[Scop | Full Entry | Seq (local cached copy) | More Options ]
HEADER TRANSPORT PROTEIN 07-JUN-06 2H8F TITLE CRYSTAL STRUCTURE OF DEOXY HEMOGLOBIN FROM TREMATOMUS TITLE 2 BERNACCHII AT PH 6.2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN ALPHA SUBUNIT; COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: HEMOGLOBIN ALPHA CHAIN, ALPHA-GLOBIN; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEMOGLOBIN BETA SUBUNIT; COMPND 7 CHAIN: B, D; COMPND 8 SYNONYM: HEMOGLOBIN BETA CHAIN, BETA-GLOBIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PAGOTHENIA BERNACCHII; SOURCE 3 ORGANISM_COMMON: FISH; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: PAGOTHENIA BERNACCHII; SOURCE 6 ORGANISM_COMMON: FISH KEYWDS ROOT EFFECT, PH, COOPERATIVITY, HEMOGLOBIN, ALLOSTERY, HIGH KEYWDS 2 RESOLUTION EXPDTA X-RAY DIFFRACTION AUTHOR L.MAZZARELLA,A.VERGARA,L.VITAGLIANO,A.MERLINO,G.BONOMI, AUTHOR 2 S.SCALA,C.VERDE,G.DI PRISCO REVDAT 2 10-OCT-06 2H8F 1 JRNL REVDAT 1 29-AUG-06 2H8F 0 JRNL AUTH L.MAZZARELLA,A.VERGARA,L.VITAGLIANO,A.MERLINO, JRNL AUTH 2 G.BONOMI,S.SCALA,C.VERDE,G.DI PRISCO JRNL TITL HIGH RESOLUTION CRYSTAL STRUCTURE OF DEOXY JRNL TITL 2 HEMOGLOBIN FROM TREMATOMUS BERNACCHII AT DIFFERENT JRNL TITL 3 PH VALUES: THE ROLE OF HISTIDINE RESIDUES IN JRNL TITL 4 MODULATING THE STRENGTH OF THE ROOT EFFECT. JRNL REF PROTEINS V. 65 490 2006 JRNL REFN ASTM PSFGEY US ISSN 0887-3585 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH L.MAZZARELLA,G.BONOMI,M.C.LUBRANO,A.MERLINO, REMARK 1 AUTH 2 A.RICCIO,A.VERGARA,L.VITAGLIANO,C.VERDE,G.DI PRISCO REMARK 1 TITL MINIMAL STRUCTURAL REQUIREMENTS FOR ROOT EFFECT: REMARK 1 TITL 2 CRYSTAL STRUCTURE OF THE CATHODIC HEMOGLOBIN REMARK 1 TITL 3 ISOLATED FROM THE ANTARCTIC FISH TREMATOMUS NEWNESI REMARK 1 REF PROTEINS V. 62 316 2006 REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 REMARK 1 REFERENCE 2 REMARK 1 AUTH L.MAZZARELLA,R.D'AVINO,G.DI PRISCO,C.SAVINO, REMARK 1 AUTH 2 L.VITAGLIANO,P.C.E.MOODY,A.ZAGARI REMARK 1 TITL CRYSTAL STRUCTURE OF TREMATOMUS NEWNESI REMARK 1 TITL 2 HAEMOGLOBIN RE-OPENS THE ROOT EFFECT QUESTION REMARK 1 REF J.MOL.BIOL. V. 287 897 1999 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 1.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SHELXL-97 REMARK 3 AUTHORS : G.M.SHELDRICK REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.83 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.156 REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.151 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.172 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 7536 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 150602 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4508 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 172 REMARK 3 SOLVENT ATOMS : 511 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL REMARK 3 NUMBER OF RESTRAINTS : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.012 REMARK 3 ANGLE DISTANCES (A) : 3.000 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: NULL REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: CRYSTALS USED FOR STRUCTURE REMARK 3 DETERMINATION PRESENT PSEUDO-MEROHEDRAL TWINNING REMARK 4 REMARK 4 2H8F 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 3.101 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE RCSB ID CODE IS RCSB038059. