HEADER METAL TRANSPORT 04-SEP-00 1FQE
TITLE CRYSTAL STRUCTURES OF MUTANT (K206A) THAT ABOLISH THE DILYSINE
TITLE 2 INTERACTION IN THE N-LOBE OF HUMAN TRANSFERRIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEROTRANSFERRIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-LOBE;
COMPND 5 SYNONYM: SERUM TRANSFERRIN;
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_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNUT-BHK
KEYWDS IRON TRANSPORT, TRANSFERRIN, N-LOBE, IRON-RELEASE, DILYSINE
KEYWDS 2 INTERACTION, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR D.NURIZZO,H.M.BAKER,E.N.BAKER
REVDAT 3 03-NOV-21 1FQE 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1FQE 1 VERSN
REVDAT 1 16-MAY-01 1FQE 0
JRNL AUTH D.NURIZZO,H.M.BAKER,Q.Y.HE,R.T.MACGILLIVRAY,A.B.MASON,
JRNL AUTH 2 R.C.WOODWORTH,E.N.BAKER
JRNL TITL CRYSTAL STRUCTURES AND IRON RELEASE PROPERTIES OF MUTANTS
JRNL TITL 2 (K206A AND K296A) THAT ABOLISH THE DILYSINE INTERACTION IN
JRNL TITL 3 THE N-LOBE OF HUMAN TRANSFERRIN.
JRNL REF BIOCHEMISTRY V. 40 1616 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11327820
JRNL DOI 10.1021/BI002050M
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.2
REMARK 3 NUMBER OF REFLECTIONS : 29721
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 SET) : 0.196
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1182
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4209
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE : 0.2510
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 168
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2547
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 442
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.63000
REMARK 3 B22 (A**2) : 5.42000
REMARK 3 B33 (A**2) : -8.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.18
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) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.14
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.210
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.760 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.300 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.330 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.130 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.29
REMARK 3 BSOL : 24.09
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN.PARAM
REMARK 3 PARAMETER FILE 2 : CARBONATE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : &_1_PARAMETER_INFILE_5
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBONATE.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : &_1_TOPOLOGY_INFILE_
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FQE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-00.
REMARK 100 THE DEPOSITION ID IS D_1000011817.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-FEB-00
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0800
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29721
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 14.730
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.400
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000
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) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.18500
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: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-25% POLYETHYLENEGLYCOL 3350, 100MM
REMARK 280 POTASSIUM ACETATE, PH 7.4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 21.95000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.95000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.65000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.95000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.95000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.65000
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 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A
REMARK 300 MONOMER CONSTITUTED BY TWO
REMARK 300 DOMAINS IN BETWEEN THE IRON
REMARK 300 AND ITS CARBONATE COUNTERPART
REMARK 300 ARE LINKED.
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 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 ARG A 327 NE - CZ - NH2 ANGL. DEV. = 3.4 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 LYS A 4 24.24 -145.12
REMARK 500 SER A 12 174.46 75.40
REMARK 500 SER A 32 10.01 -61.82
REMARK 500 THR A 93 35.92 -98.84
REMARK 500 SER A 125 -76.65 -48.23
REMARK 500 TRP A 128 -65.67 -141.13
REMARK 500 CYS A 161 -6.33 85.23
REMARK 500 CYS A 174 77.55 -156.00
REMARK 500 CYS A 179 44.96 -100.33
REMARK 500 CYS A 241 69.79 -155.29
REMARK 500 ALA A 244 167.15 179.33
REMARK 500 SER A 287 145.11 -171.13
REMARK 500 SER A 287 142.77 -170.96
REMARK 500 LEU A 294 -44.91 75.01
REMARK 500 PRO A 306 151.43 -49.15
REMARK 500 ARG A 308 12.16 59.53
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 A 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 63 OD2
REMARK 620 2 TYR A 95 OH 90.4
REMARK 620 3 TYR A 188 OH 176.3 93.3
REMARK 620 4 HIS A 249 NE2 90.3 94.2 89.2
REMARK 620 5 CO3 A 600 O3 83.1 95.0 96.8 168.7
REMARK 620 6 CO3 A 600 O2 87.2 157.5 89.5 108.2 62.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 700 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 151 O
REMARK 620 2 ASN A 152 O 78.2
REMARK 620 3 PHE A 154 O 64.1 76.9
REMARK 620 4 GLN A 169 NE2 84.1 156.4 81.4
REMARK 620 5 GLN A 169 OE1 66.9 139.3 104.2 39.5
REMARK 620 6 HOH A 799 O 102.6 89.9 162.7 109.2 78.4
REMARK 620 7 HOH A 846 O 140.5 137.1 101.7 56.7 83.2 95.6
REMARK 620 N 1 2 3 4 5 6
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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 700
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FQF RELATED DB: PDB
REMARK 900 1FQF CONTAINS K296A HUMAN SERUM TRANSFERRIN.
