HEADER METAL TRANSPORT 11-DEC-16 5WTD
TITLE STRUCTURE OF HUMAN SERUM TRANSFERRIN BOUND RUTHENIUM AT N-LOBE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEROTRANSFERRIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRANSFERRIN,BETA-1 METAL-BINDING GLOBULIN,SIDEROPHILIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS RUTHENIUM TRANSFERRIN N-LOBE, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR H.SUN,M.WANG,T.P.LAI,H.ZHANG,Q.HAO
REVDAT 3 08-NOV-23 5WTD 1 REMARK
REVDAT 2 22-JUN-22 5WTD 1 JRNL LINK
REVDAT 1 20-DEC-17 5WTD 0
JRNL AUTH M.WANG,H.WANG,X.XU,T.P.LAI,Y.ZHOU,Q.HAO,H.LI,H.SUN
JRNL TITL BINDING OF RUTHENIUM AND OSMIUM AT NON‐IRON SITES OF
JRNL TITL 2 TRANSFERRIN ACCOUNTS FOR THEIR IRON-INDEPENDENT CELLULAR
JRNL TITL 3 UPTAKE.
JRNL REF J.INORG.BIOCHEM. V. 234 11885 2022
JRNL REFN ISSN 0162-0134
JRNL PMID 35690040
JRNL DOI 10.1016/J.JINORGBIO.2022.111885
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.19
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.4
REMARK 3 NUMBER OF REFLECTIONS : 51927
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.210
REMARK 3 FREE R VALUE TEST SET COUNT : 3480
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 37.1910 - 7.2953 0.97 2889 126 0.1830 0.2058
REMARK 3 2 7.2953 - 5.7976 1.00 2907 153 0.1941 0.2318
REMARK 3 3 5.7976 - 5.0668 1.00 2971 145 0.1797 0.1784
REMARK 3 4 5.0668 - 4.6044 0.99 2926 159 0.1503 0.1849
REMARK 3 5 4.6044 - 4.2749 0.99 2869 182 0.1463 0.1798
REMARK 3 6 4.2749 - 4.0232 1.00 2903 171 0.1553 0.2115
REMARK 3 7 4.0232 - 3.8219 0.99 2912 155 0.1608 0.2197
REMARK 3 8 3.8219 - 3.6557 0.99 2912 159 0.1591 0.1831
REMARK 3 9 3.6557 - 3.5151 0.99 2897 178 0.1723 0.2003
REMARK 3 10 3.5151 - 3.3939 0.99 2902 151 0.1771 0.2588
REMARK 3 11 3.3939 - 3.2878 0.99 2932 157 0.1849 0.2126
REMARK 3 12 3.2878 - 3.1939 0.99 2896 154 0.1835 0.2264
REMARK 3 13 3.1939 - 3.1098 0.98 2904 154 0.1978 0.2263
REMARK 3 14 3.1098 - 3.0340 0.98 2862 171 0.2072 0.2680
REMARK 3 15 3.0340 - 2.9651 0.96 2823 164 0.2123 0.2500
REMARK 3 16 2.9651 - 2.9020 0.92 2648 154 0.2154 0.2199
REMARK 3 17 2.9020 - 2.8440 0.86 2570 148 0.2058 0.2491
REMARK 3 18 2.8440 - 2.7903 0.78 2249 128 0.1948 0.2131
REMARK 3 19 2.7903 - 2.7405 0.71 2066 124 0.1966 0.2161
REMARK 3 20 2.7405 - 2.6941 0.66 1959 101 0.2096 0.2538
REMARK 3 21 2.6941 - 2.6506 0.61 1801 78 0.2118 0.2614
REMARK 3 22 2.6506 - 2.6098 0.59 1713 94 0.2133 0.2161
REMARK 3 23 2.6098 - 2.5715 0.56 1663 95 0.2322 0.2365
REMARK 3 24 2.5715 - 2.5353 0.54 1567 91 0.2448 0.2210
REMARK 3 25 2.5353 - 2.5010 0.54 1589 88 0.2509 0.2947
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.500
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.62
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 5151
REMARK 3 ANGLE : 0.719 6964
REMARK 3 CHIRALITY : 0.043 743
REMARK 3 PLANARITY : 0.004 903
REMARK 3 DIHEDRAL : 8.707 3085
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 92 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.2310 10.4521 -13.1863
REMARK 3 T TENSOR
REMARK 3 T11: 0.2610 T22: 0.3840
REMARK 3 T33: 0.0793 T12: 0.0661
REMARK 3 T13: 0.0259 T23: 0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 2.0189 L22: 2.3910
REMARK 3 L33: 3.3042 L12: 0.4618
REMARK 3 L13: 0.3102 L23: 0.8520
REMARK 3 S TENSOR
REMARK 3 S11: 0.0087 S12: 0.3303 S13: 0.0285
REMARK 3 S21: -0.1728 S22: -0.0505 S23: -0.0544
REMARK 3 S31: -0.1889 S32: 0.0838 S33: 0.0394
