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HEADER OXYGEN STORAGE/TRANSPORT 12-DEC-03 1V75 TITLE CRYSTAL STRUCTURE OF HEMOGLOBIN D FROM THE ALDABRA GIANT TITLE 2 TORTOISE (GEOCHELONE GIGANTEA) AT 2.0 A RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN D ALPHA CHAIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: HEMOGLOBIN ALPHA-D CHAIN; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEMOGLOBIN A AND D BETA CHAIN; COMPND 7 CHAIN: B; COMPND 8 SYNONYM: HEMOGLOBIN BETA CHAIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ALDABRACHELYS ELEPHANTINA; SOURCE 3 ORGANISM_COMMON: ALDABRA GIANT TORTOISE; SOURCE 4 TISSUE: RED BLOOD CELL; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: ALDABRACHELYS ELEPHANTINA; SOURCE 7 ORGANISM_COMMON: ALDABRA GIANT TORTOISE; SOURCE 8 TISSUE: RED BLOOD CELL KEYWDS HEMOGLOBIN D, REPTILIA, THE ALDABRA GIANT TORTOISE, KEYWDS 2 GEOCHELONE GIGANTEA EXPDTA X-RAY DIFFRACTION AUTHOR T.KUWADA,T.HASEGAWA,I.SATOH,K.ISHIKAWA,F.SHISHIKURA REVDAT 1 30-DEC-03 1V75 0 JRNL AUTH T.KUWADA,T.HASEGAWA,I.SATOH,K.ISHIKAWA,F.SHISHIKURA JRNL TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION JRNL TITL 2 STUDY OF HEMOGLOBIN D FROM THE ALDABRA GIANT JRNL TITL 3 TORTOISE, GEOCHELONE GIGANTEA. JRNL REF PROTEIN PEPT.LETT. V. 10 422 2003 JRNL REFN ASTM PPELEN NE ISSN 0929-8665 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.02 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNX 2000.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN,MOLECULAR REMARK 3 : SIMULATIONS (BADGER,BERARD,KUMAR,SZALMA, REMARK 3 : YIP,DZAKULA) REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.96 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 411817.340 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.7 REMARK 3 NUMBER OF REFLECTIONS : 22778 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) : NULL REMARK 3 R VALUE (WORKING SET) : 0.188 REMARK 3 FREE R VALUE : 0.233 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900 REMARK 3 FREE R VALUE TEST SET COUNT : 2260 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA. REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL REMARK 3 FREE R VALUE (NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.02 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3419 REMARK 3 BIN R VALUE (WORKING SET) : 0.2610 REMARK 3 BIN FREE R VALUE : 0.2630 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 388 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2212 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 86 REMARK 3 SOLVENT ATOMS : 412 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 22.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.20 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -6.85000 REMARK 3 B22 (A**2) : 16.59000 REMARK 3 B33 (A**2) : -9.74000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.71000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22 REMARK 3 ESD FROM SIGMAA (A) : 0.23 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.27 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 1.10 