HEADER METAL TRANSPORT 16-SEP-16 5TCY
TITLE A COMPLEX OF THE SYNTHETIC SIDEROPHORE ANALOGUE FE(III)-5-LICAM WITH
TITLE 2 CEUE (H227L VARIANT), A PERIPLASMIC PROTEIN FROM CAMPYLOBACTER
TITLE 3 JEJUNI.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENTEROCHELIN UPTAKE PERIPLASMIC BINDING PROTEIN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAMPYLOBACTER JEJUNI BJ-CJGB96299;
SOURCE 3 ORGANISM_TAXID: 1316921;
SOURCE 4 GENE: K680_0601;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PERIPLASMIC, IRON-UPTAKE, TETRADENTATE, SIDEROPHORE, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR E.J.WILDE,E.BLAGOVA,A.HUGHES,D.J.RAINES,O.V.MOROZ,J.P.TURKENBURG,A.-
AUTHOR 2 K.DUHME-KLAIR,K.S.WILSON
REVDAT 4 17-JAN-24 5TCY 1 LINK
REVDAT 3 13-SEP-17 5TCY 1 REMARK
REVDAT 2 19-APR-17 5TCY 1 JRNL
REVDAT 1 12-APR-17 5TCY 0
JRNL AUTH E.J.WILDE,A.HUGHES,E.V.BLAGOVA,O.V.MOROZ,R.P.THOMAS,
JRNL AUTH 2 J.P.TURKENBURG,D.J.RAINES,A.K.DUHME-KLAIR,K.S.WILSON
JRNL TITL INTERACTIONS OF THE PERIPLASMIC BINDING PROTEIN CEUE WITH
JRNL TITL 2 FE(III) N-LICAM(4-) SIDEROPHORE ANALOGUES OF VARIED LINKER
JRNL TITL 3 LENGTH.
JRNL REF SCI REP V. 7 45941 2017
JRNL REFN ESSN 2045-2322
JRNL PMID 28383577
JRNL DOI 10.1038/SREP45941
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.13
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 67360
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3451
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4889
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.2930
REMARK 3 BIN FREE R VALUE SET COUNT : 297
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6585
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 84
REMARK 3 SOLVENT ATOMS : 167
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.76000
REMARK 3 B22 (A**2) : -0.75000
REMARK 3 B33 (A**2) : -0.10000
REMARK 3 B12 (A**2) : -0.79000
REMARK 3 B13 (A**2) : 0.14000
REMARK 3 B23 (A**2) : 1.23000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.140
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.135
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.114
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.069
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6826 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6848 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9232 ; 1.850 ; 2.002
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15785 ; 1.041 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 877 ; 6.319 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 258 ;40.078 ;26.550
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1260 ;15.013 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;11.591 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1083 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7689 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1396 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3485 ; 2.858 ; 3.267
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3484 ; 2.858 ; 3.267
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4356 ; 3.798 ; 4.886
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4357 ; 3.798 ; 4.887
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3341 ; 4.149 ; 3.659
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3342 ; 4.148 ; 3.660
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4872 ; 6.277 ; 5.279
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 7478 ; 7.326 ;39.006
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 7461 ; 7.330 ;38.969
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5TCY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1000223805.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SILICON CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70811
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 67.130
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.95600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3ZKW
REMARK 200
REMARK 200 REMARK: ROD SHAPED CRYSTAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M PCB BUFFER, PH 8, 25% PEG 1500
REMARK 280 +CRYO 33% PEG 1500 IN WELL SOLUTION, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 GLY A 20