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 93 THROUGH 246 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9190 18.6875 18.6177
REMARK 3 T TENSOR
REMARK 3 T11: 0.3145 T22: 0.4338
REMARK 3 T33: 0.0894 T12: -0.0977
REMARK 3 T13: 0.0789 T23: -0.0625
REMARK 3 L TENSOR
REMARK 3 L11: 1.3131 L22: 2.6160
REMARK 3 L33: 2.5279 L12: 0.3772
REMARK 3 L13: 0.5259 L23: 0.1586
REMARK 3 S TENSOR
REMARK 3 S11: 0.1584 S12: -0.1185 S13: 0.1140
REMARK 3 S21: 0.2610 S22: -0.1756 S23: 0.2251
REMARK 3 S31: -0.1705 S32: -0.1724 S33: 0.0008
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 247 THROUGH 332 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6575 16.7799 -8.3191
REMARK 3 T TENSOR
REMARK 3 T11: 0.2623 T22: 0.2982
REMARK 3 T33: 0.1178 T12: 0.0483
REMARK 3 T13: 0.0622 T23: 0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 2.0920 L22: 2.3394
REMARK 3 L33: 3.3088 L12: 0.5754
REMARK 3 L13: 1.1234 L23: 0.9225
REMARK 3 S TENSOR
REMARK 3 S11: -0.0311 S12: 0.1452 S13: 0.1836
REMARK 3 S21: -0.2271 S22: -0.0972 S23: 0.1420
REMARK 3 S31: -0.2489 S32: 0.2095 S33: 0.0990
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 339 THROUGH 413 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.2110 34.7260 0.8584
REMARK 3 T TENSOR
REMARK 3 T11: 0.5287 T22: 0.7686
REMARK 3 T33: 0.3180 T12: -0.3440
REMARK 3 T13: 0.0214 T23: 0.1128
REMARK 3 L TENSOR
REMARK 3 L11: 3.9546 L22: 5.3419
REMARK 3 L33: 2.5656 L12: 0.3131
REMARK 3 L13: 0.2696 L23: -0.6376
REMARK 3 S TENSOR
REMARK 3 S11: 0.4722 S12: -0.3126 S13: -0.1460
REMARK 3 S21: 0.4472 S22: -0.4205 S23: -0.7689
REMARK 3 S31: -0.3309 S32: 0.8142 S33: 0.0006
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 424 THROUGH 583 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0237 55.8624 -14.6904
REMARK 3 T TENSOR
REMARK 3 T11: 0.6524 T22: 0.4387
REMARK 3 T33: 0.2719 T12: -0.1930
REMARK 3 T13: 0.0996 T23: 0.0362
REMARK 3 L TENSOR
REMARK 3 L11: 3.3700 L22: 2.3084
REMARK 3 L33: 3.5736 L12: 0.7966
REMARK 3 L13: -1.2159 L23: -1.1225
REMARK 3 S TENSOR
REMARK 3 S11: 0.2962 S12: -0.0497 S13: 0.4444
REMARK 3 S21: 0.6418 S22: -0.1117 S23: 0.5174
REMARK 3 S31: -0.3775 S32: -0.1189 S33: -0.2139
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 584 THROUGH 679 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.4784 41.4322 3.1003
REMARK 3 T TENSOR
REMARK 3 T11: 0.8101 T22: 0.7005
REMARK 3 T33: 0.3103 T12: -0.3390
REMARK 3 T13: 0.0914 T23: 0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 3.0570 L22: 2.8519
REMARK 3 L33: 1.7635 L12: 0.6178
REMARK 3 L13: 0.2734 L23: -1.0053
REMARK 3 S TENSOR
REMARK 3 S11: 0.3607 S12: -0.3827 S13: 0.5867
REMARK 3 S21: 0.9076 S22: -0.3748 S23: -0.0190
REMARK 3 S31: -0.5690 S32: 0.5112 S33: 0.0067
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE ENTRY CONTAINS FRIEDEL PAIRS IN
REMARK 3 F_PLUS/MINUS COLUMNS AND I_PLUS/MINUS COLUMNS
REMARK 4
REMARK 4 5WTD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1300002226.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-SEP-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99182
REMARK 200 MONOCHROMATOR : GRAPHITE FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51927
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.501
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 0.79100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4X1B
REMARK 200
REMARK 200 REMARK: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS COLUMNS