REMARK 900 RELATED ID: 1A8E RELATED DB: PDB
REMARK 900 1A8E CONTAINS WILDTYPE HUMAN SERUM TRANSFERRIN.
DBREF 1FQE A 1 331 UNP P02787 TRFE_HUMAN 20 350
SEQADV 1FQE ALA A 206 UNP P02787 LYS 225 ENGINEERED MUTATION
SEQRES 1 A 331 VAL PRO ASP LYS THR VAL ARG TRP CYS ALA VAL SER GLU
SEQRES 2 A 331 HIS GLU ALA THR LYS CYS GLN SER PHE ARG ASP HIS MET
SEQRES 3 A 331 LYS SER VAL ILE PRO SER ASP GLY PRO SER VAL ALA CYS
SEQRES 4 A 331 VAL LYS LYS ALA SER TYR LEU ASP CYS ILE ARG ALA ILE
SEQRES 5 A 331 ALA ALA ASN GLU ALA ASP ALA VAL THR LEU ASP ALA GLY
SEQRES 6 A 331 LEU VAL TYR ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS
SEQRES 7 A 331 PRO VAL VAL ALA GLU PHE TYR GLY SER LYS GLU ASP PRO
SEQRES 8 A 331 GLN THR PHE TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP
SEQRES 9 A 331 SER GLY PHE GLN MET ASN GLN LEU ARG GLY LYS LYS SER
SEQRES 10 A 331 CYS HIS THR GLY LEU GLY ARG SER ALA GLY TRP ASN ILE
SEQRES 11 A 331 PRO ILE GLY LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG
SEQRES 12 A 331 LYS PRO LEU GLU LYS ALA VAL ALA ASN PHE PHE SER GLY
SEQRES 13 A 331 SER CYS ALA PRO CYS ALA ASP GLY THR ASP PHE PRO GLN
SEQRES 14 A 331 LEU CYS GLN LEU CYS PRO GLY CYS GLY CYS SER THR LEU
SEQRES 15 A 331 ASN GLN TYR PHE GLY TYR SER GLY ALA PHE LYS CYS LEU
SEQRES 16 A 331 LYS ASP GLY ALA GLY ASP VAL ALA PHE VAL ALA HIS SER
SEQRES 17 A 331 THR ILE PHE GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP
SEQRES 18 A 331 GLN TYR GLU LEU LEU CYS LEU ASP ASN THR ARG LYS PRO
SEQRES 19 A 331 VAL ASP GLU TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO
SEQRES 20 A 331 SER HIS THR VAL VAL ALA ARG SER MET GLY GLY LYS GLU
SEQRES 21 A 331 ASP LEU ILE TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS
SEQRES 22 A 331 PHE GLY LYS ASP LYS SER LYS GLU PHE GLN LEU PHE SER
SEQRES 23 A 331 SER PRO HIS GLY LYS ASP LEU LEU PHE LYS ASP SER ALA
SEQRES 24 A 331 HIS GLY PHE LEU LYS VAL PRO PRO ARG MET ASP ALA LYS
SEQRES 25 A 331 MET TYR LEU GLY TYR GLU TYR VAL THR ALA ILE ARG ASN
SEQRES 26 A 331 LEU ARG GLU GLY THR CYS
HET FE A 500 1
HET CO3 A 600 4
HET K A 700 1
HETNAM FE FE (III) ION
HETNAM CO3 CARBONATE ION
HETNAM K POTASSIUM ION
FORMUL 2 FE FE 3+
FORMUL 3 CO3 C O3 2-
FORMUL 4 K K 1+
FORMUL 5 HOH *442(H2 O)
HELIX 1 1 SER A 12 ILE A 30 1 19
HELIX 2 2 SER A 44 ALA A 54 1 11
HELIX 3 3 ASP A 63 LEU A 72 1 10
HELIX 4 4 GLN A 108 LEU A 112 5 5
HELIX 5 5 TRP A 128 TYR A 136 1 9
HELIX 6 6 CYS A 137 LEU A 139 5 3
HELIX 7 7 PRO A 145 PHE A 154 1 10
HELIX 8 8 PHE A 167 GLN A 172 5 6
HELIX 9 9 PHE A 186 ASP A 197 1 12
HELIX 10 10 SER A 208 LEU A 214 1 7
HELIX 11 11 ASN A 216 ASP A 221 1 6
