D (A**2): 2556 ; 0.06 ; 0.50
REMARK 3 TIGHT THERMAL 2 E (A**2): 2556 ; 0.06 ; 0.00
REMARK 3 TIGHT THERMAL 2 F (A**2): 2556 ; 0.06 ; 0.00
REMARK 3 TIGHT THERMAL 2 G (A**2): 2556 ; 0.06 ; 0.00
REMARK 3 TIGHT THERMAL 2 H (A**2): 2556 ; 0.06 ; 0.00
REMARK 3 TIGHT THERMAL 2 I (A**2): 2556 ; 0.05 ; 0.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 331
REMARK 3 ORIGIN FOR THE GROUP (A): -64.5800 32.0550 49.0260
REMARK 3 T TENSOR
REMARK 3 T11: -0.3979 T22: -0.3165
REMARK 3 T33: -0.3991 T12: -0.0038
REMARK 3 T13: -0.0971 T23: -0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 2.3822 L22: 6.7304
REMARK 3 L33: 5.9162 L12: 1.0388
REMARK 3 L13: -0.6126 L23: 0.9364
REMARK 3 S TENSOR
REMARK 3 S11: 0.0349 S12: 0.0245 S13: 0.0079
REMARK 3 S21: 0.0754 S22: -0.4927 S23: 0.4979
REMARK 3 S31: -0.0964 S32: -0.3354 S33: 0.4578
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 331
REMARK 3 ORIGIN FOR THE GROUP (A): -47.0860 1.7160 90.3010
REMARK 3 T TENSOR
REMARK 3 T11: -0.4019 T22: -0.2835
REMARK 3 T33: -0.4067 T12: -0.0087
REMARK 3 T13: 0.0517 T23: 0.0470
REMARK 3 L TENSOR
REMARK 3 L11: 6.1492 L22: 2.7414
REMARK 3 L33: 5.9293 L12: -1.4667
REMARK 3 L13: -0.3666 L23: 0.9379
REMARK 3 S TENSOR
REMARK 3 S11: -0.3279 S12: 0.2592 S13: -0.3759
REMARK 3 S21: 0.2029 S22: -0.1359 S23: 0.2672
REMARK 3 S31: 0.3760 S32: -0.0897 S33: 0.4638
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 3 C 331
REMARK 3 ORIGIN FOR THE GROUP (A): -17.5060 15.7390 20.6460
REMARK 3 T TENSOR
REMARK 3 T11: -0.3864 T22: -0.3196
REMARK 3 T33: -0.4005 T12: -0.0051
REMARK 3 T13: -0.0003 T23: -0.0912
REMARK 3 L TENSOR
REMARK 3 L11: 4.7241 L22: 4.4566
REMARK 3 L33: 6.1158 L12: 2.2899
REMARK 3 L13: 0.9343 L23: -0.2359
REMARK 3 S TENSOR
REMARK 3 S11: -0.4166 S12: -0.1774 S13: 0.4285
REMARK 3 S21: -0.2484 S22: -0.0603 S23: 0.2251
REMARK 3 S31: -0.2450 S32: -0.2457 S33: 0.4769
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 3 D 331
REMARK 3 ORIGIN FOR THE GROUP (A): -56.9540 42.6270 82.3620
REMARK 3 T TENSOR
REMARK 3 T11: -0.2900 T22: -0.2023
REMARK 3 T33: -0.3673 T12: -0.0542
REMARK 3 T13: -0.2055 T23: -0.0594
REMARK 3 L TENSOR
REMARK 3 L11: 4.1630 L22: 4.2139
REMARK 3 L33: 6.1668 L12: 1.9255
REMARK 3 L13: -0.2310 L23: -1.0027
REMARK 3 S TENSOR
REMARK 3 S11: -0.1733 S12: -0.1094 S13: 0.3597
REMARK 3 S21: 0.0401 S22: -0.1456 S23: -0.0942
REMARK 3 S31: -0.8544 S32: 0.1453 S33: 0.3189
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 3 E 331
REMARK 3 ORIGIN FOR THE GROUP (A): -61.9010 52.7590 12.7050
REMARK 3 T TENSOR
REMARK 3 T11: -0.2418 T22: -0.2454
REMARK 3 T33: -0.4051 T12: 0.0310
REMARK 3 T13: 0.0285 T23: 0.1895
REMARK 3 L TENSOR
REMARK 3 L11: 2.6387 L22: 5.8521
REMARK 3 L33: 6.2065 L12: -0.8419
REMARK 3 L13: -0.9791 L23: 0.3402
REMARK 3 S TENSOR
REMARK 3 S11: -0.1488 S12: -0.0888 S13: -0.2469
REMARK 3 S21: 0.1099 S22: -0.2050 S23: -0.2933
REMARK 3 S31: 0.6057 S32: 0.7008 S33: 0.3538
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 3 F 331
REMARK 3 ORIGIN FOR THE GROUP (A): -34.1110 3.0650 56.9470
REMARK 3 T TENSOR
REMARK 3 T11: -0.3300 T22: -0.1608
REMARK 3 T33: -0.4066 T12: -0.0388
REMARK 3 T13: 0.1333 T23: 0.1324
REMARK 3 L TENSOR
REMARK 3 L11: 5.9481 L22: 2.3852
REMARK 3 L33: 6.4894 L12: 0.8256
REMARK 3 L13: 0.7721 L23: -0.5839
REMARK 3 S TENSOR
REMARK 3 S11: -0.2209 S12: 0.0728 S13: -0.1199
REMARK 3 S21: -0.1386 S22: -0.1401 S23: -0.3570
REMARK 3 S31: 0.2920 S32: 0.8410 S33: 0.3611
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 3 G 331
REMARK 3 ORIGIN FOR THE GROUP (A): -15.0040 61.4830 86.8490
REMARK 3 T TENSOR
REMARK 3 T11: -0.2345 T22: 0.1827
REMARK 3 T33: -0.3446 T12: -0.1288
REMARK 3 T13: 0.0500 T23: -0.0792
REMARK 3 L TENSOR
REMARK 3 L11: 7.2916 L22: 6.4943
REMARK 3 L33: 4.3723 L12: 5.1900
REMARK 3 L13: -2.7144 L23: -1.7273
REMARK 3 S TENSOR
REMARK 3 S11: -0.5235 S12: 0.6022 S13: -0.3114
REMARK 3 S21: -0.2810 S22: 0.5110 S23: -0.0930
REMARK 3 S31: 0.1764 S32: -0.2000 S33: 0.0125
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 3 H 331
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1880 29.9970 52.4650
REMARK 3 T TENSOR
REMARK 3 T11: -0.0867 T22: 0.0237
REMARK 3 T33: -0.3220 T12: -0.2338
REMARK 3 T13: 0.0280 T23: -0.0587
REMARK 3 L TENSOR
REMARK 3 L11: 10.9746 L22: 2.4060
REMARK 3 L33: 4.3517 L12: 2.4148
REMARK 3 L13: 2.6005 L23: 1.4047
REMARK 3 S TENSOR
REMARK 3 S11: 0.3486 S12: -0.7246 S13: 0.2249
REMARK 3 S21: 0.0725 S22: -0.3533 S23: 0.2538
REMARK 3 S31: 0.0383 S32: -0.1619 S33: 0.0046
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 3 I 331
REMARK 3 ORIGIN FOR THE GROUP (A): -66.5790 6.9770 17.1820
REMARK 3 T TENSOR
REMARK 3 T11: 0.1361 T22: -0.1946
REMARK 3 T33: -0.3292 T12: -0.0998
REMARK 3 T13: -0.0927 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 2.5209 L22: 11.0787
REMARK 3 L33: 4.2699 L12: -2.3605
REMARK 3 L13: -0.0754 L23: 3.0581
REMARK 3 S TENSOR
REMARK 3 S11: 0.0926 S12: -0.0912 S13: 0.0705
REMARK 3 S21: -0.9070 S22: -0.0832 S23: 0.3329
REMARK 3 S31: -0.2096 S32: -0.0189 S33: -0.0094
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2O7U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-06.
REMARK 100 THE DEPOSITION ID IS D_1000040796.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83306
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 48.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.40600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: WILD TYPE TRANSFERRIN. PDB ENTRY CODE 1A8E.