REMARK 200 AND I_PLUS/MINUS COLUMNS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PIPES-NA 100 MM, DISODIUM MALONATE 8
REMARK 280 MM, PEG3350 17%, GLYCEROL 18%, PH 6.6, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 53.54300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.54300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 68.55650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 78.67550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 68.55650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 78.67550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 53.54300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 68.55650
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 78.67550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 53.54300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 68.55650
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 78.67550
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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 A 1
REMARK 465 PRO A 2
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 GLU A 338
REMARK 465 LYS A 414
REMARK 465 SER A 415
REMARK 465 ASP A 416
REMARK 465 ASN A 417
REMARK 465 CYS A 418
REMARK 465 GLU A 419
REMARK 465 ASP A 420
REMARK 465 THR A 421
REMARK 465 PRO A 422
REMARK 465 GLU A 423
REMARK 465 VAL A 612
REMARK 465 THR A 613
REMARK 465 ASP A 614
REMARK 465 CYS A 615
REMARK 465 SER A 616
REMARK 465 GLY A 617
REMARK 465 ASN A 618
REMARK 465 PHE A 619
REMARK 465 CYS A 620
REMARK 465 LEU A 621
REMARK 465 PHE A 622
REMARK 465 ARG A 623
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 ASP A 3 CG OD1 OD2
REMARK 470 LYS A 340 CG CD CE NZ
REMARK 470 ASP A 442 CG OD1 OD2
REMARK 470 ASN A 472 CG OD1 ND2
REMARK 470 HIS A 606 CG ND1 CD2 CE1 NE2
REMARK 470 ASN A 611 CG OD1 ND2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 875 O HOH A 943 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 31 -179.96 -67.54
REMARK 500 TRP A 128 -62.58 -144.13
REMARK 500 PHE A 153 -60.25 -103.43
REMARK 500 CYS A 179 34.44 -97.34
REMARK 500 CYS A 241 72.37 -156.05
REMARK 500 LYS A 259 78.43 -107.22
REMARK 500 LEU A 294 -42.10 68.52
REMARK 500 LYS A 340 171.67 78.27
REMARK 500 ALA A 453 154.67 174.04
REMARK 500 TRP A 460 -65.36 -139.93
REMARK 500 LYS A 527 -32.94 -136.54
REMARK 500 GLU A 573 30.23 -90.05
REMARK 500 CYS A 577 65.29 -160.54
REMARK 500 SER A 610 52.32 -90.46
REMARK 500 THR A 626 -102.19 -109.83
REMARK 500 LEU A 630 -51.51 66.11
REMARK 500 HIS A 642 -112.16 56.78
REMARK 500 THR A 667 -120.56 -100.88
REMARK 500 SER A 668 97.14 72.32
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 RU A 703 RU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 14 NE2
REMARK 620 2 HIS A 289 NE2 95.4
REMARK 620 3 HOH A 916 O 92.0 75.8
REMARK 620 4 HOH A 946 O 176.6 81.9 89.2
REMARK 620 5 HOH A 948 O 94.3 102.5 173.7 84.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A 701 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 392 OD1
REMARK 620 2 TYR A 426 OH 95.0
REMARK 620 3 TYR A 517 OH 174.2 88.0
REMARK 620 4 HIS A 585 NE2 91.3 100.2 93.0
REMARK 620 5 MLI A 702 O7 82.9 91.0 92.1 167.8
REMARK 620 6 MLI A 702 O9 93.3 171.3 83.5 82.2 87.4
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 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue RU A 703
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS SEQUENCE IS NATURAL VARIANT.