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 16.00 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.71 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.40 REMARK 3 BSOL : 91.57 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : ION.PARAM REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 4 : HEM2.PARAM REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : ION.TOP REMARK 3 TOPOLOGY FILE 3 : WATER.TOP REMARK 3 TOPOLOGY FILE 4 : HEM2.TOP REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1V75 COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB006290. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-OCT-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.50 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 ULTRAX 18 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : CONFORCAL MAX-FLUX REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++ REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22787 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020 REMARK 200 RESOLUTION RANGE LOW (A) : 53.650 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8 REMARK 200 DATA REDUNDANCY : 2.780 REMARK 200 R MERGE (I) : 0.04000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 2.71 REMARK 200 R MERGE FOR SHELL (I) : 0.13500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.300 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: CNX 2000.1 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.89 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG3350, 50MM HEPES-NA, PH 7.5, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K 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 1/2+X,1/2+Y,Z REMARK 290 4555 1/2-X,1/2+Y,-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 56.07100 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.18700 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 56.07100 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.18700 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 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 -1.000000 0.000000 0.000000 112.14200 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 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 303 LIES ON A SPECIAL POSITION. REMARK 375 HOH 372 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 VAL B 1 REMARK 465 GLY B 144 REMARK 465 TYR B 145 REMARK 465 HIS B 146 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 HIS A 20 CG ND1 CD2 CE1 NE2 REMARK 470 LYS A 71 CB CG CD CE NZ REMARK 470 ALA A 78 CB REMARK 470 ARG A 141 CG CD NE CZ NH1 NH2 REMARK 470 HIS B 2 CB CG ND1 CD2 CE1 NE2 REMARK 470 LYS B 83 CG CD CE NZ REMARK 470 GLN B 87 CG CD OE1 NE2 REMARK 470 GLU B 90 CG CD OE1 OE2 REMARK 470 GLU B 94 CG CD OE1 OE2 REMARK 470 LYS B 120 CG CD CE NZ REMARK 470 LEU B 143 CG CD1 CD2 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 REMARK 500 FE HEM B 201 O HOH 412 2.01 REMARK 500 FE HEM A 201 O HOH 411 2.18 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 HOH 281 O HOH 281 2655 1.91 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 THR B 38 CA THR B 38 CB 0.038 