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 35MG/ML, 0.1M AMMONIUM
REMARK 280 BICARBONATE. WELL: 20% PEG 3350, 0.2 M POTASSIUM ACETATE, PH 7.4,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 84.73100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.94850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.73100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 48.94850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H
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: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I
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 VAL B 1
REMARK 465 PRO B 2
REMARK 465 PRO B 332
REMARK 465 GLU B 333
REMARK 465 ALA B 334
REMARK 465 PRO B 335
REMARK 465 THR B 336
REMARK 465 ASP B 337
REMARK 465 VAL A 1
REMARK 465 PRO A 2
REMARK 465 PRO A 332
REMARK 465 GLU A 333
REMARK 465 ALA A 334
REMARK 465 PRO A 335
REMARK 465 THR A 336
REMARK 465 ASP A 337
REMARK 465 VAL C 1
REMARK 465 PRO C 2
REMARK 465 PRO C 332
REMARK 465 GLU C 333
REMARK 465 ALA C 334
REMARK 465 PRO C 335
REMARK 465 THR C 336
REMARK 465 ASP C 337
REMARK 465 VAL D 1
REMARK 465 PRO D 2
REMARK 465 PRO D 332
REMARK 465 GLU D 333
REMARK 465 ALA D 334
REMARK 465 PRO D 335
REMARK 465 THR D 336
REMARK 465 ASP D 337
REMARK 465 VAL E 1
REMARK 465 PRO E 2
REMARK 465 PRO E 332
REMARK 465 GLU E 333
REMARK 465 ALA E 334
REMARK 465 PRO E 335
REMARK 465 THR E 336
REMARK 465 ASP E 337
REMARK 465 VAL F 1
REMARK 465 PRO F 2
REMARK 465 PRO F 332
REMARK 465 GLU F 333
REMARK 465 ALA F 334
REMARK 465 PRO F 335
REMARK 465 THR F 336
REMARK 465 ASP F 337
REMARK 465 VAL G 1
REMARK 465 PRO G 2
REMARK 465 PRO G 332
REMARK 465 GLU G 333
REMARK 465 ALA G 334
REMARK 465 PRO G 335
REMARK 465 THR G 336
REMARK 465 ASP G 337
REMARK 465 VAL H 1
REMARK 465 PRO H 2
REMARK 465 PRO H 332
REMARK 465 GLU H 333
REMARK 465 ALA H 334
REMARK 465 PRO H 335
REMARK 465 THR H 336
REMARK 465 ASP H 337
REMARK 465 VAL I 1
REMARK 465 PRO I 2
REMARK 465 PRO I 332
REMARK 465 GLU I 333
REMARK 465 ALA I 334
REMARK 465 PRO I 335
REMARK 465 THR I 336
REMARK 465 ASP I 337
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 OE1 GLU F 206 O HOH F 604 2.17
REMARK 500 OE1 GLU D 206 O HOH D 607 2.18
REMARK 500 O GLU A 89 OH TYR I 71 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O GLU A 141 OG1 THR F 330 3455 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLU A 206 CA - CB - CG ANGL. DEV. = 14.1 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 SER B 12 177.07 86.86
REMARK 500 TYR B 85 -160.96 -113.82
REMARK 500 ASP B 90 75.90 -151.01
REMARK 500 THR B 93 31.22 -99.49
REMARK 500 ASP B 104 83.56 67.74
REMARK 500 SER B 105 23.36 -162.47
REMARK 500 ASN B 110 1.02 -62.41
REMARK 500 SER B 125 -72.67 -59.99
REMARK 500 TRP B 128 -65.57 -137.33
REMARK 500 SER B 155 53.64 -111.40
REMARK 500 CYS B 161 -9.65 83.57
REMARK 500 CYS B 177 56.30 38.31
REMARK 500 CYS B 179 41.94 -106.89
REMARK 500 VAL B 205 -153.35 -137.26
REMARK 500 ASP B 221 -7.94 -56.09
REMARK 500 ASP B 229 27.01 -74.46
REMARK 500 ALA B 244 156.32 179.58
REMARK 500 ASP B 277 61.81 21.83
REMARK 500 LYS B 278 -103.26 -108.39
REMARK 500 LYS B 280 -38.45 -38.70
REMARK 500 GLU B 281 -84.38 -63.20
REMARK 500 LEU B 294 -31.47 62.07
REMARK 500 ASN B 325 4.64 -61.09
REMARK 500 ARG B 327 -33.24 -150.19
REMARK 500 GLU B 328 -57.08 -126.34
REMARK 500 THR B 330 -175.88 -59.58
REMARK 500 SER A 12 179.44 84.44
REMARK 500 TYR A 85 -164.59 -116.99
REMARK 500 ASP A 90 74.27 -152.61
REMARK 500 ASP A 104 82.23 65.50
REMARK 500 SER A 105 25.36 -160.16
REMARK 500 PHE A 107 161.24 -47.61
REMARK 500 ASN A 110 1.05 -62.49
REMARK 500 SER A 125 -72.58 -61.24
REMARK 500 TRP A 128 -63.95 -136.78
REMARK 500 SER A 155 50.52 -109.75
REMARK 500 CYS A 161 -11.22 81.51
REMARK 500 ASP A 221 -8.41 -54.90
REMARK 500 ASP A 229 27.45 -75.23
REMARK 500 ASP A 277 62.87 24.16
REMARK 500 LYS A 278 -104.00 -109.46
REMARK 500 GLU A 281 -83.36 -66.81
REMARK 500 LEU A 294 -34.00 63.89
REMARK 500 ASN A 325 3.63 -59.09
REMARK 500 ARG A 327 -32.71 -150.24
REMARK 500 GLU A 328 -57.20 -126.64
REMARK 500 THR A 330 -176.06 -59.72
REMARK 500 SER C 12 -179.56 86.34
REMARK 500 TYR C 85 -161.87 -114.05
REMARK 500 ASP C 90 73.92 -150.98
REMARK 500
REMARK 500 THIS ENTRY HAS 182 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 63 OD1
REMARK 620 2 TYR B 95 OH 91.8
REMARK 620 3 TYR B 188 OH 167.7 86.3
REMARK 620 4 HIS B 249 NE2 95.9 92.9 96.3
REMARK 620 5 CO3 B 600 O2 83.9 159.9 93.7 107.1
REMARK 620 6 CO3 B 600 O3 87.6 100.6 80.8 165.9 59.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 63 OD1
REMARK 620 2 TYR A 95 OH 93.6
REMARK 620 3 TYR A 188 OH 165.4 80.5
REMARK 620 4 HIS A 249 NE2 96.9 90.1 96.4
REMARK 620 5 CO3 A 600 O3 89.7 99.3 78.2 168.1
REMARK 620 6 CO3 A 600 O2 85.1 158.4 95.5 111.4 59.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE C 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 63 OD1
REMARK 620 2 TYR C 95 OH 88.3
REMARK 620 3 TYR C 188 OH 164.9 84.0
REMARK 620 4 HIS C 249 NE2 95.2 93.8 98.2
REMARK 620 5 CO3 C 600 O2 86.6 155.5 95.0 110.5
REMARK 620 6 CO3 C 600 O3 88.9 96.4 79.1 169.1 59.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE D 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 63 OD1
REMARK 620 2 TYR D 95 OH 93.4
REMARK 620 3 TYR D 188 OH 171.5 93.7
REMARK 620 4 HIS D 249 NE2 102.2 95.2 81.8
REMARK 620 5 CO3 D 600 O2 83.2 152.8 88.4 111.9
REMARK 620 6 CO3 D 600 O3 85.4 94.8 89.3 167.0 58.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE E 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 63 OD1
REMARK 620 2 TYR E 95 OH 90.4
REMARK 620 3 TYR E 188 OH 170.6 91.9
REMARK 620 4 HIS E 249 NE2 102.6 98.5 86.1
REMARK 620 5 CO3 E 600 O3 85.3 90.6 85.5 167.9
REMARK 620 6 CO3 E 600 O2 89.1 149.0 84.3 111.8 58.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE F 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 63 OD1
REMARK 620 2 TYR F 95 OH 93.9
REMARK 620 3 TYR F 188 OH 170.7 90.9
REMARK 620 4 HIS F 249 NE2 102.3 96.5 85.0
REMARK 620 5 CO3 F 600 O2 87.3 151.4 84.7 111.1
REMARK 620 6 CO3 F 600 O3 85.6 92.6 86.3 167.5 59.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE G 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 63 OD1
REMARK 620 2 TYR G 95 OH 87.8
REMARK 620 3 TYR G 188 OH 175.5 94.9
REMARK 620 4 HIS G 249 NE2 103.2 95.2 80.2
REMARK 620 5 CO3 G 600 O2 87.3 150.2 88.6 114.6
REMARK 620 6 CO3 G 600 O3 80.7 91.7 95.6 172.2 58.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE H 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 63 OD1
REMARK 620 2 TYR H 95 OH 90.2
REMARK 620 3 TYR H 188 OH 174.2 90.9
REMARK 620 4 HIS H 249 NE2 105.0 93.6 80.6
REMARK 620 5 CO3 H 600 O2 88.6 151.0 87.7 114.7
REMARK 620 6 CO3 H 600 O3 82.4 92.2 91.9 170.6 58.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE I 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 63 OD1
REMARK 620 2 TYR I 95 OH 88.9
REMARK 620 3 TYR I 188 OH 173.5 88.8
REMARK 620 4 HIS I 249 NE2 103.4 94.3 82.8
REMARK 620 5 CO3 I 600 O3 83.1 87.5 90.7 173.2