DBREF 5WTD A 1 679 UNP P02787 TRFE_HUMAN 20 698
SEQADV 5WTD VAL A 429 UNP P02787 ILE 448 SEE SEQUENCE DETAILS
SEQRES 1 A 679 VAL PRO ASP LYS THR VAL ARG TRP CYS ALA VAL SER GLU
SEQRES 2 A 679 HIS GLU ALA THR LYS CYS GLN SER PHE ARG ASP HIS MET
SEQRES 3 A 679 LYS SER VAL ILE PRO SER ASP GLY PRO SER VAL ALA CYS
SEQRES 4 A 679 VAL LYS LYS ALA SER TYR LEU ASP CYS ILE ARG ALA ILE
SEQRES 5 A 679 ALA ALA ASN GLU ALA ASP ALA VAL THR LEU ASP ALA GLY
SEQRES 6 A 679 LEU VAL TYR ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS
SEQRES 7 A 679 PRO VAL VAL ALA GLU PHE TYR GLY SER LYS GLU ASP PRO
SEQRES 8 A 679 GLN THR PHE TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP
SEQRES 9 A 679 SER GLY PHE GLN MET ASN GLN LEU ARG GLY LYS LYS SER
SEQRES 10 A 679 CYS HIS THR GLY LEU GLY ARG SER ALA GLY TRP ASN ILE
SEQRES 11 A 679 PRO ILE GLY LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG
SEQRES 12 A 679 LYS PRO LEU GLU LYS ALA VAL ALA ASN PHE PHE SER GLY
SEQRES 13 A 679 SER CYS ALA PRO CYS ALA ASP GLY THR ASP PHE PRO GLN
SEQRES 14 A 679 LEU CYS GLN LEU CYS PRO GLY CYS GLY CYS SER THR LEU
SEQRES 15 A 679 ASN GLN TYR PHE GLY TYR SER GLY ALA PHE LYS CYS LEU
SEQRES 16 A 679 LYS ASP GLY ALA GLY ASP VAL ALA PHE VAL LYS HIS SER
SEQRES 17 A 679 THR ILE PHE GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP
SEQRES 18 A 679 GLN TYR GLU LEU LEU CYS LEU ASP ASN THR ARG LYS PRO
SEQRES 19 A 679 VAL ASP GLU TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO
SEQRES 20 A 679 SER HIS THR VAL VAL ALA ARG SER MET GLY GLY LYS GLU
SEQRES 21 A 679 ASP LEU ILE TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS
SEQRES 22 A 679 PHE GLY LYS ASP LYS SER LYS GLU PHE GLN LEU PHE SER
SEQRES 23 A 679 SER PRO HIS GLY LYS ASP LEU LEU PHE LYS ASP SER ALA
SEQRES 24 A 679 HIS GLY PHE LEU LYS VAL PRO PRO ARG MET ASP ALA LYS
SEQRES 25 A 679 MET TYR LEU GLY TYR GLU TYR VAL THR ALA ILE ARG ASN
SEQRES 26 A 679 LEU ARG GLU GLY THR CYS PRO GLU ALA PRO THR ASP GLU
SEQRES 27 A 679 CYS LYS PRO VAL LYS TRP CYS ALA LEU SER HIS HIS GLU
SEQRES 28 A 679 ARG LEU LYS CYS ASP GLU TRP SER VAL ASN SER VAL GLY
SEQRES 29 A 679 LYS ILE GLU CYS VAL SER ALA GLU THR THR GLU ASP CYS
SEQRES 30 A 679 ILE ALA LYS ILE MET ASN GLY GLU ALA ASP ALA MET SER