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-OCT-2000 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.20 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-4 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 150761 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300 REMARK 200 RESOLUTION RANGE LOW (A) : 19.830 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 86.3 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.46 REMARK 200 COMPLETENESS FOR SHELL (%) : 57.2 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.89 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: DEOXY-HBTB 8-9.5 MG/ML MIXED WITH REMARK 280 EQUAL AMOUNT OF 7-12 % W/V PEG 6000, PBS 100 MM, PH 6.2, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -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 47.52100 REMARK 290 SMTRY3 2 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 4 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, C, 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 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 N SER A 1 O ACE A 0 2.14 REMARK 500 N SER C 1 O ACE C 0 2.19 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2AA1 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE CATHODIC HEMOLGLOBIN ISOLATED FROM REMARK 900 THE ANTARCTIC FISH TREMATOMUS NEWNESI REMARK 900 RELATED ID: 2H8D RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF DEOXY HEMOGLOBIN FROM TREMATOMUS REMARK 900 BERNACCHII AT PH 8.4 DBREF 2H8F A 1 142 UNP P80043 HBA_PAGBE 1 142 DBREF 2H8F C 1 142 UNP P80043 HBA_PAGBE 1 142 DBREF 2H8F B 1 146 UNP P80044 HBB_PAGBE 1 146 DBREF 2H8F D 1 146 UNP P80044 HBB_PAGBE 1 146 SEQRES 1 A 142 SER LEU SER ASP LYS ASP LYS ALA ALA VAL ARG ALA LEU SEQRES 2 A 142 TRP SER LYS ILE GLY LYS SER ALA ASP ALA ILE GLY ASN SEQRES 3 A 142 ASP ALA LEU SER ARG MET ILE VAL VAL TYR PRO GLN THR SEQRES 4 A 142 LYS THR TYR PHE SER HIS TRP PRO ASP VAL THR PRO GLY SEQRES 5 A 142 SER PRO HIS ILE LYS ALA HIS GLY LYS LYS VAL MET GLY SEQRES 6 A 142 GLY ILE ALA LEU ALA VAL SER LYS ILE ASP ASP LEU LYS SEQRES 7 A 142 THR GLY LEU MET GLU LEU SER GLU GLN HIS ALA TYR LYS SEQRES 8 A 142 LEU ARG VAL ASP PRO ALA ASN PHE LYS ILE LEU ASN HIS SEQRES 9 A 142 CYS ILE LEU VAL VAL ILE SER THR MET PHE PRO LYS GLU SEQRES 10 A 142 PHE THR PRO GLU ALA HIS VAL SER LEU ASP LYS PHE LEU SEQRES 11 A 142 SER GLY VAL ALA LEU ALA LEU ALA GLU ARG TYR ARG SEQRES 1 B 146 VAL GLU TRP THR ASP LYS GLU ARG SER ILE ILE SER ASP SEQRES 2 B 146 ILE PHE SER HIS MET ASP TYR ASP ASP ILE GLY PRO LYS SEQRES 3 B 146 ALA LEU SER ARG CYS LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 B 146 ARG HIS PHE SER GLY PHE GLY ASN LEU TYR ASN ALA GLU SEQRES 5 B 146 ALA ILE ILE GLY ASN ALA ASN VAL ALA ALA HIS GLY ILE SEQRES 6 B 146 LYS VAL LEU HIS GLY LEU ASP ARG GLY VAL LYS ASN MET SEQRES 7 B 146 ASP ASN ILE ALA ALA THR TYR ALA ASP LEU SER THR LEU SEQRES 8 B 146 HIS SER GLU LYS LEU HIS VAL ASP PRO ASP ASN PHE LYS SEQRES 9 B 146 LEU LEU SER ASP CYS ILE THR ILE VAL LEU ALA ALA LYS SEQRES 10 B 146 MET GLY HIS ALA PHE THR ALA GLU THR GLN GLY ALA PHE SEQRES 11 B 146 GLN LYS PHE LEU ALA VAL VAL VAL SER ALA LEU GLY LYS SEQRES 12 B 146 GLN TYR HIS SEQRES 1 C 142 SER LEU SER ASP LYS ASP LYS ALA ALA VAL ARG ALA LEU SEQRES 2 C 142 TRP SER LYS ILE GLY LYS SER ALA ASP ALA ILE GLY