HEADER OXYGEN TRANSPORT 22-DEC-16 5UCU
TITLE STRUCTURAL AND MECHANISTIC INSIGHTS INTO HEMOGLOBIN-CATALYZED HYDROGEN
TITLE 2 SULFIDE OXIDATION AND THE FATE OF POLYSULFIDE PRODUCTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMOGLOBIN SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA-GLOBIN,HEMOGLOBIN ALPHA CHAIN;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HEMOGLOBIN SUBUNIT BETA;
COMPND 7 CHAIN: B;
COMPND 8 SYNONYM: BETA-GLOBIN,HEMOGLOBIN BETA CHAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606
KEYWDS MECHANISM OF HEMOGLOBIN CATALYZED H2S OXIDATION, OXYGEN TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR V.VITVITSKY,P.K.YADAV,S.AN,J.SERAVALLI,U.-S.CHO,R.BANERJEE
REVDAT 6 04-OCT-23 5UCU 1 LINK
REVDAT 5 25-DEC-19 5UCU 1 REMARK
REVDAT 4 27-NOV-19 5UCU 1 REMARK
REVDAT 3 27-SEP-17 5UCU 1 REMARK
REVDAT 2 12-APR-17 5UCU 1 JRNL
REVDAT 1 01-MAR-17 5UCU 0
JRNL AUTH V.VITVITSKY,P.K.YADAV,S.AN,J.SERAVALLI,U.S.CHO,R.BANERJEE
JRNL TITL STRUCTURAL AND MECHANISTIC INSIGHTS INTO
JRNL TITL 2 HEMOGLOBIN-CATALYZED HYDROGEN SULFIDE OXIDATION AND THE FATE
JRNL TITL 3 OF POLYSULFIDE PRODUCTS.
JRNL REF J. BIOL. CHEM. V. 292 5584 2017
JRNL REFN ESSN 1083-351X
JRNL PMID 28213526
JRNL DOI 10.1074/JBC.M117.774943
REMARK 2
REMARK 2 RESOLUTION. 1.80 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 27405
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.300
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 37.3113 - 4.3295 0.99 1996 157 0.1857 0.2035
REMARK 3 2 4.3295 - 3.4372 1.00 1879 148 0.1593 0.2105
REMARK 3 3 3.4372 - 3.0030 1.00 1841 145 0.1892 0.2287
REMARK 3 4 3.0030 - 2.7285 1.00 1830 144 0.1955 0.2512
REMARK 3 5 2.7285 - 2.5330 1.00 1821 144 0.1967 0.2159
REMARK 3 6 2.5330 - 2.3837 1.00 1801 142 0.1876 0.2480
REMARK 3 7 2.3837 - 2.2643 1.00 1806 142 0.1843 0.2279
REMARK 3 8 2.2643 - 2.1657 1.00 1789 140 0.1822 0.2317
REMARK 3 9 2.1657 - 2.0824 1.00 1795 141 0.1892 0.1869
REMARK 3 10 2.0824 - 2.0105 1.00 1781 141 0.1873 0.2080
REMARK 3 11 2.0105 - 1.9477 1.00 1778 139 0.1963 0.2122
REMARK 3 12 1.9477 - 1.8920 1.00 1778 141 0.2079 0.2617
REMARK 3 13 1.8920 - 1.8422 1.00 1779 139 0.2440 0.3055
REMARK 3 14 1.8422 - 1.7972 0.98 1731 137 0.2713 0.3283
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.770
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 2390
REMARK 3 ANGLE : 0.688 3292
REMARK 3 CHIRALITY : 0.041 358
REMARK 3 PLANARITY : 0.005 414
REMARK 3 DIHEDRAL : 6.391 1832
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 35 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9202 31.2329 -18.9182
REMARK 3 T TENSOR
REMARK 3 T11: 0.2253 T22: 0.4450
REMARK 3 T33: 0.2323 T12: 0.0374
REMARK 3 T13: 0.0321 T23: -0.0393
REMARK 3 L TENSOR
REMARK 3 L11: 2.9053 L22: 2.0461
REMARK 3 L33: 0.8912 L12: -0.2139
REMARK 3 L13: -0.2083 L23: -0.1946
REMARK 3 S TENSOR
REMARK 3 S11: 0.0955 S12: 0.5499 S13: 0.0630
REMARK 3 S21: -0.2569 S22: -0.0644 S23: -0.3268
REMARK 3 S31: -0.0635 S32: 0.2008 S33: 0.0139
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 36 THROUGH 71 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.4774 36.8917 -20.7698