SEQRES 31 A 679 LEU ASP GLY GLY PHE VAL TYR ILE ALA GLY LYS CYS GLY
SEQRES 32 A 679 LEU VAL PRO VAL LEU ALA GLU ASN TYR ASN LYS SER ASP
SEQRES 33 A 679 ASN CYS GLU ASP THR PRO GLU ALA GLY TYR PHE ALA VAL
SEQRES 34 A 679 ALA VAL VAL LYS LYS SER ALA SER ASP LEU THR TRP ASP
SEQRES 35 A 679 ASN LEU LYS GLY LYS LYS SER CYS HIS THR ALA VAL GLY
SEQRES 36 A 679 ARG THR ALA GLY TRP ASN ILE PRO MET GLY LEU LEU TYR
SEQRES 37 A 679 ASN LYS ILE ASN HIS CYS ARG PHE ASP GLU PHE PHE SER
SEQRES 38 A 679 GLU GLY CYS ALA PRO GLY SER LYS LYS ASP SER SER LEU
SEQRES 39 A 679 CYS LYS LEU CYS MET GLY SER GLY LEU ASN LEU CYS GLU
SEQRES 40 A 679 PRO ASN ASN LYS GLU GLY TYR TYR GLY TYR THR GLY ALA
SEQRES 41 A 679 PHE ARG CYS LEU VAL GLU LYS GLY ASP VAL ALA PHE VAL
SEQRES 42 A 679 LYS HIS GLN THR VAL PRO GLN ASN THR GLY GLY LYS ASN
SEQRES 43 A 679 PRO ASP PRO TRP ALA LYS ASN LEU ASN GLU LYS ASP TYR
SEQRES 44 A 679 GLU LEU LEU CYS LEU ASP GLY THR ARG LYS PRO VAL GLU
SEQRES 45 A 679 GLU TYR ALA ASN CYS HIS LEU ALA ARG ALA PRO ASN HIS
SEQRES 46 A 679 ALA VAL VAL THR ARG LYS ASP LYS GLU ALA CYS VAL HIS
SEQRES 47 A 679 LYS ILE LEU ARG GLN GLN GLN HIS LEU PHE GLY SER ASN
SEQRES 48 A 679 VAL THR ASP CYS SER GLY ASN PHE CYS LEU PHE ARG SER
SEQRES 49 A 679 GLU THR LYS ASP LEU LEU PHE ARG ASP ASP THR VAL CYS
SEQRES 50 A 679 LEU ALA LYS LEU HIS ASP ARG ASN THR TYR GLU LYS TYR
SEQRES 51 A 679 LEU GLY GLU GLU TYR VAL LYS ALA VAL GLY ASN LEU ARG
SEQRES 52 A 679 LYS CYS SER THR SER SER LEU LEU GLU ALA CYS THR PHE
SEQRES 53 A 679 ARG ARG PRO
HET FE A 701 1
HET MLI A 702 7
HET RU A 703 1
HETNAM FE FE (III) ION
HETNAM MLI MALONATE ION
HETNAM RU RUTHENIUM ION
FORMUL 2 FE FE 3+
FORMUL 3 MLI C3 H2 O4 2-
FORMUL 4 RU RU 3+
FORMUL 5 HOH *155(H2 O)
HELIX 1 AA1 SER A 12 LYS A 27 1 16
HELIX 2 AA2 SER A 44 ALA A 54 1 11
HELIX 3 AA3 ASP A 63 LEU A 72 1 10
HELIX 4 AA4 GLN A 108 LEU A 112 5 5
HELIX 5 AA5 TRP A 128 TYR A 136 1 9
HELIX 6 AA6 CYS A 137 LEU A 139 5 3
HELIX 7 AA7 PRO A 145 ASN A 152 1 8
HELIX 8 AA8 PHE A 167 GLN A 172 5 6
HELIX 9 AA9 PHE A 186 ASP A 197 1 12
HELIX 10 AB1 SER A 208 LEU A 214 1 7
HELIX 11 AB2 ASN A 216 ASP A 221 1 6
HELIX 12 AB3 GLU A 237 CYS A 241 5 5
HELIX 13 AB4 LYS A 259 GLY A 275 1 17
HELIX 14 AB5 ASP A 310 GLY A 316 1 7
HELIX 15 AB6 GLY A 316 GLY A 329 1 14