REMARK 620 6 CO3 I 600 O2 87.5 146.8 91.1 118.6 59.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 D 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE E 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 E 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE F 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 F 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE G 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 G 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE H 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 H 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE I 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 I 600
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A8E RELATED DB: PDB
REMARK 900 RELATED ID: 1FQF RELATED DB: PDB
REMARK 900 RELATED ID: 1FQE RELATED DB: PDB
REMARK 900 RELATED ID: 1EH3 RELATED DB: PDB
REMARK 900 RELATED ID: 1H43 RELATED DB: PDB
REMARK 900 RELATED ID: 1H45 RELATED DB: PDB
REMARK 900 RELATED ID: 2O84 RELATED DB: PDB
DBREF 2O7U B 1 337 UNP P02787 TRFE_HUMAN 20 356
DBREF 2O7U A 1 337 UNP P02787 TRFE_HUMAN 20 356
DBREF 2O7U C 1 337 UNP P02787 TRFE_HUMAN 20 356
DBREF 2O7U D 1 337 UNP P02787 TRFE_HUMAN 20 356
DBREF 2O7U E 1 337 UNP P02787 TRFE_HUMAN 20 356
DBREF 2O7U F 1 337 UNP P02787 TRFE_HUMAN 20 356
DBREF 2O7U G 1 337 UNP P02787 TRFE_HUMAN 20 356
DBREF 2O7U H 1 337 UNP P02787 TRFE_HUMAN 20 356
DBREF 2O7U I 1 337 UNP P02787 TRFE_HUMAN 20 356
SEQADV 2O7U GLU B 206 UNP P02787 LYS 225 ENGINEERED MUTATION
SEQADV 2O7U GLU B 296 UNP P02787 LYS 315 ENGINEERED MUTATION
SEQADV 2O7U GLU A 206 UNP P02787 LYS 225 ENGINEERED MUTATION
SEQADV 2O7U GLU A 296 UNP P02787 LYS 315 ENGINEERED MUTATION
SEQADV 2O7U GLU C 206 UNP P02787 LYS 225 ENGINEERED MUTATION
SEQADV 2O7U GLU C 296 UNP P02787 LYS 315 ENGINEERED MUTATION
SEQADV 2O7U GLU D 206 UNP P02787 LYS 225 ENGINEERED MUTATION
SEQADV 2O7U GLU D 296 UNP P02787 LYS 315 ENGINEERED MUTATION
SEQADV 2O7U GLU E 206 UNP P02787 LYS 225 ENGINEERED MUTATION
SEQADV 2O7U GLU E 296 UNP P02787 LYS 315 ENGINEERED MUTATION
SEQADV 2O7U GLU F 206 UNP P02787 LYS 225 ENGINEERED MUTATION
SEQADV 2O7U GLU F 296 UNP P02787 LYS 315 ENGINEERED MUTATION
SEQADV 2O7U GLU G 206 UNP P02787 LYS 225 ENGINEERED MUTATION
SEQADV 2O7U GLU G 296 UNP P02787 LYS 315 ENGINEERED MUTATION
SEQADV 2O7U GLU H 206 UNP P02787 LYS 225 ENGINEERED MUTATION
SEQADV 2O7U GLU H 296 UNP P02787 LYS 315 ENGINEERED MUTATION
SEQADV 2O7U GLU I 206 UNP P02787 LYS 225 ENGINEERED MUTATION
SEQADV 2O7U GLU I 296 UNP P02787 LYS 315 ENGINEERED MUTATION
SEQRES 1 B 337 VAL PRO ASP LYS THR VAL ARG TRP CYS ALA VAL SER GLU
SEQRES 2 B 337 HIS GLU ALA THR LYS CYS GLN SER PHE ARG ASP HIS MET
SEQRES 3 B 337 LYS SER VAL ILE PRO SER ASP GLY PRO SER VAL ALA CYS
SEQRES 4 B 337 VAL LYS LYS ALA SER TYR LEU ASP CYS ILE ARG ALA ILE
SEQRES 5 B 337 ALA ALA ASN GLU ALA ASP ALA VAL THR LEU ASP ALA GLY
SEQRES 6 B 337 LEU VAL TYR ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS
SEQRES 7 B 337 PRO VAL VAL ALA GLU PHE TYR GLY SER LYS GLU ASP PRO
SEQRES 8 B 337 GLN THR PHE TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP
SEQRES 9 B 337 SER GLY PHE GLN MET ASN GLN LEU ARG GLY LYS LYS SER
SEQRES 10 B 337 CYS HIS THR GLY LEU GLY ARG SER ALA GLY TRP ASN ILE
SEQRES 11 B 337 PRO ILE GLY LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG
SEQRES 12 B 337 LYS PRO LEU GLU LYS ALA VAL ALA ASN PHE PHE SER GLY
SEQRES 13 B 337 SER CYS ALA PRO CYS ALA ASP GLY THR ASP PHE PRO GLN
SEQRES 14 B 337 LEU CYS GLN LEU CYS PRO GLY CYS GLY CYS SER THR LEU
SEQRES 15 B 337 ASN GLN TYR PHE GLY TYR SER GLY ALA PHE LYS CYS LEU
SEQRES 16 B 337 LYS ASP GLY ALA GLY ASP VAL ALA PHE VAL GLU HIS SER
SEQRES 17 B 337 THR ILE PHE GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP
SEQRES 18 B 337 GLN TYR GLU LEU LEU CYS LEU ASP ASN THR ARG LYS PRO
SEQRES 19 B 337 VAL ASP GLU TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO
SEQRES 20 B 337 SER HIS THR VAL VAL ALA ARG SER MET GLY GLY LYS GLU
SEQRES 21 B 337 ASP LEU ILE TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS
SEQRES 22 B 337 PHE GLY LYS ASP LYS SER LYS GLU PHE GLN LEU PHE SER
SEQRES 23 B 337 SER PRO HIS GLY LYS ASP LEU LEU PHE GLU ASP SER ALA
SEQRES 24 B 337 HIS GLY PHE LEU LYS VAL PRO PRO ARG MET ASP ALA LYS
SEQRES 25 B 337 MET TYR LEU GLY TYR GLU TYR VAL THR ALA ILE ARG ASN
SEQRES 26 B 337 LEU ARG GLU GLY THR CYS PRO GLU ALA PRO THR ASP
SEQRES 1 A 337 VAL PRO ASP LYS THR VAL ARG TRP CYS ALA VAL SER GLU
SEQRES 2 A 337 HIS GLU ALA THR LYS CYS GLN SER PHE ARG ASP HIS MET
SEQRES 3 A 337 LYS SER VAL ILE PRO SER ASP GLY PRO SER VAL ALA CYS
SEQRES 4 A 337 VAL LYS LYS ALA SER TYR LEU ASP CYS ILE ARG ALA ILE
SEQRES 5 A 337 ALA ALA ASN GLU ALA ASP ALA VAL THR LEU ASP ALA GLY
SEQRES 6 A 337 LEU VAL TYR ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS
SEQRES 7 A 337 PRO VAL VAL ALA GLU PHE TYR GLY SER LYS GLU ASP PRO
SEQRES 8 A 337 GLN THR PHE TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP
SEQRES 9 A 337 SER GLY PHE GLN MET ASN GLN LEU ARG GLY LYS LYS SER
SEQRES 10 A 337 CYS HIS THR GLY LEU GLY ARG SER ALA GLY TRP ASN ILE
SEQRES 11 A 337 PRO ILE GLY LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG
SEQRES 12 A 337 LYS PRO LEU GLU LYS ALA VAL ALA ASN PHE PHE SER GLY
SEQRES 13 A 337 SER CYS ALA PRO CYS ALA ASP GLY THR ASP PHE PRO GLN
SEQRES 14 A 337 LEU CYS GLN LEU CYS PRO GLY CYS GLY CYS SER THR LEU
SEQRES 15 A 337 ASN GLN TYR PHE GLY TYR SER GLY ALA PHE LYS CYS LEU
SEQRES 16 A 337 LYS ASP GLY ALA GLY ASP VAL ALA PHE VAL GLU HIS SER
SEQRES 17 A 337 THR ILE PHE GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP
SEQRES 18 A 337 GLN TYR GLU LEU LEU CYS LEU ASP ASN THR ARG LYS PRO
SEQRES 19 A 337 VAL ASP GLU TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO
SEQRES 20 A 337 SER HIS THR VAL VAL ALA ARG SER MET GLY GLY LYS GLU
SEQRES 21 A 337 ASP LEU ILE TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS
SEQRES 22 A 337 PHE GLY LYS ASP LYS SER LYS GLU PHE GLN LEU PHE SER
SEQRES 23 A 337 SER PRO HIS GLY LYS ASP LEU LEU PHE GLU ASP SER ALA
SEQRES 24 A 337 HIS GLY PHE LEU LYS VAL PRO PRO ARG MET ASP ALA LYS
SEQRES 25 A 337 MET TYR LEU GLY TYR GLU TYR VAL THR ALA ILE ARG ASN
SEQRES 26 A 337 LEU ARG GLU GLY THR CYS PRO GLU ALA PRO THR ASP
SEQRES 1 C 337 VAL PRO ASP LYS THR VAL ARG TRP CYS ALA VAL SER GLU
SEQRES 2 C 337 HIS GLU ALA THR LYS CYS GLN SER PHE ARG ASP HIS MET
SEQRES 3 C 337 LYS SER VAL ILE PRO SER ASP GLY PRO SER VAL ALA CYS
SEQRES 4 C 337 VAL LYS LYS ALA SER TYR LEU ASP CYS ILE ARG ALA ILE
SEQRES 5 C 337 ALA ALA ASN GLU ALA ASP ALA VAL THR LEU ASP ALA GLY
SEQRES 6 C 337 LEU VAL TYR ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS
SEQRES 7 C 337 PRO VAL VAL ALA GLU PHE TYR GLY SER LYS GLU ASP PRO
SEQRES 8 C 337 GLN THR PHE TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP
SEQRES 9 C 337 SER GLY PHE GLN MET ASN GLN LEU ARG GLY LYS LYS SER
SEQRES 10 C 337 CYS HIS THR GLY LEU GLY ARG SER ALA GLY TRP ASN ILE
SEQRES 11 C 337 PRO ILE GLY LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG
SEQRES 12 C 337 LYS PRO LEU GLU LYS ALA VAL ALA ASN PHE PHE SER GLY
SEQRES 13 C 337 SER CYS ALA PRO CYS ALA ASP GLY THR ASP PHE PRO GLN
SEQRES 14 C 337 LEU CYS GLN LEU CYS PRO GLY CYS GLY CYS SER THR LEU
SEQRES 15 C 337 ASN GLN TYR PHE GLY TYR SER GLY ALA PHE LYS CYS LEU