REMARK 465 PRO A 21
REMARK 465 GLY B 20
REMARK 465 LYS B 310
REMARK 465 GLY C 20
REMARK 465 PRO C 21
REMARK 465 ALA C 22
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 GLU A 31 CD OE1 OE2
REMARK 470 ASP A 33 CG OD1 OD2
REMARK 470 LYS A 83 CG CD CE NZ
REMARK 470 GLU A 183 CG CD OE1 OE2
REMARK 470 ASP A 184 CG OD1 OD2
REMARK 470 LYS A 223 CG CD CE NZ
REMARK 470 GLU A 234 CG CD OE1 OE2
REMARK 470 GLU A 238 CG CD OE1 OE2
REMARK 470 LYS A 256 CB CG CD CE NZ
REMARK 470 LYS A 270 CG CD CE NZ
REMARK 470 LYS A 272 CG CD CE NZ
REMARK 470 GLN A 275 CG CD OE1 NE2
REMARK 470 LYS A 277 CG CD CE NZ
REMARK 470 LYS A 310 N CG CD CE NZ
REMARK 470 PRO B 21 N CB CG CD
REMARK 470 ALA B 22 CB
REMARK 470 GLU B 31 OE1 OE2
REMARK 470 ASP B 33 CG OD1 OD2
REMARK 470 LYS B 38 CE NZ
REMARK 470 GLU B 43 CD OE1 OE2
REMARK 470 LYS B 45 CD CE NZ
REMARK 470 ASP B 71 CG OD1 OD2
REMARK 470 LYS B 79 NZ
REMARK 470 GLN B 99 CD OE1 NE2
REMARK 470 GLU B 103 OE1 OE2
REMARK 470 LYS B 109 CD CE NZ
REMARK 470 GLU B 147 CD OE1 OE2
REMARK 470 GLU B 165 CD OE1 OE2
REMARK 470 ASP B 169 OD1 OD2
REMARK 470 GLU B 175 OE1 OE2
REMARK 470 GLU B 183 CG CD OE1 OE2
REMARK 470 ASP B 184 CB CG OD1 OD2
REMARK 470 ASN B 216 OD1 ND2
REMARK 470 LYS B 223 CD CE NZ
REMARK 470 GLU B 238 CD OE1 OE2
REMARK 470 LYS C 79 CG CD CE NZ
REMARK 470 GLN C 99 CG CD OE1 NE2
REMARK 470 GLU C 103 CG CD OE1 OE2
REMARK 470 GLU C 183 CB CG CD OE1 OE2
REMARK 470 ASP C 219 OD1 OD2
REMARK 470 GLU C 220 CD OE1 OE2
REMARK 470 ASN C 221 CG OD1 ND2
REMARK 470 ILE C 222 CD1
REMARK 470 LYS C 223 CB CG CD CE NZ
REMARK 470 THR C 226 CG2
REMARK 470 LYS C 270 CD CE NZ
REMARK 470 LYS C 310 NZ
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 NE2 GLN A 98 O HOH A 501 2.11
REMARK 500
REMARK 500 REMARK: NULL
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 B 118 NE - CZ - NH1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ARG B 118 NE - CZ - NH2 ANGL. DEV. = -7.5 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 GLU A 31 43.60 -143.66
REMARK 500 SER A 116 -157.52 -125.52
REMARK 500 ASN A 141 56.66 -143.97
REMARK 500 SER A 194 -125.70 38.43
REMARK 500 ALA A 290 68.00 81.06
REMARK 500 SER A 291 34.98 -99.96
REMARK 500 LYS B 68 47.43 70.14
REMARK 500 SER B 116 -167.74 -123.13
REMARK 500 VAL B 135 64.82 -114.44
REMARK 500 ASN B 141 57.40 -146.23
REMARK 500 SER B 194 -121.47 47.32
REMARK 500 ALA B 290 67.22 72.12
REMARK 500 SER B 291 33.40 -95.80
REMARK 500 VAL C 135 57.41 -116.72
REMARK 500 SER C 194 -130.56 47.23
REMARK 500 THR C 226 -26.30 -39.34
REMARK 500 ALA C 290 77.85 65.27
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 401 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 288 OH
REMARK 620 2 5LC A 402 O23 154.8
REMARK 620 3 5LC A 402 O24 99.1 75.5
REMARK 620 4 5LC A 402 O26 98.3 106.5 93.0
REMARK 620 5 5LC A 402 O25 102.9 87.3 157.0 77.1
REMARK 620 6 HOH A 511 O 82.8 74.8 103.2 163.4 86.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 401 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 288 OH
REMARK 620 2 5LC B 402 O23 154.1
REMARK 620 3 5LC B 402 O24 101.2 77.8
REMARK 620 4 5LC B 402 O25 104.9 80.9 153.3
REMARK 620 5 5LC B 402 O26 101.4 104.4 94.2 75.5
REMARK 620 6 HOH B 503 O 71.7 82.7 96.8 96.4 168.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE C 401 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 288 OH
REMARK 620 2 5LC C 402 O23 111.6
REMARK 620 3 5LC C 402 O24 103.9 77.1
REMARK 620 4 5LC C 402 O25 97.5 90.7 158.1
REMARK 620 5 5LC C 402 O26 111.8 136.4 96.5 79.6
REMARK 620 N 1 2 3 4
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5LC A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5LC B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5LC C 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ZKW RELATED DB: PDB
REMARK 900 3ZKW IS THE NATIVE CEUE PROTEIN SEQUENCE. THIS STRUCTURE CONTAINS
REMARK 900 MUTATION H227L AND IS COMPLEXED WITH LIGAND FE(III)-5-LICAM
REMARK 900 RELATED ID: 5A1J RELATED DB: PDB
REMARK 900 5A1J IS THE NATIVE CEUE PROTEIN SEQUENCE WITH LIGAND FE(III)-5-
REMARK 900 LICAM. THIS STRUCTURE CONTAINS MUTATION H227L AND IS ALSO COMPLEXED
REMARK 900 WITH LIGAND FE(III)-5-LICAM.