HELIX 12 12 PRO A 234 CYS A 241 5 8
HELIX 13 13 LYS A 259 GLY A 275 1 17
HELIX 14 14 ASP A 310 GLY A 316 1 7
HELIX 15 15 GLY A 316 GLU A 328 1 13
SHEET 1 A 2 THR A 5 VAL A 11 0
SHEET 2 A 2 SER A 36 LYS A 42 1 O SER A 36 N VAL A 6
SHEET 1 B 4 VAL A 60 LEU A 62 0
SHEET 2 B 4 THR A 250 ALA A 253 -1 N THR A 250 O LEU A 62
SHEET 3 B 4 LYS A 78 PHE A 84 -1 N LYS A 78 O ALA A 253
SHEET 4 B 4 GLY A 301 LYS A 304 -1 O GLY A 301 N PHE A 84
SHEET 1 C 6 SER A 157 CYS A 158 0
SHEET 2 C 6 SER A 117 HIS A 119 1 O SER A 117 N CYS A 158
SHEET 3 C 6 VAL A 202 ALA A 206 1 O VAL A 202 N CYS A 118
SHEET 4 C 6 PHE A 94 LYS A 102 -1 N VAL A 98 O VAL A 205
SHEET 5 C 6 TYR A 223 CYS A 227 -1 N GLU A 224 O VAL A 101
SHEET 6 C 6 THR A 231 LYS A 233 -1 O THR A 231 N CYS A 227
SHEET 1 D 5 SER A 157 CYS A 158 0
SHEET 2 D 5 SER A 117 HIS A 119 1 O SER A 117 N CYS A 158
SHEET 3 D 5 VAL A 202 ALA A 206 1 O VAL A 202 N CYS A 118
SHEET 4 D 5 PHE A 94 LYS A 102 -1 N VAL A 98 O VAL A 205
SHEET 5 D 5 ALA A 244 PRO A 247 -1 O ALA A 244 N ALA A 97
SSBOND 1 CYS A 9 CYS A 48 1555 1555 2.03
SSBOND 2 CYS A 19 CYS A 39 1555 1555 2.04
SSBOND 3 CYS A 118 CYS A 194 1555 1555 2.03
SSBOND 4 CYS A 137 CYS A 331 1555 1555 2.03
SSBOND 5 CYS A 158 CYS A 174 1555 1555 2.03
SSBOND 6 CYS A 161 CYS A 179 1555 1555 2.03
SSBOND 7 CYS A 171 CYS A 177 1555 1555 2.03
SSBOND 8 CYS A 227 CYS A 241 1555 1555 2.03
LINK OD2 ASP A 63 FE FE A 500 1555 1555 2.12
LINK OH TYR A 95 FE FE A 500 1555 1555 1.98
LINK O ALA A 151 K K A 700 1555 1555 2.98
LINK O ASN A 152 K K A 700 1555 1555 2.93
LINK O PHE A 154 K K A 700 1555 1555 2.65
LINK NE2 GLN A 169 K K A 700 1555 1555 3.50
LINK OE1 GLN A 169 K K A 700 1555 1555 2.98
LINK OH TYR A 188 FE FE A 500 1555 1555 2.04
LINK NE2 HIS A 249 FE FE A 500 1555 1555 2.15
LINK FE FE A 500 O3 CO3 A 600 1555 1555 2.17
LINK FE FE A 500 O2 CO3 A 600 1555 1555 2.22
LINK K K A 700 O HOH A 799 1555 1555 2.68
LINK K K A 700 O HOH A 846 1555 1555 3.19
CISPEP 1 ALA A 73 PRO A 74 0 -1.49
CISPEP 2 GLU A 141 PRO A 142 0 -0.09
CISPEP 3 LYS A 144 PRO A 145 0 0.64
SITE 1 AC1 5 ASP A 63 TYR A 95 TYR A 188 HIS A 249
SITE 2 AC1 5 CO3 A 600
SITE 1 AC2 10 ASP A 63 TYR A 95 THR A 120 ARG A 124
SITE 2 AC2 10 SER A 125 ALA A 126 GLY A 127 TYR A 188
SITE 3 AC2 10 HIS A 249 FE A 500
SITE 1 AC3 5 ALA A 151 ASN A 152 PHE A 154 GLN A 169
SITE 2 AC3 5 HOH A 799
CRYST1 43.900 57.300 135.900 90.00 90.00 90.00 P 21 21 21 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 0.022779 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017452 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007358 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