SEQRES 16 C 337 LYS ASP GLY ALA GLY ASP VAL ALA PHE VAL GLU HIS SER
SEQRES 17 C 337 THR ILE PHE GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP
SEQRES 18 C 337 GLN TYR GLU LEU LEU CYS LEU ASP ASN THR ARG LYS PRO
SEQRES 19 C 337 VAL ASP GLU TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO
SEQRES 20 C 337 SER HIS THR VAL VAL ALA ARG SER MET GLY GLY LYS GLU
SEQRES 21 C 337 ASP LEU ILE TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS
SEQRES 22 C 337 PHE GLY LYS ASP LYS SER LYS GLU PHE GLN LEU PHE SER
SEQRES 23 C 337 SER PRO HIS GLY LYS ASP LEU LEU PHE GLU ASP SER ALA
SEQRES 24 C 337 HIS GLY PHE LEU LYS VAL PRO PRO ARG MET ASP ALA LYS
SEQRES 25 C 337 MET TYR LEU GLY TYR GLU TYR VAL THR ALA ILE ARG ASN
SEQRES 26 C 337 LEU ARG GLU GLY THR CYS PRO GLU ALA PRO THR ASP
SEQRES 1 D 337 VAL PRO ASP LYS THR VAL ARG TRP CYS ALA VAL SER GLU
SEQRES 2 D 337 HIS GLU ALA THR LYS CYS GLN SER PHE ARG ASP HIS MET
SEQRES 3 D 337 LYS SER VAL ILE PRO SER ASP GLY PRO SER VAL ALA CYS
SEQRES 4 D 337 VAL LYS LYS ALA SER TYR LEU ASP CYS ILE ARG ALA ILE
SEQRES 5 D 337 ALA ALA ASN GLU ALA ASP ALA VAL THR LEU ASP ALA GLY
SEQRES 6 D 337 LEU VAL TYR ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS
SEQRES 7 D 337 PRO VAL VAL ALA GLU PHE TYR GLY SER LYS GLU ASP PRO
SEQRES 8 D 337 GLN THR PHE TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP
SEQRES 9 D 337 SER GLY PHE GLN MET ASN GLN LEU ARG GLY LYS LYS SER
SEQRES 10 D 337 CYS HIS THR GLY LEU GLY ARG SER ALA GLY TRP ASN ILE
SEQRES 11 D 337 PRO ILE GLY LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG
SEQRES 12 D 337 LYS PRO LEU GLU LYS ALA VAL ALA ASN PHE PHE SER GLY
SEQRES 13 D 337 SER CYS ALA PRO CYS ALA ASP GLY THR ASP PHE PRO GLN
SEQRES 14 D 337 LEU CYS GLN LEU CYS PRO GLY CYS GLY CYS SER THR LEU
SEQRES 15 D 337 ASN GLN TYR PHE GLY TYR SER GLY ALA PHE LYS CYS LEU
SEQRES 16 D 337 LYS ASP GLY ALA GLY ASP VAL ALA PHE VAL GLU HIS SER
SEQRES 17 D 337 THR ILE PHE GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP
SEQRES 18 D 337 GLN TYR GLU LEU LEU CYS LEU ASP ASN THR ARG LYS PRO
SEQRES 19 D 337 VAL ASP GLU TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO
SEQRES 20 D 337 SER HIS THR VAL VAL ALA ARG SER MET GLY GLY LYS GLU
SEQRES 21 D 337 ASP LEU ILE TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS
SEQRES 22 D 337 PHE GLY LYS ASP LYS SER LYS GLU PHE GLN LEU PHE SER
SEQRES 23 D 337 SER PRO HIS GLY LYS ASP LEU LEU PHE GLU ASP SER ALA
SEQRES 24 D 337 HIS GLY PHE LEU LYS VAL PRO PRO ARG MET ASP ALA LYS
SEQRES 25 D 337 MET TYR LEU GLY TYR GLU TYR VAL THR ALA ILE ARG ASN
SEQRES 26 D 337 LEU ARG GLU GLY THR CYS PRO GLU ALA PRO THR ASP
SEQRES 1 E 337 VAL PRO ASP LYS THR VAL ARG TRP CYS ALA VAL SER GLU
SEQRES 2 E 337 HIS GLU ALA THR LYS CYS GLN SER PHE ARG ASP HIS MET
SEQRES 3 E 337 LYS SER VAL ILE PRO SER ASP GLY PRO SER VAL ALA CYS
SEQRES 4 E 337 VAL LYS LYS ALA SER TYR LEU ASP CYS ILE ARG ALA ILE
SEQRES 5 E 337 ALA ALA ASN GLU ALA ASP ALA VAL THR LEU ASP ALA GLY
SEQRES 6 E 337 LEU VAL TYR ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS
SEQRES 7 E 337 PRO VAL VAL ALA GLU PHE TYR GLY SER LYS GLU ASP PRO
SEQRES 8 E 337 GLN THR PHE TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP
SEQRES 9 E 337 SER GLY PHE GLN MET ASN GLN LEU ARG GLY LYS LYS SER
SEQRES 10 E 337 CYS HIS THR GLY LEU GLY ARG SER ALA GLY TRP ASN ILE
SEQRES 11 E 337 PRO ILE GLY LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG
SEQRES 12 E 337 LYS PRO LEU GLU LYS ALA VAL ALA ASN PHE PHE SER GLY
SEQRES 13 E 337 SER CYS ALA PRO CYS ALA ASP GLY THR ASP PHE PRO GLN
SEQRES 14 E 337 LEU CYS GLN LEU CYS PRO GLY CYS GLY CYS SER THR LEU
SEQRES 15 E 337 ASN GLN TYR PHE GLY TYR SER GLY ALA PHE LYS CYS LEU
SEQRES 16 E 337 LYS ASP GLY ALA GLY ASP VAL ALA PHE VAL GLU HIS SER
SEQRES 17 E 337 THR ILE PHE GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP
SEQRES 18 E 337 GLN TYR GLU LEU LEU CYS LEU ASP ASN THR ARG LYS PRO
SEQRES 19 E 337 VAL ASP GLU TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO
SEQRES 20 E 337 SER HIS THR VAL VAL ALA ARG SER MET GLY GLY LYS GLU
SEQRES 21 E 337 ASP LEU ILE TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS
SEQRES 22 E 337 PHE GLY LYS ASP LYS SER LYS GLU PHE GLN LEU PHE SER
SEQRES 23 E 337 SER PRO HIS GLY LYS ASP LEU LEU PHE GLU ASP SER ALA
SEQRES 24 E 337 HIS GLY PHE LEU LYS VAL PRO PRO ARG MET ASP ALA LYS
SEQRES 25 E 337 MET TYR LEU GLY TYR GLU TYR VAL THR ALA ILE ARG ASN
SEQRES 26 E 337 LEU ARG GLU GLY THR CYS PRO GLU ALA PRO THR ASP
SEQRES 1 F 337 VAL PRO ASP LYS THR VAL ARG TRP CYS ALA VAL SER GLU
SEQRES 2 F 337 HIS GLU ALA THR LYS CYS GLN SER PHE ARG ASP HIS MET
SEQRES 3 F 337 LYS SER VAL ILE PRO SER ASP GLY PRO SER VAL ALA CYS
SEQRES 4 F 337 VAL LYS LYS ALA SER TYR LEU ASP CYS ILE ARG ALA ILE
SEQRES 5 F 337 ALA ALA ASN GLU ALA ASP ALA VAL THR LEU ASP ALA GLY
SEQRES 6 F 337 LEU VAL TYR ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS
SEQRES 7 F 337 PRO VAL VAL ALA GLU PHE TYR GLY SER LYS GLU ASP PRO
SEQRES 8 F 337 GLN THR PHE TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP
SEQRES 9 F 337 SER GLY PHE GLN MET ASN GLN LEU ARG GLY LYS LYS SER
SEQRES 10 F 337 CYS HIS THR GLY LEU GLY ARG SER ALA GLY TRP ASN ILE
SEQRES 11 F 337 PRO ILE GLY LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG
SEQRES 12 F 337 LYS PRO LEU GLU LYS ALA VAL ALA ASN PHE PHE SER GLY
SEQRES 13 F 337 SER CYS ALA PRO CYS ALA ASP GLY THR ASP PHE PRO GLN
SEQRES 14 F 337 LEU CYS GLN LEU CYS PRO GLY CYS GLY CYS SER THR LEU
SEQRES 15 F 337 ASN GLN TYR PHE GLY TYR SER GLY ALA PHE LYS CYS LEU
SEQRES 16 F 337 LYS ASP GLY ALA GLY ASP VAL ALA PHE VAL GLU HIS SER
SEQRES 17 F 337 THR ILE PHE GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP
SEQRES 18 F 337 GLN TYR GLU LEU LEU CYS LEU ASP ASN THR ARG LYS PRO
SEQRES 19 F 337 VAL ASP GLU TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO
SEQRES 20 F 337 SER HIS THR VAL VAL ALA ARG SER MET GLY GLY LYS GLU
SEQRES 21 F 337 ASP LEU ILE TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS
SEQRES 22 F 337 PHE GLY LYS ASP LYS SER LYS GLU PHE GLN LEU PHE SER
SEQRES 23 F 337 SER PRO HIS GLY LYS ASP LEU LEU PHE GLU ASP SER ALA
SEQRES 24 F 337 HIS GLY PHE LEU LYS VAL PRO PRO ARG MET ASP ALA LYS
SEQRES 25 F 337 MET TYR LEU GLY TYR GLU TYR VAL THR ALA ILE ARG ASN
SEQRES 26 F 337 LEU ARG GLU GLY THR CYS PRO GLU ALA PRO THR ASP
SEQRES 1 G 337 VAL PRO ASP LYS THR VAL ARG TRP CYS ALA VAL SER GLU
SEQRES 2 G 337 HIS GLU ALA THR LYS CYS GLN SER PHE ARG ASP HIS MET
SEQRES 3 G 337 LYS SER VAL ILE PRO SER ASP GLY PRO SER VAL ALA CYS
SEQRES 4 G 337 VAL LYS LYS ALA SER TYR LEU ASP CYS ILE ARG ALA ILE
SEQRES 5 G 337 ALA ALA ASN GLU ALA ASP ALA VAL THR LEU ASP ALA GLY
SEQRES 6 G 337 LEU VAL TYR ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS
SEQRES 7 G 337 PRO VAL VAL ALA GLU PHE TYR GLY SER LYS GLU ASP PRO
SEQRES 8 G 337 GLN THR PHE TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP
SEQRES 9 G 337 SER GLY PHE GLN MET ASN GLN LEU ARG GLY LYS LYS SER
SEQRES 10 G 337 CYS HIS THR GLY LEU GLY ARG SER ALA GLY TRP ASN ILE
SEQRES 11 G 337 PRO ILE GLY LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG