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP A 47 N - CA - C ANGL. DEV. =-14.9 DEGREES REMARK 500 ASP A 51 N - CA - C ANGL. DEV. = 7.9 DEGREES REMARK 500 ASN B 19 N - CA - C ANGL. DEV. =-10.3 DEGREES REMARK 500 PRO B 36 N - CA - C ANGL. DEV. = 8.0 DEGREES REMARK 500 SER B 49 N - CA - C ANGL. DEV. = 7.3 DEGREES REMARK 500 LEU B 78 N - CA - C ANGL. DEV. = 7.2 DEGREES REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 3 DISTANCE = 6.49 ANGSTROMS REMARK 525 HOH 175 DISTANCE = 5.21 ANGSTROMS REMARK 525 HOH 178 DISTANCE = 6.07 ANGSTROMS REMARK 525 HOH 220 DISTANCE = 6.08 ANGSTROMS REMARK 525 HOH 221 DISTANCE = 6.28 ANGSTROMS REMARK 525 HOH 247 DISTANCE = 6.39 ANGSTROMS REMARK 525 HOH 249 DISTANCE = 8.43 ANGSTROMS REMARK 525 HOH 250 DISTANCE = 8.45 ANGSTROMS REMARK 525 HOH 251 DISTANCE = 9.12 ANGSTROMS REMARK 525 HOH 261 DISTANCE = 6.69 ANGSTROMS REMARK 525 HOH 264 DISTANCE = 12.67 ANGSTROMS REMARK 525 HOH 270 DISTANCE = 9.79 ANGSTROMS REMARK 525 HOH 271 DISTANCE = 5.16 ANGSTROMS REMARK 525 HOH 272 DISTANCE = 7.66 ANGSTROMS REMARK 525 HOH 274 DISTANCE = 6.35 ANGSTROMS REMARK 525 HOH 277 DISTANCE = 5.26 ANGSTROMS REMARK 525 HOH 279 DISTANCE = 5.82 ANGSTROMS REMARK 525 HOH 283 DISTANCE = 9.60 ANGSTROMS REMARK 525 HOH 286 DISTANCE = 12.93 ANGSTROMS REMARK 525 HOH 287 DISTANCE = 5.87 ANGSTROMS REMARK 525 HOH 288 DISTANCE = 7.50 ANGSTROMS REMARK 525 HOH 296 DISTANCE = 11.07 ANGSTROMS REMARK 525 HOH 297 DISTANCE = 6.94 ANGSTROMS REMARK 525 HOH 298 DISTANCE = 13.23 ANGSTROMS REMARK 525 HOH 299 DISTANCE = 10.01 ANGSTROMS REMARK 525 HOH 300 DISTANCE = 16.38 ANGSTROMS REMARK 525 HOH 301 DISTANCE = 14.52 ANGSTROMS REMARK 525 HOH 304 DISTANCE = 5.51 ANGSTROMS REMARK 525 HOH 306 DISTANCE = 12.51 ANGSTROMS REMARK 525 HOH 309 DISTANCE = 5.67 ANGSTROMS REMARK 525 HOH 310 DISTANCE = 9.22 ANGSTROMS REMARK 525 HOH 313 DISTANCE = 15.08 ANGSTROMS REMARK 525 HOH 315 DISTANCE = 6.99 ANGSTROMS REMARK 525 HOH 316 DISTANCE = 6.79 ANGSTROMS REMARK 525 HOH 318 DISTANCE = 6.76 ANGSTROMS REMARK 525 HOH 319 DISTANCE = 8.89 ANGSTROMS REMARK 525 HOH 320 DISTANCE = 9.69 ANGSTROMS REMARK 525 HOH 323 DISTANCE = 12.89 ANGSTROMS REMARK 525 HOH 325 DISTANCE = 15.00 ANGSTROMS REMARK 525 HOH 326 DISTANCE = 11.87 ANGSTROMS REMARK 525 HOH 331 DISTANCE = 15.06 ANGSTROMS REMARK 525 HOH 332 DISTANCE = 7.89 ANGSTROMS REMARK 525 HOH 334 DISTANCE = 22.62 ANGSTROMS REMARK 525 HOH 335 DISTANCE = 11.01 ANGSTROMS REMARK 525 HOH 342 DISTANCE = 8.71 ANGSTROMS REMARK 525 HOH 344 DISTANCE = 10.85 ANGSTROMS REMARK 525 HOH 347 DISTANCE = 9.93 ANGSTROMS REMARK 525 HOH 351 DISTANCE = 20.20 ANGSTROMS REMARK 525 HOH 354 DISTANCE = 10.11 ANGSTROMS REMARK 525 HOH 357 DISTANCE = 8.68 ANGSTROMS REMARK 525 HOH 358 DISTANCE = 7.41 ANGSTROMS REMARK 525 HOH 360 DISTANCE = 7.18 ANGSTROMS REMARK 525 HOH 369 DISTANCE = 6.26 ANGSTROMS REMARK 525 HOH 372 DISTANCE = 6.59 ANGSTROMS REMARK 525 HOH 374 DISTANCE = 8.10 ANGSTROMS REMARK 525 HOH 375 DISTANCE = 10.80 ANGSTROMS REMARK 525 HOH 376 DISTANCE = 18.79 ANGSTROMS REMARK 525 HOH 378 DISTANCE = 21.96 ANGSTROMS REMARK 525 HOH 379 DISTANCE = 8.98 ANGSTROMS REMARK 525 HOH 381 