REMARK 3 T TENSOR
REMARK 3 T11: 0.2343 T22: 0.3762
REMARK 3 T33: 0.2851 T12: 0.0514
REMARK 3 T13: 0.0258 T23: 0.0373
REMARK 3 L TENSOR
REMARK 3 L11: 2.4185 L22: 2.0988
REMARK 3 L33: 2.1318 L12: 0.6453
REMARK 3 L13: 0.8160 L23: -0.7674
REMARK 3 S TENSOR
REMARK 3 S11: 0.0541 S12: 0.5799 S13: 0.4991
REMARK 3 S21: -0.2485 S22: 0.0316 S23: 0.3186
REMARK 3 S31: -0.0860 S32: -0.0440 S33: -0.1110
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 72 THROUGH 80 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.5698 44.8447 -9.9396
REMARK 3 T TENSOR
REMARK 3 T11: 0.3122 T22: 0.4017
REMARK 3 T33: 0.3988 T12: -0.0807
REMARK 3 T13: -0.0391 T23: -0.0790
REMARK 3 L TENSOR
REMARK 3 L11: 6.3834 L22: 2.8444
REMARK 3 L33: 4.9828 L12: -2.2435
REMARK 3 L13: -2.4635 L23: 0.1698
REMARK 3 S TENSOR
REMARK 3 S11: 0.3797 S12: -0.8230 S13: 0.6838
REMARK 3 S21: 0.6301 S22: -0.0482 S23: -0.6143
REMARK 3 S31: -0.2216 S32: 0.3377 S33: -0.1771
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 81 THROUGH 94 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.9715 45.5975 -9.1950
REMARK 3 T TENSOR
REMARK 3 T11: 0.4447 T22: 0.2760
REMARK 3 T33: 0.4001 T12: 0.0829
REMARK 3 T13: 0.0849 T23: 0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 6.2224 L22: 8.2332
REMARK 3 L33: 3.9419 L12: 4.5778
REMARK 3 L13: -1.8733 L23: -1.8693
REMARK 3 S TENSOR
REMARK 3 S11: 0.3801 S12: -0.0375 S13: 1.0347
REMARK 3 S21: 0.9810 S22: 0.0632 S23: 0.3916
REMARK 3 S31: -1.4572 S32: -0.6382 S33: -0.4478
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 95 THROUGH 140 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.4745 30.5603 -11.8355
REMARK 3 T TENSOR
REMARK 3 T11: 0.1845 T22: 0.3003
REMARK 3 T33: 0.1845 T12: -0.0065
REMARK 3 T13: -0.0029 T23: -0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 2.6510 L22: 2.2184
REMARK 3 L33: 1.3396 L12: 0.9448
REMARK 3 L13: 0.2531 L23: -1.1755
REMARK 3 S TENSOR
REMARK 3 S11: 0.1368 S12: 0.1978 S13: -0.0304
REMARK 3 S21: 0.1088 S22: -0.1561 S23: -0.1215
REMARK 3 S31: 0.0138 S32: 0.1468 S33: -0.0150
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 22 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.3754 9.4703 -19.0134
REMARK 3 T TENSOR
REMARK 3 T11: 0.4958 T22: 0.3956
REMARK 3 T33: 0.4435 T12: -0.0628
REMARK 3 T13: -0.0672 T23: -0.1778
REMARK 3 L TENSOR
REMARK 3 L11: 4.4452 L22: 4.0372
REMARK 3 L33: 3.4486 L12: -2.1230
REMARK 3 L13: 1.6085 L23: -0.9545
REMARK 3 S TENSOR
REMARK 3 S11: 0.4248 S12: 0.4018 S13: -0.7117
REMARK 3 S21: -0.6388 S22: -0.0218 S23: 0.2333
REMARK 3 S31: 0.6704 S32: 0.0071 S33: -0.2770
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 23 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.6317 11.6173 -4.3584
REMARK 3 T TENSOR
REMARK 3 T11: 0.4094 T22: 0.2943
REMARK 3 T33: 0.3572 T12: 0.1371
REMARK 3 T13: -0.0329 T23: -0.0521
REMARK 3 L TENSOR
REMARK 3 L11: 1.4105 L22: 2.2906
REMARK 3 L33: 2.8887 L12: -0.4311
REMARK 3 L13: -0.6380 L23: 0.0185
REMARK 3 S TENSOR
REMARK 3 S11: -0.1005 S12: -0.0299 S13: -0.4746