SEQRES 12 G 337 LYS PRO LEU GLU LYS ALA VAL ALA ASN PHE PHE SER GLY
SEQRES 13 G 337 SER CYS ALA PRO CYS ALA ASP GLY THR ASP PHE PRO GLN
SEQRES 14 G 337 LEU CYS GLN LEU CYS PRO GLY CYS GLY CYS SER THR LEU
SEQRES 15 G 337 ASN GLN TYR PHE GLY TYR SER GLY ALA PHE LYS CYS LEU
SEQRES 16 G 337 LYS ASP GLY ALA GLY ASP VAL ALA PHE VAL GLU HIS SER
SEQRES 17 G 337 THR ILE PHE GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP
SEQRES 18 G 337 GLN TYR GLU LEU LEU CYS LEU ASP ASN THR ARG LYS PRO
SEQRES 19 G 337 VAL ASP GLU TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO
SEQRES 20 G 337 SER HIS THR VAL VAL ALA ARG SER MET GLY GLY LYS GLU
SEQRES 21 G 337 ASP LEU ILE TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS
SEQRES 22 G 337 PHE GLY LYS ASP LYS SER LYS GLU PHE GLN LEU PHE SER
SEQRES 23 G 337 SER PRO HIS GLY LYS ASP LEU LEU PHE GLU ASP SER ALA
SEQRES 24 G 337 HIS GLY PHE LEU LYS VAL PRO PRO ARG MET ASP ALA LYS
SEQRES 25 G 337 MET TYR LEU GLY TYR GLU TYR VAL THR ALA ILE ARG ASN
SEQRES 26 G 337 LEU ARG GLU GLY THR CYS PRO GLU ALA PRO THR ASP
SEQRES 1 H 337 VAL PRO ASP LYS THR VAL ARG TRP CYS ALA VAL SER GLU
SEQRES 2 H 337 HIS GLU ALA THR LYS CYS GLN SER PHE ARG ASP HIS MET
SEQRES 3 H 337 LYS SER VAL ILE PRO SER ASP GLY PRO SER VAL ALA CYS
SEQRES 4 H 337 VAL LYS LYS ALA SER TYR LEU ASP CYS ILE ARG ALA ILE
SEQRES 5 H 337 ALA ALA ASN GLU ALA ASP ALA VAL THR LEU ASP ALA GLY
SEQRES 6 H 337 LEU VAL TYR ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS
SEQRES 7 H 337 PRO VAL VAL ALA GLU PHE TYR GLY SER LYS GLU ASP PRO
SEQRES 8 H 337 GLN THR PHE TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP
SEQRES 9 H 337 SER GLY PHE GLN MET ASN GLN LEU ARG GLY LYS LYS SER
SEQRES 10 H 337 CYS HIS THR GLY LEU GLY ARG SER ALA GLY TRP ASN ILE
SEQRES 11 H 337 PRO ILE GLY LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG
SEQRES 12 H 337 LYS PRO LEU GLU LYS ALA VAL ALA ASN PHE PHE SER GLY
SEQRES 13 H 337 SER CYS ALA PRO CYS ALA ASP GLY THR ASP PHE PRO GLN
SEQRES 14 H 337 LEU CYS GLN LEU CYS PRO GLY CYS GLY CYS SER THR LEU
SEQRES 15 H 337 ASN GLN TYR PHE GLY TYR SER GLY ALA PHE LYS CYS LEU
SEQRES 16 H 337 LYS ASP GLY ALA GLY ASP VAL ALA PHE VAL GLU HIS SER
SEQRES 17 H 337 THR ILE PHE GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP
SEQRES 18 H 337 GLN TYR GLU LEU LEU CYS LEU ASP ASN THR ARG LYS PRO
SEQRES 19 H 337 VAL ASP GLU TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO
SEQRES 20 H 337 SER HIS THR VAL VAL ALA ARG SER MET GLY GLY LYS GLU
SEQRES 21 H 337 ASP LEU ILE TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS
SEQRES 22 H 337 PHE GLY LYS ASP LYS SER LYS GLU PHE GLN LEU PHE SER
SEQRES 23 H 337 SER PRO HIS GLY LYS ASP LEU LEU PHE GLU ASP SER ALA
SEQRES 24 H 337 HIS GLY PHE LEU LYS VAL PRO PRO ARG MET ASP ALA LYS
SEQRES 25 H 337 MET TYR LEU GLY TYR GLU TYR VAL THR ALA ILE ARG ASN
SEQRES 26 H 337 LEU ARG GLU GLY THR CYS PRO GLU ALA PRO THR ASP
SEQRES 1 I 337 VAL PRO ASP LYS THR VAL ARG TRP CYS ALA VAL SER GLU
SEQRES 2 I 337 HIS GLU ALA THR LYS CYS GLN SER PHE ARG ASP HIS MET
SEQRES 3 I 337 LYS SER VAL ILE PRO SER ASP GLY PRO SER VAL ALA CYS
SEQRES 4 I 337 VAL LYS LYS ALA SER TYR LEU ASP CYS ILE ARG ALA ILE
SEQRES 5 I 337 ALA ALA ASN GLU ALA ASP ALA VAL THR LEU ASP ALA GLY
SEQRES 6 I 337 LEU VAL TYR ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS
SEQRES 7 I 337 PRO VAL VAL ALA GLU PHE TYR GLY SER LYS GLU ASP PRO
SEQRES 8 I 337 GLN THR PHE TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP
SEQRES 9 I 337 SER GLY PHE GLN MET ASN GLN LEU ARG GLY LYS LYS SER
SEQRES 10 I 337 CYS HIS THR GLY LEU GLY ARG SER ALA GLY TRP ASN ILE
SEQRES 11 I 337 PRO ILE GLY LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG
SEQRES 12 I 337 LYS PRO LEU GLU LYS ALA VAL ALA ASN PHE PHE SER GLY
SEQRES 13 I 337 SER CYS ALA PRO CYS ALA ASP GLY THR ASP PHE PRO GLN
SEQRES 14 I 337 LEU CYS GLN LEU CYS PRO GLY CYS GLY CYS SER THR LEU
SEQRES 15 I 337 ASN GLN TYR PHE GLY TYR SER GLY ALA PHE LYS CYS LEU
SEQRES 16 I 337 LYS ASP GLY ALA GLY ASP VAL ALA PHE VAL GLU HIS SER
SEQRES 17 I 337 THR ILE PHE GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP
SEQRES 18 I 337 GLN TYR GLU LEU LEU CYS LEU ASP ASN THR ARG LYS PRO
SEQRES 19 I 337 VAL ASP GLU TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO
SEQRES 20 I 337 SER HIS THR VAL VAL ALA ARG SER MET GLY GLY LYS GLU
SEQRES 21 I 337 ASP LEU ILE TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS
SEQRES 22 I 337 PHE GLY LYS ASP LYS SER LYS GLU PHE GLN LEU PHE SER
SEQRES 23 I 337 SER PRO HIS GLY LYS ASP LEU LEU PHE GLU ASP SER ALA
SEQRES 24 I 337 HIS GLY PHE LEU LYS VAL PRO PRO ARG MET ASP ALA LYS
SEQRES 25 I 337 MET TYR LEU GLY TYR GLU TYR VAL THR ALA ILE ARG ASN
SEQRES 26 I 337 LEU ARG GLU GLY THR CYS PRO GLU ALA PRO THR ASP
HET FE B 500 1
HET CO3 B 600 4
HET FE A 500 1
HET CO3 A 600 4
HET FE C 500 1
HET CO3 C 600 4
HET FE D 500 1
HET CO3 D 600 4
HET FE E 500 1
HET CO3 E 600 4
HET FE F 500 1
HET CO3 F 600 4
HET FE G 500 1
HET CO3 G 600 4
HET FE H 500 1
HET CO3 H 600 4
HET FE I 500 1
HET CO3 I 600 4
HETNAM FE FE (III) ION
HETNAM CO3 CARBONATE ION
FORMUL 10 FE 9(FE 3+)
FORMUL 11 CO3 9(C O3 2-)
FORMUL 28 HOH *72(H2 O)
HELIX 1 1 SER B 12 ILE B 30 1 19
HELIX 2 2 SER B 44 ALA B 54 1 11
HELIX 3 3 ASP B 63 LEU B 72 1 10
HELIX 4 4 GLN B 108 LEU B 112 5 5
HELIX 5 5 TRP B 128 TYR B 136 1 9
HELIX 6 6 CYS B 137 LEU B 139 5 3
HELIX 7 7 PRO B 145 PHE B 154 1 10
HELIX 8 8 PHE B 167 GLN B 172 5 6
HELIX 9 9 CYS B 174 GLY B 178 5 5
HELIX 10 10 PHE B 186 ASP B 197 1 12
HELIX 11 11 SER B 208 LEU B 214 1 7
HELIX 12 12 ASN B 216 ASP B 221 1 6
HELIX 13 13 LYS B 259 PHE B 274 1 16
HELIX 14 14 ASP B 310 GLY B 316 1 7
HELIX 15 15 GLY B 316 ASN B 325 1 10
HELIX 16 16 SER A 12 ILE A 30 1 19
HELIX 17 17 SER A 44 ALA A 54 1 11
HELIX 18 18 ASP A 63 LEU A 72 1 10
HELIX 19 19 GLN A 108 LEU A 112 5 5
HELIX 20 20 TRP A 128 TYR A 136 1 9
HELIX 21 21 CYS A 137 LEU A 139 5 3
HELIX 22 22 PRO A 145 PHE A 154 1 10
HELIX 23 23 PHE A 167 GLN A 172 5 6
HELIX 24 24 CYS A 174 GLY A 178 5 5
HELIX 25 25 PHE A 186 ASP A 197 1 12
HELIX 26 26 SER A 208 LEU A 214 1 7
HELIX 27 27 ASN A 216 ASP A 221 1 6
HELIX 28 28 LYS A 259 PHE A 274 1 16
HELIX 29 29 ASP A 310 GLY A 316 1 7
HELIX 30 30 GLY A 316 ASN A 325 1 10
HELIX 31 31 SER C 12 ILE C 30 1 19
HELIX 32 32 SER C 44 ALA C 54 1 11
HELIX 33 33 ASP C 63 LEU C 72 1 10
HELIX 34 34 GLN C 108 LEU C 112 5 5
HELIX 35 35 TRP C 128 TYR C 136 1 9
HELIX 36 36 CYS C 137 LEU C 139 5 3
HELIX 37 37 PRO C 145 PHE C 154 1 10
HELIX 38 38 PHE C 167 GLN C 172 5 6
HELIX 39 39 CYS C 174 GLY C 178 5 5
HELIX 40 40 PHE C 186 ASP C 197 1 12
HELIX 41 41 SER C 208 LEU C 214 1 7
HELIX 42 42 ASN C 216 ASP C 221 1 6
HELIX 43 43 LYS C 259 PHE C 274 1 16
HELIX 44 44 ASP C 310 GLY C 316 1 7
HELIX 45 45 GLY C 316 ASN C 325 1 10
HELIX 46 46 SER D 12 ILE D 30 1 19
HELIX 47 47 SER D 44 ALA D 54 1 11
HELIX 48 48 ASP D 63 LEU D 72 1 10
HELIX 49 49 GLN D 108 LEU D 112 5 5
HELIX 50 50 TRP D 128 TYR D 136 1 9
HELIX 51 51 CYS D 137 LEU D 139 5 3
HELIX 52 52 PRO D 145 PHE D 154 1 10
HELIX 53 53 PHE D 167 GLN D 172 5 6
HELIX 54 54 PHE D 186 ASP D 197 1 12
HELIX 55 55 SER D 208 ASN D 213 1 6
HELIX 56 56 ASN D 216 ASP D 221 1 6