DISTANCE = 8.03 ANGSTROMS REMARK 525 HOH 386 DISTANCE = 7.58 ANGSTROMS REMARK 525 HOH 387 DISTANCE = 7.22 ANGSTROMS REMARK 525 HOH 392 DISTANCE = 5.13 ANGSTROMS REMARK 525 HOH 396 DISTANCE = 7.97 ANGSTROMS REMARK 525 HOH 397 DISTANCE = 21.41 ANGSTROMS REMARK 525 HOH 399 DISTANCE = 18.77 ANGSTROMS REMARK 525 HOH 401 DISTANCE = 7.09 ANGSTROMS REMARK 525 HOH 404 DISTANCE = 5.10 ANGSTROMS REMARK 525 HOH 405 DISTANCE = 7.82 ANGSTROMS REMARK 525 HOH 409 DISTANCE = 9.02 ANGSTROMS DBREF 1V75 A 1 141 UNP P83134 HBAD_ALDEL 1 141 DBREF 1V75 B 1 146 UNP P83133 HBB_ALDEL 1 146 SEQRES 1 A 141 MET LEU THR GLU ASP ASP LYS GLN LEU ILE GLN HIS VAL SEQRES 2 A 141 TRP GLU LYS VAL LEU GLU HIS GLN GLU ASP PHE GLY ALA SEQRES 3 A 141 GLU ALA LEU GLU ARG MET PHE ILE VAL TYR PRO SER THR SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASP LEU HIS HIS ASP SER SEQRES 5 A 141 GLU GLN ILE ARG HIS HIS GLY LYS LYS VAL VAL GLY ALA SEQRES 6 A 141 LEU GLY ASP ALA VAL LYS HIS ILE ASP ASN LEU SER ALA SEQRES 7 A 141 THR LEU SER GLU LEU SER ASN LEU HIS ALA TYR ASN LEU SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS SEQRES 9 A 141 PHE GLN VAL VAL LEU GLY ALA HIS LEU GLY ARG GLU TYR SEQRES 10 A 141 THR PRO GLN VAL GLN VAL ALA TYR ASP LYS PHE LEU ALA SEQRES 11 A 141 ALA VAL SER ALA VAL LEU ALA GLU LYS TYR ARG SEQRES 1 B 146 VAL HIS TRP THR SER GLU GLU LYS GLN TYR ILE THR SER SEQRES 2 B 146 LEU TRP ALA LYS VAL ASN VAL GLY GLU VAL GLY GLY GLU SEQRES 3 B 146 ALA LEU ALA ARG LEU LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 B 146 ARG PHE PHE ALA SER PHE GLY ASN LEU SER SER ALA ASN SEQRES 5 B 146 ALA ILE LEU HIS ASN ALA LYS VAL LEU ALA HIS GLY GLN SEQRES 6 B 146 LYS VAL LEU THR SER PHE GLY GLU ALA VAL LYS ASN LEU SEQRES 7 B 146 ASP ASN ILE LYS LYS THR PHE ALA GLN LEU SER GLU LEU SEQRES 8 B 146 HIS CYS GLU LYS LEU HIS VAL ASP PRO GLU ASN PHE LYS SEQRES 9 B 146 LEU LEU GLY ASN ILE LEU ILE ILE VAL LEU ALA THR HIS SEQRES 10 B 146 PHE PRO LYS GLU PHE THR PRO ALA SER GLN ALA ALA TRP SEQRES 11 B 146 THR LYS LEU VAL ASN ALA VAL ALA HIS ALA LEU ALA LEU SEQRES 12 B 146 GLY TYR HIS HET HEM A 201 43 HET HEM B 201 43 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 3 HEM 2(C34 H32 FE N4 O4) FORMUL 5 HOH *412(H2 O) HELIX 1 1 THR A 3 LEU A 18 1 16 HELIX 2 2 HIS A 20 TYR A 36 1 17 HELIX 3 3 PRO A 37 PHE A 43 5 7 HELIX 4 4 SER A 52 HIS A 72 1 21 HELIX 5 5 ASN A 75 ASN A 90 1 16 HELIX 6 6 ASP A 94 GLY A 114 1 21 HELIX 7 7 ARG A 115 TYR A 117 5 3 HELIX 8 8 THR A 118 GLU A 138 1 21 HELIX 9 9 LYS A 139 ARG A 141 5 3 HELIX 10 10 THR B 4 ALA B 16 1 13 HELIX 11 11 ASN B 19 TYR B 35 1 17 HELIX 12 12 PRO B 36 GLY B 46 5 11 HELIX 13 13 SER B 50 HIS B 56 1 7 HELIX 14 14 ASN B 57 LYS B 76 1 20 HELIX 15 15 ASN B 80 GLU B 94 1 15 HELIX 16 16 PRO B 100 PHE B 118 1 19 HELIX 17 17 THR B 123 LEU B 143 1 21 LINK FE HEM A 201 NE2 HIS A 87 LINK FE HEM B 201 NE2 HIS B 92 CRYST1 112.142 62.374 53.980 90.00 110.26 90.00 C 1 2 1 4 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 0.008917 0.000000 0.003292 0.00000 SCALE2 0.000000 0.016032 0.000000 0.00000 SCALE3 0.000000 0.000000 0.019747 0.00000