REMARK 3 S21: 0.3304 S22: 0.0180 S23: -0.3119
REMARK 3 S31: 0.7382 S32: 0.4328 S33: 0.0389
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 78 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.0584 8.8882 2.4945
REMARK 3 T TENSOR
REMARK 3 T11: 0.6962 T22: 0.2913
REMARK 3 T33: 0.5522 T12: -0.0259
REMARK 3 T13: 0.0456 T23: -0.0246
REMARK 3 L TENSOR
REMARK 3 L11: 3.3318 L22: 4.0261
REMARK 3 L33: 3.4156 L12: 1.6183
REMARK 3 L13: 0.1911 L23: 0.9139
REMARK 3 S TENSOR
REMARK 3 S11: 0.1059 S12: -0.2654 S13: -0.4735
REMARK 3 S21: 1.0306 S22: -0.1834 S23: 0.8806
REMARK 3 S31: 0.9591 S32: -0.5210 S33: -0.1059
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 100 THROUGH 146 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5882 16.8482 -10.6832
REMARK 3 T TENSOR
REMARK 3 T11: 0.2398 T22: 0.2545
REMARK 3 T33: 0.3122 T12: 0.0019
REMARK 3 T13: -0.0259 T23: -0.0940
REMARK 3 L TENSOR
REMARK 3 L11: 1.8645 L22: 2.9027
REMARK 3 L33: 1.6931 L12: 0.2063
REMARK 3 L13: 0.5666 L23: -0.2798
REMARK 3 S TENSOR
REMARK 3 S11: 0.0582 S12: 0.2319 S13: -0.3051
REMARK 3 S21: 0.0970 S22: -0.0354 S23: 0.1313
REMARK 3 S31: 0.1755 S32: -0.1261 S33: -0.0368
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5UCU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1000225651.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-AUG-15
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1272
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27405
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.797
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 11.90
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.9700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 12.30
REMARK 200 R MERGE FOR SHELL (I) : 1.46300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3D7O
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% TOLUENE, 2.3 M K2HPO4/NH2PO4 PH,
REMARK 280 7.2., PH 7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 96.62700
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 26.88300
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 26.88300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 48.31350
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 26.88300
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 26.88300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 144.94050
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 26.88300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 26.88300
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 48.31350
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 26.88300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 26.88300
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 144.94050
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 96.62700
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -150.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 -53.76600
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 53.76600
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 392 LIES ON A SPECIAL POSITION.