HELIX 57 57 ASP D 236 CYS D 241 5 6
HELIX 58 58 LYS D 259 GLY D 275 1 17
HELIX 59 59 ASP D 310 GLY D 316 1 7
HELIX 60 60 GLY D 316 LEU D 326 1 11
HELIX 61 61 SER E 12 ILE E 30 1 19
HELIX 62 62 SER E 44 ALA E 54 1 11
HELIX 63 63 ASP E 63 LEU E 72 1 10
HELIX 64 64 GLN E 108 LEU E 112 5 5
HELIX 65 65 TRP E 128 TYR E 136 1 9
HELIX 66 66 CYS E 137 LEU E 139 5 3
HELIX 67 67 PRO E 145 PHE E 154 1 10
HELIX 68 68 PHE E 167 GLN E 172 5 6
HELIX 69 69 PHE E 186 ASP E 197 1 12
HELIX 70 70 SER E 208 ASN E 213 1 6
HELIX 71 71 ASN E 216 ASP E 221 1 6
HELIX 72 72 ASP E 236 CYS E 241 5 6
HELIX 73 73 LYS E 259 GLY E 275 1 17
HELIX 74 74 ASP E 310 GLY E 316 1 7
HELIX 75 75 GLY E 316 LEU E 326 1 11
HELIX 76 76 SER F 12 ILE F 30 1 19
HELIX 77 77 SER F 44 ALA F 54 1 11
HELIX 78 78 ASP F 63 LEU F 72 1 10
HELIX 79 79 GLN F 108 LEU F 112 5 5
HELIX 80 80 TRP F 128 TYR F 136 1 9
HELIX 81 81 CYS F 137 LEU F 139 5 3
HELIX 82 82 PRO F 145 PHE F 154 1 10
HELIX 83 83 PHE F 167 GLN F 172 5 6
HELIX 84 84 PHE F 186 ASP F 197 1 12
HELIX 85 85 SER F 208 ASN F 213 1 6
HELIX 86 86 ASN F 216 ASP F 221 1 6
HELIX 87 87 ASP F 236 CYS F 241 5 6
HELIX 88 88 LYS F 259 GLY F 275 1 17
HELIX 89 89 ASP F 310 GLY F 316 1 7
HELIX 90 90 GLY F 316 LEU F 326 1 11
HELIX 91 91 SER G 12 ILE G 30 1 19
HELIX 92 92 SER G 44 ALA G 54 1 11
HELIX 93 93 ASP G 63 LEU G 72 1 10
HELIX 94 94 GLN G 108 LEU G 112 5 5
HELIX 95 95 TRP G 128 TYR G 136 1 9
HELIX 96 96 CYS G 137 LEU G 139 5 3
HELIX 97 97 PRO G 145 PHE G 154 1 10
HELIX 98 98 PHE G 167 GLN G 172 5 6
HELIX 99 99 PHE G 186 ASP G 197 1 12
HELIX 100 100 SER G 208 ASN G 213 1 6
HELIX 101 101 ASN G 216 ASP G 221 1 6
HELIX 102 102 ASP G 236 CYS G 241 5 6
HELIX 103 103 LYS G 259 GLY G 275 1 17
HELIX 104 104 ASP G 310 GLY G 316 1 7
HELIX 105 105 GLY G 316 LEU G 326 1 11
HELIX 106 106 SER H 12 ILE H 30 1 19
HELIX 107 107 SER H 44 ALA H 54 1 11
HELIX 108 108 ASP H 63 LEU H 72 1 10
HELIX 109 109 GLN H 108 LEU H 112 5 5
HELIX 110 110 TRP H 128 TYR H 136 1 9
HELIX 111 111 CYS H 137 LEU H 139 5 3
HELIX 112 112 PRO H 145 PHE H 154 1 10
HELIX 113 113 PHE H 167 GLN H 172 5 6
HELIX 114 114 PHE H 186 ASP H 197 1 12
HELIX 115 115 SER H 208 ASN H 213 1 6
HELIX 116 116 ASN H 216 ASP H 221 1 6
HELIX 117 117 ASP H 236 CYS H 241 5 6
HELIX 118 118 LYS H 259 GLY H 275 1 17
HELIX 119 119 ASP H 310 GLY H 316 1 7
HELIX 120 120 GLY H 316 LEU H 326 1 11
HELIX 121 121 SER I 12 ILE I 30 1 19
HELIX 122 122 SER I 44 ALA I 54 1 11
HELIX 123 123 ASP I 63 LEU I 72 1 10
HELIX 124 124 GLN I 108 LEU I 112 5 5
HELIX 125 125 TRP I 128 TYR I 136 1 9
HELIX 126 126 CYS I 137 LEU I 139 5 3
HELIX 127 127 PRO I 145 PHE I 154 1 10
HELIX 128 128 PHE I 167 GLN I 172 5 6
HELIX 129 129 PHE I 186 ASP I 197 1 12
HELIX 130 130 SER I 208 ASN I 213 1 6
HELIX 131 131 ASN I 216 ASP I 221 1 6
HELIX 132 132 ASP I 236 CYS I 241 5 6
HELIX 133 133 LYS I 259 GLY I 275 1 17
HELIX 134 134 ASP I 310 GLY I 316 1 7
HELIX 135 135 GLY I 316 LEU I 326 1 11
SHEET 1 A 2 THR B 5 VAL B 11 0
SHEET 2 A 2 SER B 36 LYS B 42 1 O LYS B 42 N ALA B 10
SHEET 1 B 4 VAL B 60 LEU B 62 0
SHEET 2 B 4 THR B 250 ARG B 254 -1 O THR B 250 N LEU B 62
SHEET 3 B 4 LEU B 77 GLY B 86 -1 N VAL B 80 O VAL B 251
SHEET 4 B 4 PRO B 91 GLN B 92 -1 O GLN B 92 N TYR B 85
SHEET 1 C 4 VAL B 60 LEU B 62 0
SHEET 2 C 4 THR B 250 ARG B 254 -1 O THR B 250 N LEU B 62
SHEET 3 C 4 LEU B 77 GLY B 86 -1 N VAL B 80 O VAL B 251
SHEET 4 C 4 GLY B 301 LYS B 304 -1 O LEU B 303 N ALA B 82
SHEET 1 D 6 SER B 157 CYS B 158 0
SHEET 2 D 6 SER B 117 HIS B 119 1 N HIS B 119 O CYS B 158
SHEET 3 D 6 VAL B 202 GLU B 206 1 O VAL B 202 N CYS B 118
SHEET 4 D 6 PHE B 94 LYS B 102 -1 N VAL B 100 O ALA B 203
SHEET 5 D 6 TYR B 223 CYS B 227 -1 O GLU B 224 N VAL B 101
SHEET 6 D 6 THR B 231 PRO B 234 -1 O THR B 231 N CYS B 227
SHEET 1 E 5 SER B 157 CYS B 158 0
SHEET 2 E 5 SER B 117 HIS B 119 1 N HIS B 119 O CYS B 158
SHEET 3 E 5 VAL B 202 GLU B 206 1 O VAL B 202 N CYS B 118
SHEET 4 E 5 PHE B 94 LYS B 102 -1 N VAL B 100 O ALA B 203
SHEET 5 E 5 ALA B 244 PRO B 247 -1 O ALA B 244 N ALA B 97
SHEET 1 F 2 THR A 5 VAL A 11 0
SHEET 2 F 2 SER A 36 LYS A 42 1 O LYS A 42 N ALA A 10
SHEET 1 G 4 VAL A 60 LEU A 62 0
SHEET 2 G 4 THR A 250 ARG A 254 -1 O THR A 250 N LEU A 62
SHEET 3 G 4 LEU A 77 GLY A 86 -1 N VAL A 80 O VAL A 251
SHEET 4 G 4 PRO A 91 GLN A 92 -1 O GLN A 92 N TYR A 85
SHEET 1 H 4 VAL A 60 LEU A 62 0
SHEET 2 H 4 THR A 250 ARG A 254 -1 O THR A 250 N LEU A 62
SHEET 3 H 4 LEU A 77 GLY A 86 -1 N VAL A 80 O VAL A 251
SHEET 4 H 4 GLY A 301 LYS A 304 -1 O LEU A 303 N ALA A 82
SHEET 1 I 6 SER A 157 CYS A 158 0
SHEET 2 I 6 SER A 117 CYS A 118 1 N SER A 117 O CYS A 158
SHEET 3 I 6 VAL A 202 GLU A 206 1 O VAL A 202 N CYS A 118
SHEET 4 I 6 PHE A 94 LYS A 102 -1 N VAL A 100 O ALA A 203
SHEET 5 I 6 TYR A 223 CYS A 227 -1 O GLU A 224 N VAL A 101
SHEET 6 I 6 THR A 231 PRO A 234 -1 O THR A 231 N CYS A 227
SHEET 1 J 5 SER A 157 CYS A 158 0
SHEET 2 J 5 SER A 117 CYS A 118 1 N SER A 117 O CYS A 158
SHEET 3 J 5 VAL A 202 GLU A 206 1 O VAL A 202 N CYS A 118
SHEET 4 J 5 PHE A 94 LYS A 102 -1 N VAL A 100 O ALA A 203
SHEET 5 J 5 ALA A 244 PRO A 247 -1 O ALA A 244 N ALA A 97
SHEET 1 K 2 THR C 5 VAL C 11 0
SHEET 2 K 2 SER C 36 LYS C 42 1 O ALA C 38 N TRP C 8
SHEET 1 L 4 VAL C 60 LEU C 62 0
SHEET 2 L 4 THR C 250 ARG C 254 -1 O THR C 250 N LEU C 62
SHEET 3 L 4 LEU C 77 GLY C 86 -1 N VAL C 81 O VAL C 251
SHEET 4 L 4 PRO C 91 GLN C 92 -1 O GLN C 92 N TYR C 85
SHEET 1 M 4 VAL C 60 LEU C 62 0
SHEET 2 M 4 THR C 250 ARG C 254 -1 O THR C 250 N LEU C 62
SHEET 3 M 4 LEU C 77 GLY C 86 -1 N VAL C 81 O VAL C 251
SHEET 4 M 4 GLY C 301 LYS C 304 -1 O LEU C 303 N ALA C 82
SHEET 1 N 6 SER C 157 CYS C 158 0
SHEET 2 N 6 SER C 117 HIS C 119 1 N HIS C 119 O CYS C 158
SHEET 3 N 6 VAL C 202 GLU C 206 1 O VAL C 202 N CYS C 118
SHEET 4 N 6 PHE C 94 LYS C 102 -1 N VAL C 100 O ALA C 203
SHEET 5 N 6 TYR C 223 CYS C 227 -1 O GLU C 224 N VAL C 101
SHEET 6 N 6 THR C 231 PRO C 234 -1 O LYS C 233 N LEU C 225
SHEET 1 O 5 SER C 157 CYS C 158 0
SHEET 2 O 5 SER C 117 HIS C 119 1 N HIS C 119 O CYS C 158
SHEET 3 O 5 VAL C 202 GLU C 206 1 O VAL C 202 N CYS C 118
SHEET 4 O 5 PHE C 94 LYS C 102 -1 N VAL C 100 O ALA C 203
SHEET 5 O 5 ALA C 244 PRO C 247 -1 O ALA C 244 N ALA C 97
SHEET 1 P 2 THR D 5 VAL D 11 0
SHEET 2 P 2 SER D 36 LYS D 42 1 O ALA D 38 N VAL D 6
SHEET 1 Q 4 VAL D 60 LEU D 62 0
SHEET 2 Q 4 THR D 250 ARG D 254 -1 O THR D 250 N LEU D 62
SHEET 3 Q 4 LEU D 77 GLY D 86 -1 N VAL D 80 O VAL D 251
SHEET 4 Q 4 PRO D 91 GLN D 92 -1 O GLN D 92 N TYR D 85
SHEET 1 R 4 VAL D 60 LEU D 62 0
SHEET 2 R 4 THR D 250 ARG D 254 -1 O THR D 250 N LEU D 62
SHEET 3 R 4 LEU D 77 GLY D 86 -1 N VAL D 80 O VAL D 251
SHEET 4 R 4 GLY D 301 LYS D 304 -1 O LEU D 303 N ALA D 82
SHEET 1 S 6 SER D 157 CYS D 158 0
SHEET 2 S 6 SER D 117 HIS D 119 1 N HIS D 119 O CYS D 158
SHEET 3 S 6 VAL D 202 GLU D 206 1 O VAL D 202 N CYS D 118
SHEET 4 S 6 PHE D 94 LYS D 102 -1 N VAL D 98 O VAL D 205
SHEET 5 S 6 TYR D 223 LEU D 226 -1 O GLU D 224 N VAL D 101
SHEET 6 S 6 ARG D 232 PRO D 234 -1 O LYS D 233 N LEU D 225
SHEET 1 T 5 SER D 157 CYS D 158 0
SHEET 2 T 5 SER D 117 HIS D 119 1 N HIS D 119 O CYS D 158
SHEET 3 T 5 VAL D 202 GLU D 206 1 O VAL D 202 N CYS D 118