HELIX 16 AB7 SER A 348 SER A 362 1 15
HELIX 17 AB8 THR A 373 ASN A 383 1 11
HELIX 18 AB9 ASP A 392 CYS A 402 1 11
HELIX 19 AC1 TRP A 460 ASN A 472 1 13
HELIX 20 AC2 ARG A 475 PHE A 479 5 5
HELIX 21 AC3 SER A 492 LYS A 496 5 5
HELIX 22 AC4 SER A 501 LEU A 505 5 5
HELIX 23 AC5 TYR A 515 LYS A 527 1 13
HELIX 24 AC6 GLN A 536 ASN A 541 1 6
HELIX 25 AC7 ASP A 548 ASN A 553 1 6
HELIX 26 AC8 ASN A 555 LYS A 557 5 3
HELIX 27 AC9 GLU A 572 CYS A 577 5 6
HELIX 28 AD1 ARG A 590 ASP A 592 5 3
HELIX 29 AD2 LYS A 593 GLY A 609 1 17
HELIX 30 AD3 THR A 646 GLY A 652 1 7
HELIX 31 AD4 GLY A 652 ARG A 663 1 12
HELIX 32 AD5 SER A 668 ARG A 678 1 11
SHEET 1 AA1 2 THR A 5 ALA A 10 0
SHEET 2 AA1 2 SER A 36 LYS A 41 1 O VAL A 40 N ALA A 10
SHEET 1 AA2 4 VAL A 60 LEU A 62 0
SHEET 2 AA2 4 THR A 250 ARG A 254 -1 O THR A 250 N LEU A 62
SHEET 3 AA2 4 LEU A 77 PHE A 84 -1 N VAL A 81 O VAL A 251
SHEET 4 AA2 4 GLY A 301 LYS A 304 -1 O LEU A 303 N ALA A 82
SHEET 1 AA3 6 GLY A 156 CYS A 158 0
SHEET 2 AA3 6 LYS A 116 HIS A 119 1 N HIS A 119 O CYS A 158
SHEET 3 AA3 6 VAL A 202 LYS A 206 1 O VAL A 202 N CYS A 118
SHEET 4 AA3 6 PHE A 94 LYS A 102 -1 N VAL A 98 O VAL A 205
SHEET 5 AA3 6 TYR A 223 LEU A 226 -1 O GLU A 224 N VAL A 101
SHEET 6 AA3 6 ARG A 232 LYS A 233 -1 O LYS A 233 N LEU A 225
SHEET 1 AA4 5 GLY A 156 CYS A 158 0
SHEET 2 AA4 5 LYS A 116 HIS A 119 1 N HIS A 119 O CYS A 158
SHEET 3 AA4 5 VAL A 202 LYS A 206 1 O VAL A 202 N CYS A 118
SHEET 4 AA4 5 PHE A 94 LYS A 102 -1 N VAL A 98 O VAL A 205
SHEET 5 AA4 5 ALA A 244 PRO A 247 -1 O VAL A 246 N TYR A 95
SHEET 1 AA5 2 VAL A 342 ALA A 346 0
SHEET 2 AA5 2 ILE A 366 SER A 370 1 O GLU A 367 N TRP A 344
SHEET 1 AA6 4 MET A 389 LEU A 391 0
SHEET 2 AA6 4 ALA A 586 THR A 589 -1 O ALA A 586 N LEU A 391
SHEET 3 AA6 4 VAL A 405 ASN A 411 -1 N LEU A 408 O VAL A 587
SHEET 4 AA6 4 CYS A 637 ALA A 639 -1 O ALA A 639 N ALA A 409
SHEET 1 AA7 6 GLU A 482 CYS A 484 0
SHEET 2 AA7 6 LYS A 448 HIS A 451 1 N HIS A 451 O CYS A 484
SHEET 3 AA7 6 VAL A 530 LYS A 534 1 O PHE A 532 N CYS A 450
SHEET 4 AA7 6 TYR A 426 LYS A 433 -1 N VAL A 431 O ALA A 531
SHEET 5 AA7 6 TYR A 559 LEU A 562 -1 O LEU A 562 N ALA A 430
SHEET 6 AA7 6 ARG A 568 PRO A 570 -1 O LYS A 569 N LEU A 561
SHEET 1 AA8 5 GLU A 482 CYS A 484 0