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 ARG A 141
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 VAL A 1 CG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NZ LYS A 11 O HOH A 301 1.91
REMARK 500 O HOH A 363 O HOH A 374 1.97
REMARK 500 O HOH A 375 O HOH A 376 2.07
REMARK 500 NZ LYS A 11 O HOH A 302 2.15
REMARK 500 O HOH B 369 O HOH B 375 2.15
REMARK 500 NE2 HIS B 117 O HOH B 301 2.16
REMARK 500 O HOH A 374 O HOH A 389 2.17
REMARK 500 O HOH A 363 O HOH A 391 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 HYDROGEN SULFIDE H2S A203 FORMS HYDROGEN BOND WITH CARBOXYL GROUPS
REMARK 600 OF THE POLYPEPTIDE
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 H2S A 202 S
REMARK 620 2 HEM A 201 NA 94.5
REMARK 620 3 HEM A 201 NB 89.4 91.6
REMARK 620 4 HEM A 201 NC 85.0 177.9 90.4
REMARK 620 5 HEM A 201 ND 89.7 88.8 179.0 89.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 92 NE2
REMARK 620 2 HEM B 201 NA 86.2
REMARK 620 3 HEM B 201 NB 86.9 88.2
REMARK 620 4 HEM B 201 NC 89.0 175.2 90.9
REMARK 620 5 HEM B 201 ND 90.9 91.7 177.7 89.0
REMARK 620 6 H2S B 202 S 177.9 95.5 91.9 89.3 90.4
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 HEM A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H2S A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H2S A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H2S B 202
DBREF 5UCU A 1 141 UNP P69905 HBA_HUMAN 2 142
DBREF 5UCU B 1 146 UNP P68871 HBB_HUMAN 2 147
SEQRES 1 A 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 A 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 A 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 A 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
SEQRES 6 A 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 A 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 A 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 A 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 B 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
SEQRES 2 B 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU
SEQRES 3 B 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
SEQRES 4 B 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 B 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 B 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 B 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU
SEQRES 8 B 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 B 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS
SEQRES 10 B 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR
SEQRES 11 B 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 B 146 LYS TYR HIS
HET HEM A 201 43
HET H2S A 202 1
HET H2S A 203 1
HET HEM B 201 43
HET H2S B 202 1
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H2S HYDROSULFURIC ACID
HETSYN HEM HEME
HETSYN H2S HYDROGEN SULFIDE
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 H2S 3(H2 S)
FORMUL 8 HOH *169(H2 O)
HELIX 1 AA1 SER A 3 GLY A 18 1 16
HELIX 2 AA2 HIS A 20 PHE A 36 1 17
HELIX 3 AA3 PRO A 37 PHE A 43 5 7
HELIX 4 AA4 SER A 52 HIS A 72 1 21
HELIX 5 AA5 ASP A 75 LEU A 80 1 6
HELIX 6 AA6 LEU A 80 LYS A 90 1 11
HELIX 7 AA7 PRO A 95 LEU A 113 1 19
HELIX 8 AA8 THR A 118 THR A 137 1 20
HELIX 9 AA9 THR B 4 GLY B 16 1 13
HELIX 10 AB1 GLU B 22 TYR B 35 1 14
HELIX 11 AB2 PRO B 36 GLY B 46 5 11
HELIX 12 AB3 THR B 50 ASN B 57 1 8
HELIX 13 AB4 ASN B 57 HIS B 77 1 21
HELIX 14 AB5 ASN B 80 PHE B 85 1 6
HELIX 15 AB6 PHE B 85 LYS B 95 1 11
HELIX 16 AB7 PRO B 100 GLY B 119 1 20
HELIX 17 AB8 LYS B 120 PHE B 122 5 3
HELIX 18 AB9 THR B 123 ALA B 142 1 20
HELIX 19 AC1 HIS B 143 HIS B 146 5 4
LINK FE HEM A 201 S H2S A 202 1555 1555 2.22
LINK NE2 HIS B 92 FE HEM B 201 1555 1555 2.32
LINK FE HEM B 201 S H2S B 202 1555 1555 2.16
SITE 1 AC1 14 TYR A 42 PHE A 43 HIS A 45 PHE A 46
SITE 2 AC1 14 HIS A 58 LYS A 61 HIS A 87 LEU A 91
SITE 3 AC1 14 VAL A 93 ASN A 97 PHE A 98 LEU A 101
SITE 4 AC1 14 LEU A 136 H2S A 202
SITE 1 AC2 3 HIS A 58 VAL A 62 HEM A 201
SITE 1 AC3 4 PHE A 43 PRO A 44 PHE A 46 HOH A 355
SITE 1 AC4 16 PRO A 4 THR B 38 PHE B 41 PHE B 42
SITE 2 AC4 16 HIS B 63 LYS B 66 PHE B 71 LEU B 88
SITE 3 AC4 16 HIS B 92 LEU B 96 ASN B 102 LEU B 141
SITE 4 AC4 16 H2S B 202 HOH B 306 HOH B 314 HOH B 322
SITE 1 AC5 3 HIS B 63 VAL B 67 HEM B 201
CRYST1 53.766 53.766 193.254 90.00 90.00 90.00 P 41 21 2 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 0.018599 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018599 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005175 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