SHEET 4 T 5 PHE D 94 LYS D 102 -1 N VAL D 98 O VAL D 205
SHEET 5 T 5 ALA D 244 PRO D 247 -1 O ALA D 244 N ALA D 97
SHEET 1 U 2 THR E 5 VAL E 11 0
SHEET 2 U 2 SER E 36 LYS E 42 1 O VAL E 40 N ALA E 10
SHEET 1 V 4 VAL E 60 LEU E 62 0
SHEET 2 V 4 THR E 250 ARG E 254 -1 O THR E 250 N LEU E 62
SHEET 3 V 4 LEU E 77 GLY E 86 -1 N VAL E 80 O VAL E 251
SHEET 4 V 4 PRO E 91 GLN E 92 -1 O GLN E 92 N TYR E 85
SHEET 1 W 4 VAL E 60 LEU E 62 0
SHEET 2 W 4 THR E 250 ARG E 254 -1 O THR E 250 N LEU E 62
SHEET 3 W 4 LEU E 77 GLY E 86 -1 N VAL E 80 O VAL E 251
SHEET 4 W 4 GLY E 301 LYS E 304 -1 O LEU E 303 N ALA E 82
SHEET 1 X 6 SER E 157 CYS E 158 0
SHEET 2 X 6 SER E 117 HIS E 119 1 N HIS E 119 O CYS E 158
SHEET 3 X 6 VAL E 202 GLU E 206 1 O PHE E 204 N CYS E 118
SHEET 4 X 6 PHE E 94 LYS E 102 -1 N VAL E 98 O VAL E 205
SHEET 5 X 6 TYR E 223 LEU E 226 -1 O GLU E 224 N VAL E 101
SHEET 6 X 6 ARG E 232 PRO E 234 -1 O LYS E 233 N LEU E 225
SHEET 1 Y 5 SER E 157 CYS E 158 0
SHEET 2 Y 5 SER E 117 HIS E 119 1 N HIS E 119 O CYS E 158
SHEET 3 Y 5 VAL E 202 GLU E 206 1 O PHE E 204 N CYS E 118
SHEET 4 Y 5 PHE E 94 LYS E 102 -1 N VAL E 98 O VAL E 205
SHEET 5 Y 5 ALA E 244 PRO E 247 -1 O ALA E 244 N ALA E 97
SHEET 1 Z 2 THR F 5 VAL F 11 0
SHEET 2 Z 2 SER F 36 LYS F 42 1 O ALA F 38 N TRP F 8
SHEET 1 AA 4 VAL F 60 LEU F 62 0
SHEET 2 AA 4 THR F 250 ARG F 254 -1 O THR F 250 N LEU F 62
SHEET 3 AA 4 LEU F 77 GLY F 86 -1 N VAL F 80 O VAL F 251
SHEET 4 AA 4 PRO F 91 GLN F 92 -1 O GLN F 92 N TYR F 85
SHEET 1 AB 4 VAL F 60 LEU F 62 0
SHEET 2 AB 4 THR F 250 ARG F 254 -1 O THR F 250 N LEU F 62
SHEET 3 AB 4 LEU F 77 GLY F 86 -1 N VAL F 80 O VAL F 251
SHEET 4 AB 4 GLY F 301 LYS F 304 -1 O LEU F 303 N ALA F 82
SHEET 1 AC 6 SER F 157 CYS F 158 0
SHEET 2 AC 6 SER F 117 HIS F 119 1 N HIS F 119 O CYS F 158
SHEET 3 AC 6 VAL F 202 GLU F 206 1 O PHE F 204 N CYS F 118
SHEET 4 AC 6 PHE F 94 LYS F 102 -1 N VAL F 98 O VAL F 205
SHEET 5 AC 6 TYR F 223 LEU F 226 -1 O GLU F 224 N VAL F 101
SHEET 6 AC 6 ARG F 232 PRO F 234 -1 O LYS F 233 N LEU F 225
SHEET 1 AD 5 SER F 157 CYS F 158 0
SHEET 2 AD 5 SER F 117 HIS F 119 1 N HIS F 119 O CYS F 158
SHEET 3 AD 5 VAL F 202 GLU F 206 1 O PHE F 204 N CYS F 118
SHEET 4 AD 5 PHE F 94 LYS F 102 -1 N VAL F 98 O VAL F 205
SHEET 5 AD 5 ALA F 244 PRO F 247 -1 O ALA F 244 N ALA F 97
SHEET 1 AE 2 THR G 5 VAL G 11 0
SHEET 2 AE 2 SER G 36 LYS G 42 1 O VAL G 40 N ALA G 10
SHEET 1 AF 4 VAL G 60 LEU G 62 0
SHEET 2 AF 4 THR G 250 ARG G 254 -1 O THR G 250 N LEU G 62
SHEET 3 AF 4 LEU G 77 GLY G 86 -1 N VAL G 80 O VAL G 251
SHEET 4 AF 4 PRO G 91 GLN G 92 -1 O GLN G 92 N TYR G 85
SHEET 1 AG 4 VAL G 60 LEU G 62 0
SHEET 2 AG 4 THR G 250 ARG G 254 -1 O THR G 250 N LEU G 62
SHEET 3 AG 4 LEU G 77 GLY G 86 -1 N VAL G 80 O VAL G 251
SHEET 4 AG 4 GLY G 301 LYS G 304 -1 O LEU G 303 N ALA G 82
SHEET 1 AH 6 SER G 157 CYS G 158 0
SHEET 2 AH 6 SER G 117 HIS G 119 1 N HIS G 119 O CYS G 158
SHEET 3 AH 6 VAL G 202 GLU G 206 1 O PHE G 204 N CYS G 118
SHEET 4 AH 6 PHE G 94 LYS G 102 -1 N VAL G 98 O VAL G 205
SHEET 5 AH 6 TYR G 223 LEU G 226 -1 O LEU G 226 N ALA G 99
SHEET 6 AH 6 ARG G 232 PRO G 234 -1 O LYS G 233 N LEU G 225
SHEET 1 AI 5 SER G 157 CYS G 158 0
SHEET 2 AI 5 SER G 117 HIS G 119 1 N HIS G 119 O CYS G 158
SHEET 3 AI 5 VAL G 202 GLU G 206 1 O PHE G 204 N CYS G 118
SHEET 4 AI 5 PHE G 94 LYS G 102 -1 N VAL G 98 O VAL G 205
SHEET 5 AI 5 ALA G 244 PRO G 247 -1 O ALA G 244 N ALA G 97
SHEET 1 AJ 2 THR H 5 VAL H 11 0
SHEET 2 AJ 2 SER H 36 LYS H 42 1 O VAL H 40 N TRP H 8
SHEET 1 AK 4 VAL H 60 LEU H 62 0
SHEET 2 AK 4 THR H 250 ARG H 254 -1 O THR H 250 N LEU H 62
SHEET 3 AK 4 LEU H 77 GLY H 86 -1 N VAL H 80 O VAL H 251
SHEET 4 AK 4 PRO H 91 GLN H 92 -1 O GLN H 92 N TYR H 85
SHEET 1 AL 4 VAL H 60 LEU H 62 0
SHEET 2 AL 4 THR H 250 ARG H 254 -1 O THR H 250 N LEU H 62
SHEET 3 AL 4 LEU H 77 GLY H 86 -1 N VAL H 80 O VAL H 251
SHEET 4 AL 4 GLY H 301 LYS H 304 -1 O LEU H 303 N ALA H 82
SHEET 1 AM 6 SER H 157 CYS H 158 0
SHEET 2 AM 6 SER H 117 HIS H 119 1 N HIS H 119 O CYS H 158
SHEET 3 AM 6 VAL H 202 GLU H 206 1 O PHE H 204 N CYS H 118
SHEET 4 AM 6 PHE H 94 LYS H 102 -1 N VAL H 98 O VAL H 205
SHEET 5 AM 6 TYR H 223 LEU H 226 -1 O LEU H 226 N ALA H 99
SHEET 6 AM 6 ARG H 232 PRO H 234 -1 O LYS H 233 N LEU H 225
SHEET 1 AN 5 SER H 157 CYS H 158 0
SHEET 2 AN 5 SER H 117 HIS H 119 1 N HIS H 119 O CYS H 158
SHEET 3 AN 5 VAL H 202 GLU H 206 1 O PHE H 204 N CYS H 118
SHEET 4 AN 5 PHE H 94 LYS H 102 -1 N VAL H 98 O VAL H 205
SHEET 5 AN 5 ALA H 244 PRO H 247 -1 O ALA H 244 N ALA H 97
SHEET 1 AO 2 THR I 5 VAL I 11 0
SHEET 2 AO 2 SER I 36 LYS I 42 1 O ALA I 38 N VAL I 6
SHEET 1 AP 4 VAL I 60 LEU I 62 0
SHEET 2 AP 4 THR I 250 ARG I 254 -1 O THR I 250 N LEU I 62
SHEET 3 AP 4 LEU I 77 SER I 87 -1 N VAL I 80 O VAL I 251
SHEET 4 AP 4 ASP I 90 GLN I 92 -1 O GLN I 92 N TYR I 85
SHEET 1 AQ 4 VAL I 60 LEU I 62 0
SHEET 2 AQ 4 THR I 250 ARG I 254 -1 O THR I 250 N LEU I 62
SHEET 3 AQ 4 LEU I 77 SER I 87 -1 N VAL I 80 O VAL I 251
SHEET 4 AQ 4 GLY I 301 LYS I 304 -1 O LEU I 303 N ALA I 82
SHEET 1 AR 6 SER I 157 CYS I 158 0
SHEET 2 AR 6 SER I 117 HIS I 119 1 N HIS I 119 O CYS I 158
SHEET 3 AR 6 VAL I 202 GLU I 206 1 O VAL I 202 N CYS I 118
SHEET 4 AR 6 PHE I 94 LYS I 102 -1 N VAL I 98 O VAL I 205
SHEET 5 AR 6 TYR I 223 LEU I 226 -1 O LEU I 226 N ALA I 99
SHEET 6 AR 6 ARG I 232 PRO I 234 -1 O LYS I 233 N LEU I 225
SHEET 1 AS 5 SER I 157 CYS I 158 0
SHEET 2 AS 5 SER I 117 HIS I 119 1 N HIS I 119 O CYS I 158
SHEET 3 AS 5 VAL I 202 GLU I 206 1 O VAL I 202 N CYS I 118
SHEET 4 AS 5 PHE I 94 LYS I 102 -1 N VAL I 98 O VAL I 205
SHEET 5 AS 5 ALA I 244 PRO I 247 -1 O ALA I 244 N ALA I 97
SSBOND 1 CYS B 9 CYS B 48 1555 1555 2.03
SSBOND 2 CYS B 19 CYS B 39 1555 1555 2.02
SSBOND 3 CYS B 118 CYS B 194 1555 1555 2.03
SSBOND 4 CYS B 137 CYS B 331 1555 1555 2.04
SSBOND 5 CYS B 158 CYS B 174 1555 1555 2.01
SSBOND 6 CYS B 161 CYS B 179 1555 1555 2.01
SSBOND 7 CYS B 171 CYS B 177 1555 1555 2.02
SSBOND 8 CYS B 227 CYS B 241 1555 1555 2.00
SSBOND 9 CYS A 9 CYS A 48 1555 1555 2.02
SSBOND 10 CYS A 19 CYS A 39 1555 1555 1.99
SSBOND 11 CYS A 118 CYS A 194 1555 1555 2.02
SSBOND 12 CYS A 137 CYS A 331 1555 1555 2.05
SSBOND 13 CYS A 158 CYS A 174 1555 1555 2.04
SSBOND 14 CYS A 161 CYS A 179 1555 1555 2.00
SSBOND 15 CYS A 171 CYS A 177 1555 1555 2.02
SSBOND 16 CYS A 227 CYS A 241 1555 1555 2.00
SSBOND 17 CYS C 9 CYS C 48 1555 1555 2.04
SSBOND 18 CYS C 19 CYS C 39 1555 1555 2.02
SSBOND 19 CYS C 118 CYS C 194 1555 1555 2.03
SSBOND 20 CYS C 137 CYS C 331 1555 1555 2.05
SSBOND 21 CYS C 158 CYS C 174 1555 1555 2.04
SSBOND 22 CYS C 161 CYS C 179 1555 1555 2.03
SSBOND 23 CYS C 171 CYS C 177 1555 1555 2.05
SSBOND 24 CYS C 227 CYS C 241 1555 1555 2.01
SSBOND 25 CYS D 9 CYS D 48 1555 1555 2.03
SSBOND 26 CYS D 19 CYS D 39 1555 1555 2.07
SSBOND 27 CYS D 118 CYS D 194 1555 1555 2.03
SSBOND 28 CYS D 137 CYS D 331 1555 1555 2.05
SSBOND 29 CYS D 158 CYS D 174 1555 1555 2.04
SSBOND 30 CYS D 161 CYS D 179 1555 1555 2.02
SSBOND 31 CYS D 171 CYS D 177 1555 1555 2.03
SSBOND 32 CYS D 227 CYS D 241 1555 1555 2.00
SSBOND 33 CYS E 9 CYS E 48 1555 1555 2.03
SSBOND 34 CYS E 19 CYS E 39 1555 1555 2.06
SSBOND 35 CYS E 118 CYS E 194 1555 1555 2.03
SSBOND 36 CYS E 137 CYS E 331 1555 1555 2.06