SHEET 2 AA8 5 LYS A 448 HIS A 451 1 N HIS A 451 O CYS A 484
SHEET 3 AA8 5 VAL A 530 LYS A 534 1 O PHE A 532 N CYS A 450
SHEET 4 AA8 5 TYR A 426 LYS A 433 -1 N VAL A 431 O ALA A 531
SHEET 5 AA8 5 ALA A 580 ALA A 582 -1 O ALA A 582 N TYR A 426
SSBOND 1 CYS A 9 CYS A 48 1555 1555 2.01
SSBOND 2 CYS A 19 CYS A 39 1555 1555 2.03
SSBOND 3 CYS A 118 CYS A 194 1555 1555 2.01
SSBOND 4 CYS A 137 CYS A 331 1555 1555 2.03
SSBOND 5 CYS A 158 CYS A 174 1555 1555 2.00
SSBOND 6 CYS A 161 CYS A 179 1555 1555 2.00
SSBOND 7 CYS A 171 CYS A 177 1555 1555 2.03
SSBOND 8 CYS A 227 CYS A 241 1555 1555 2.03
SSBOND 9 CYS A 339 CYS A 596 1555 1555 2.08
SSBOND 10 CYS A 345 CYS A 377 1555 1555 2.03
SSBOND 11 CYS A 355 CYS A 368 1555 1555 2.03
SSBOND 12 CYS A 402 CYS A 674 1555 1555 2.03
SSBOND 13 CYS A 450 CYS A 523 1555 1555 2.04
SSBOND 14 CYS A 474 CYS A 665 1555 1555 2.04
SSBOND 15 CYS A 484 CYS A 498 1555 1555 2.03
SSBOND 16 CYS A 495 CYS A 506 1555 1555 2.01
SSBOND 17 CYS A 563 CYS A 577 1555 1555 2.03
LINK NE2 HIS A 14 RU RU A 703 1555 1555 2.33
LINK NE2 HIS A 289 RU RU A 703 1555 1555 2.56
LINK OD1 ASP A 392 FE FE A 701 1555 1555 2.23
LINK OH TYR A 426 FE FE A 701 1555 1555 2.19
LINK OH TYR A 517 FE FE A 701 1555 1555 1.93
LINK NE2 HIS A 585 FE FE A 701 1555 1555 2.24
LINK FE FE A 701 O7 MLI A 702 1555 1555 1.98
LINK FE FE A 701 O9 MLI A 702 1555 1555 2.06
LINK RU RU A 703 O HOH A 916 1555 1555 2.23
LINK RU RU A 703 O HOH A 946 1555 1555 2.68
LINK RU RU A 703 O HOH A 948 1555 1555 2.55
CISPEP 1 ALA A 73 PRO A 74 0 2.37
CISPEP 2 GLU A 141 PRO A 142 0 2.13
CISPEP 3 LYS A 144 PRO A 145 0 -1.92
CISPEP 4 GLY A 258 LYS A 259 0 2.59
SITE 1 AC1 5 ASP A 392 TYR A 426 TYR A 517 HIS A 585
SITE 2 AC1 5 MLI A 702
SITE 1 AC2 11 ASP A 392 TYR A 426 THR A 452 ARG A 456
SITE 2 AC2 11 THR A 457 ALA A 458 GLY A 459 TYR A 517
SITE 3 AC2 11 HIS A 585 FE A 701 HOH A 820
SITE 1 AC3 6 HIS A 14 HIS A 289 HOH A 916 HOH A 946
SITE 2 AC3 6 HOH A 948 HOH A 954
CRYST1 137.113 157.351 107.086 90.00 90.00 90.00 C 2 2 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 0.007293 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006355 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009338 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