ASN SEQRES 3 C 142 ASP ALA LEU SER ARG MET ILE VAL VAL TYR PRO GLN THR SEQRES 4 C 142 LYS THR TYR PHE SER HIS TRP PRO ASP VAL THR PRO GLY SEQRES 5 C 142 SER PRO HIS ILE LYS ALA HIS GLY LYS LYS VAL MET GLY SEQRES 6 C 142 GLY ILE ALA LEU ALA VAL SER LYS ILE ASP ASP LEU LYS SEQRES 7 C 142 THR GLY LEU MET GLU LEU SER GLU GLN HIS ALA TYR LYS SEQRES 8 C 142 LEU ARG VAL ASP PRO ALA ASN PHE LYS ILE LEU ASN HIS SEQRES 9 C 142 CYS ILE LEU VAL VAL ILE SER THR MET PHE PRO LYS GLU SEQRES 10 C 142 PHE THR PRO GLU ALA HIS VAL SER LEU ASP LYS PHE LEU SEQRES 11 C 142 SER GLY VAL ALA LEU ALA LEU ALA GLU ARG TYR ARG SEQRES 1 D 146 VAL GLU TRP THR ASP LYS GLU ARG SER ILE ILE SER ASP SEQRES 2 D 146 ILE PHE SER HIS MET ASP TYR ASP ASP ILE GLY PRO LYS SEQRES 3 D 146 ALA LEU SER ARG CYS LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 D 146 ARG HIS PHE SER GLY PHE GLY ASN LEU TYR ASN ALA GLU SEQRES 5 D 146 ALA ILE ILE GLY ASN ALA ASN VAL ALA ALA HIS GLY ILE SEQRES 6 D 146 LYS VAL LEU HIS GLY LEU ASP ARG GLY VAL LYS ASN MET SEQRES 7 D 146 ASP ASN ILE ALA ALA THR TYR ALA ASP LEU SER THR LEU SEQRES 8 D 146 HIS SER GLU LYS LEU HIS VAL ASP PRO ASP ASN PHE LYS SEQRES 9 D 146 LEU LEU SER ASP CYS ILE THR ILE VAL LEU ALA ALA LYS SEQRES 10 D 146 MET GLY HIS ALA PHE THR ALA GLU THR GLN GLY ALA PHE SEQRES 11 D 146 GLN LYS PHE LEU ALA VAL VAL VAL SER ALA LEU GLY LYS SEQRES 12 D 146 GLN TYR HIS HET ACE A 0 3 HET ACE C 0 3 HET HEM A 200 43 HET HEM B 400 43 HET HEM C 600 43 HET HEM D 800 43 HETNAM ACE ACETYL GROUP HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 5 ACE 2(C2 H4 O) FORMUL 7 HEM 4(C34 H32 FE N4 O4) FORMUL 11 HOH *511(H2 O) HELIX 1 1 SER A 3 GLY A 18 1 16 HELIX 2 2 SER A 20 TYR A 36 1 17 HELIX 3 3 PRO A 37 SER A 44 5 8 HELIX 4 4 SER A 53 LYS A 73 1 21 HELIX 5 5 ASP A 76 LEU A 81 1 6 HELIX 6 6 LEU A 81 LYS A 91 1 11 HELIX 7 7 PRO A 96 PHE A 114 1 19 HELIX 8 8 THR A 119 ALA A 138 1 20 HELIX 9 9 THR B 4 MET B 18 1 15 HELIX 10 10 ASP B 19 TYR B 35 1 17 HELIX 11 11 PRO B 36 PHE B 42 5 7 HELIX 12 12 ASN B 50 GLY B 56 1 7 HELIX 13 13 ASN B 57 GLY B 70 1 14 HELIX 14 14 LEU B 71 LYS B 76 1 6 HELIX 15 15 ASN B 80 TYR B 85 1 6 HELIX 16 16 TYR B 85 LYS B 95 1 11 HELIX 17 17 PRO B 100 GLY B 119 1 20 HELIX 18 18 HIS B 120 PHE B 122 5 3 HELIX 19 19 THR B 123 GLN B 144 1 22 HELIX 20 20 SER C 3 GLY C 18 1 16 HELIX 21 21 SER C 20 TYR C 36 1 17 HELIX 22 22 PRO C 37 SER C 44 5 8 HELIX 23 23 SER C 53 LYS C 73 1 21 HELIX 24 24 ASP C 76 LEU C 81 1 6 HELIX 25 25 LEU C 81 LYS C 91 1 11 HELIX 26 26 PRO C 96 PHE C 114 1 19 HELIX 27 27 THR C 119 ALA C 138 1 20 HELIX 28 28 THR D 4 HIS D 17 1 14 HELIX 29 29 ASP D 19 TYR D 35 1 17 HELIX 30 30 PRO D 36 GLY D 46 5 11 HELIX 31 31 ASN D 50 GLY D 56 1 7 HELIX 32 32 ASN D 57 GLY D 70 1 14 HELIX 33 33 LEU D 71 ASN D 77 1 7 HELIX 34 34 ASN D 80 LYS D 95 1 16 HELIX 35 35 PRO D 100 GLY D 119 1 20 HELIX 36 36 HIS D 120 PHE D 122 5 3 HELIX 37 37 THR D 123 GLN D 144 1 22 LINK FE HEM A 200 NE2 HIS A 88 LINK FE HEM B 400 NE2 HIS B 92 LINK FE HEM C 600 NE2 HIS C 88 LINK FE HEM D 800 NE2 HIS D 92 LINK C ACE A 0 N SER A 1 LINK C ACE C 0 N SER C 1 CRYST1 61.850 95.042 61.824 90.00 90.19 90.00 P 1 21 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 0.016168 0.000000 0.000054 0.00000 SCALE2 0.000000 0.010522 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016175 0.00000