SSBOND 37 CYS E 158 CYS E 174 1555 1555 2.03
SSBOND 38 CYS E 161 CYS E 179 1555 1555 2.02
SSBOND 39 CYS E 171 CYS E 177 1555 1555 2.03
SSBOND 40 CYS E 227 CYS E 241 1555 1555 2.02
SSBOND 41 CYS F 9 CYS F 48 1555 1555 2.03
SSBOND 42 CYS F 19 CYS F 39 1555 1555 2.04
SSBOND 43 CYS F 118 CYS F 194 1555 1555 2.02
SSBOND 44 CYS F 137 CYS F 331 1555 1555 2.06
SSBOND 45 CYS F 158 CYS F 174 1555 1555 2.03
SSBOND 46 CYS F 161 CYS F 179 1555 1555 2.02
SSBOND 47 CYS F 171 CYS F 177 1555 1555 2.04
SSBOND 48 CYS F 227 CYS F 241 1555 1555 2.03
SSBOND 49 CYS G 9 CYS G 48 1555 1555 2.02
SSBOND 50 CYS G 19 CYS G 39 1555 1555 2.06
SSBOND 51 CYS G 118 CYS G 194 1555 1555 2.04
SSBOND 52 CYS G 137 CYS G 331 1555 1555 2.03
SSBOND 53 CYS G 158 CYS G 174 1555 1555 2.05
SSBOND 54 CYS G 161 CYS G 179 1555 1555 2.04
SSBOND 55 CYS G 171 CYS G 177 1555 1555 2.03
SSBOND 56 CYS G 227 CYS G 241 1555 1555 1.99
SSBOND 57 CYS H 9 CYS H 48 1555 1555 2.03
SSBOND 58 CYS H 19 CYS H 39 1555 1555 2.05
SSBOND 59 CYS H 118 CYS H 194 1555 1555 2.03
SSBOND 60 CYS H 137 CYS H 331 1555 1555 2.03
SSBOND 61 CYS H 158 CYS H 174 1555 1555 2.05
SSBOND 62 CYS H 161 CYS H 179 1555 1555 2.03
SSBOND 63 CYS H 171 CYS H 177 1555 1555 2.02
SSBOND 64 CYS H 227 CYS H 241 1555 1555 2.00
SSBOND 65 CYS I 9 CYS I 48 1555 1555 2.02
SSBOND 66 CYS I 19 CYS I 39 1555 1555 2.06
SSBOND 67 CYS I 118 CYS I 194 1555 1555 2.04
SSBOND 68 CYS I 137 CYS I 331 1555 1555 2.03
SSBOND 69 CYS I 158 CYS I 174 1555 1555 2.05
SSBOND 70 CYS I 161 CYS I 179 1555 1555 2.04
SSBOND 71 CYS I 171 CYS I 177 1555 1555 2.02
SSBOND 72 CYS I 227 CYS I 241 1555 1555 2.00
LINK OD1 ASP B 63 FE FE B 500 1555 1555 1.92
LINK OH TYR B 95 FE FE B 500 1555 1555 1.77
LINK OH TYR B 188 FE FE B 500 1555 1555 2.13
LINK NE2 HIS B 249 FE FE B 500 1555 1555 2.05
LINK FE FE B 500 O2 CO3 B 600 1555 1555 2.20
LINK FE FE B 500 O3 CO3 B 600 1555 1555 2.15
LINK OD1 ASP A 63 FE FE A 500 1555 1555 1.90
LINK OH TYR A 95 FE FE A 500 1555 1555 1.82
LINK OH TYR A 188 FE FE A 500 1555 1555 2.18
LINK NE2 HIS A 249 FE FE A 500 1555 1555 2.01
LINK FE FE A 500 O3 CO3 A 600 1555 1555 2.16
LINK FE FE A 500 O2 CO3 A 600 1555 1555 2.20
LINK OD1 ASP C 63 FE FE C 500 1555 1555 1.92
LINK OH TYR C 95 FE FE C 500 1555 1555 1.85
LINK OH TYR C 188 FE FE C 500 1555 1555 2.13
LINK NE2 HIS C 249 FE FE C 500 1555 1555 1.99
LINK FE FE C 500 O2 CO3 C 600 1555 1555 2.22
LINK FE FE C 500 O3 CO3 C 600 1555 1555 2.14
LINK OD1 ASP D 63 FE FE D 500 1555 1555 1.94
LINK OH TYR D 95 FE FE D 500 1555 1555 1.99
LINK OH TYR D 188 FE FE D 500 1555 1555 1.90
LINK NE2 HIS D 249 FE FE D 500 1555 1555 2.15
LINK FE FE D 500 O2 CO3 D 600 1555 1555 2.24
LINK FE FE D 500 O3 CO3 D 600 1555 1555 2.22
LINK OD1 ASP E 63 FE FE E 500 1555 1555 1.97
LINK OH TYR E 95 FE FE E 500 1555 1555 1.97
LINK OH TYR E 188 FE FE E 500 1555 1555 1.92
LINK NE2 HIS E 249 FE FE E 500 1555 1555 2.07
LINK FE FE E 500 O3 CO3 E 600 1555 1555 2.29
LINK FE FE E 500 O2 CO3 E 600 1555 1555 2.14
LINK OD1 ASP F 63 FE FE F 500 1555 1555 1.94
LINK OH TYR F 95 FE FE F 500 1555 1555 1.90
LINK OH TYR F 188 FE FE F 500 1555 1555 1.92
LINK NE2 HIS F 249 FE FE F 500 1555 1555 2.13
LINK FE FE F 500 O2 CO3 F 600 1555 1555 2.24
LINK FE FE F 500 O3 CO3 F 600 1555 1555 2.17
LINK OD1 ASP G 63 FE FE G 500 1555 1555 2.14
LINK OH TYR G 95 FE FE G 500 1555 1555 2.08
LINK OH TYR G 188 FE FE G 500 1555 1555 1.82
LINK NE2 HIS G 249 FE FE G 500 1555 1555 2.19
LINK FE FE G 500 O2 CO3 G 600 1555 1555 2.21
LINK FE FE G 500 O3 CO3 G 600 1555 1555 2.20
LINK OD1 ASP H 63 FE FE H 500 1555 1555 2.07
LINK OH TYR H 95 FE FE H 500 1555 1555 2.06
LINK OH TYR H 188 FE FE H 500 1555 1555 1.89
LINK NE2 HIS H 249 FE FE H 500 1555 1555 2.19
LINK FE FE H 500 O2 CO3 H 600 1555 1555 2.15
LINK FE FE H 500 O3 CO3 H 600 1555 1555 2.28
LINK OD1 ASP I 63 FE FE I 500 1555 1555 2.12
LINK OH TYR I 95 FE FE I 500 1555 1555 2.07
LINK OH TYR I 188 FE FE I 500 1555 1555 1.86
LINK NE2 HIS I 249 FE FE I 500 1555 1555 2.16
LINK FE FE I 500 O3 CO3 I 600 1555 1555 2.13
LINK FE FE I 500 O2 CO3 I 600 1555 1555 2.24
CISPEP 1 ALA B 73 PRO B 74 0 13.50
CISPEP 2 GLU B 141 PRO B 142 0 -1.85
CISPEP 3 LYS B 144 PRO B 145 0 1.13
CISPEP 4 ALA A 73 PRO A 74 0 14.52
CISPEP 5 GLU A 141 PRO A 142 0 -0.45
CISPEP 6 LYS A 144 PRO A 145 0 -0.33
CISPEP 7 ALA C 73 PRO C 74 0 11.98
CISPEP 8 GLU C 141 PRO C 142 0 -1.42
CISPEP 9 LYS C 144 PRO C 145 0 0.35
CISPEP 10 ALA D 73 PRO D 74 0 5.49
CISPEP 11 GLU D 141 PRO D 142 0 1.20
CISPEP 12 LYS D 144 PRO D 145 0 1.46
CISPEP 13 ALA E 73 PRO E 74 0 4.78
CISPEP 14 GLU E 141 PRO E 142 0 1.12
CISPEP 15 LYS E 144 PRO E 145 0 1.79
CISPEP 16 ALA F 73 PRO F 74 0 6.35
CISPEP 17 GLU F 141 PRO F 142 0 0.89
CISPEP 18 LYS F 144 PRO F 145 0 0.94
CISPEP 19 ALA G 73 PRO G 74 0 4.89
CISPEP 20 GLU G 141 PRO G 142 0 1.94
CISPEP 21 LYS G 144 PRO G 145 0 1.15
CISPEP 22 ALA H 73 PRO H 74 0 4.43
CISPEP 23 GLU H 141 PRO H 142 0 1.38
CISPEP 24 LYS H 144 PRO H 145 0 1.53
CISPEP 25 ALA I 73 PRO I 74 0 4.94
CISPEP 26 GLU I 141 PRO I 142 0 1.49
CISPEP 27 LYS I 144 PRO I 145 0 1.25
SITE 1 AC1 5 ASP B 63 TYR B 95 TYR B 188 HIS B 249
SITE 2 AC1 5 CO3 B 600
SITE 1 AC2 9 ASP B 63 TYR B 95 THR B 120 ARG B 124
SITE 2 AC2 9 ALA B 126 GLY B 127 TYR B 188 HIS B 249
SITE 3 AC2 9 FE B 500
SITE 1 AC3 5 ASP A 63 TYR A 95 TYR A 188 HIS A 249
SITE 2 AC3 5 CO3 A 600
SITE 1 AC4 9 ASP A 63 TYR A 95 THR A 120 ARG A 124
SITE 2 AC4 9 ALA A 126 GLY A 127 TYR A 188 HIS A 249
SITE 3 AC4 9 FE A 500
SITE 1 AC5 5 ASP C 63 TYR C 95 TYR C 188 HIS C 249
SITE 2 AC5 5 CO3 C 600
SITE 1 AC6 9 ASP C 63 TYR C 95 THR C 120 ARG C 124
SITE 2 AC6 9 ALA C 126 GLY C 127 TYR C 188 HIS C 249
SITE 3 AC6 9 FE C 500
SITE 1 AC7 5 ASP D 63 TYR D 95 TYR D 188 HIS D 249
SITE 2 AC7 5 CO3 D 600
SITE 1 AC8 10 ASP D 63 TYR D 95 THR D 120 ARG D 124
SITE 2 AC8 10 SER D 125 ALA D 126 GLY D 127 TYR D 188
SITE 3 AC8 10 HIS D 249 FE D 500
SITE 1 AC9 5 ASP E 63 TYR E 95 TYR E 188 HIS E 249
SITE 2 AC9 5 CO3 E 600
SITE 1 BC1 10 ASP E 63 TYR E 95 THR E 120 ARG E 124
SITE 2 BC1 10 SER E 125 ALA E 126 GLY E 127 TYR E 188
SITE 3 BC1 10 HIS E 249 FE E 500
SITE 1 BC2 5 ASP F 63 TYR F 95 TYR F 188 HIS F 249
SITE 2 BC2 5 CO3 F 600
SITE 1 BC3 10 ASP F 63 TYR F 95 THR F 120 ARG F 124
SITE 2 BC3 10 SER F 125 ALA F 126 GLY F 127 TYR F 188
SITE 3 BC3 10 HIS F 249 FE F 500
SITE 1 BC4 5 ASP G 63 TYR G 95 TYR G 188 HIS G 249
SITE 2 BC4 5 CO3 G 600
SITE 1 BC5 9 ASP G 63 TYR G 95 THR G 120 ARG G 124
SITE 2 BC5 9 SER G 125 ALA G 126 GLY G 127 TYR G 188
SITE 3 BC5 9 FE G 500
SITE 1 BC6 5 ASP H 63 TYR H 95 TYR H 188 HIS H 249
SITE 2 BC6 5 CO3 H 600
SITE 1 BC7 10 ASP H 63 TYR H 95 THR H 120 ARG H 124
SITE 2 BC7 10 SER H 125 ALA H 126 GLY H 127 TYR H 188
SITE 3 BC7 10 HIS H 249 FE H 500
SITE 1 BC8 5 ASP I 63 TYR I 95 TYR I 188 HIS I 249
SITE 2 BC8 5 CO3 I 600
SITE 1 BC9 9 ASP I 63 TYR I 95 THR I 120 ARG I 124
SITE 2 BC9 9 SER I 125 ALA I 126 GLY I 127 TYR I 188
SITE 3 BC9 9 FE I 500
CRYST1 169.462 97.897 208.953 90.00 90.01 90.00 C 1 2 1 36
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 0.005901 0.000000 0.000001 0.00000
SCALE2 0.000000 0.010215 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004786 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