REMARK 900 RELATED ID: 5A5V RELATED DB: PDB
REMARK 900 5A5V IS THE NATIVE CEUE PROTEIN SEQUENCE WITH LIGAND FE(III)-6-
REMARK 900 LICAM. THIS STRUCTURE CONTAINS MUTATION H227L AND IS INSTEAD
REMARK 900 COMPLEXED WITH LIGAND FE(III)-5-LICAM.
REMARK 900 RELATED ID: 5AD1 RELATED DB: PDB
REMARK 900 5AD1 IS THE NATIVE CEUE PROTEIN SEQUENCE WITH LIGAND FE(III)-8-
REMARK 900 LICAM. THIS STRUCTURE CONTAINS MUTATION H227L AND IS INSTEAD
REMARK 900 COMPLEXED WITH LIGAND FE(III)-5-LICAM.
DBREF1 5TCY A 24 310 UNP A0A0W8LI20_CAMJU
DBREF2 5TCY A A0A0W8LI20 44 330
DBREF1 5TCY B 24 310 UNP A0A0W8LI20_CAMJU
DBREF2 5TCY B A0A0W8LI20 44 330
DBREF1 5TCY C 24 310 UNP A0A0W8LI20_CAMJU
DBREF2 5TCY C A0A0W8LI20 44 330
SEQADV 5TCY GLY A 20 UNP A0A0W8LI2 EXPRESSION TAG
SEQADV 5TCY PRO A 21 UNP A0A0W8LI2 EXPRESSION TAG
SEQADV 5TCY ALA A 22 UNP A0A0W8LI2 EXPRESSION TAG
SEQADV 5TCY MET A 23 UNP A0A0W8LI2 EXPRESSION TAG
SEQADV 5TCY LEU A 227 UNP A0A0W8LI2 HIS 247 ENGINEERED MUTATION
SEQADV 5TCY GLY B 20 UNP A0A0W8LI2 EXPRESSION TAG
SEQADV 5TCY PRO B 21 UNP A0A0W8LI2 EXPRESSION TAG
SEQADV 5TCY ALA B 22 UNP A0A0W8LI2 EXPRESSION TAG
SEQADV 5TCY MET B 23 UNP A0A0W8LI2 EXPRESSION TAG
SEQADV 5TCY LEU B 227 UNP A0A0W8LI2 HIS 247 ENGINEERED MUTATION
SEQADV 5TCY GLY C 20 UNP A0A0W8LI2 EXPRESSION TAG
SEQADV 5TCY PRO C 21 UNP A0A0W8LI2 EXPRESSION TAG
SEQADV 5TCY ALA C 22 UNP A0A0W8LI2 EXPRESSION TAG
SEQADV 5TCY MET C 23 UNP A0A0W8LI2 EXPRESSION TAG
SEQADV 5TCY LEU C 227 UNP A0A0W8LI2 HIS 247 ENGINEERED MUTATION
SEQRES 1 A 291 GLY PRO ALA MET LEU PRO ILE SER MET SER ASP GLU GLY
SEQRES 2 A 291 ASP SER PHE LEU VAL LYS ASP SER LEU GLY GLU ASN LYS
SEQRES 3 A 291 ILE PRO LYS ASN PRO SER LYS VAL VAL ILE LEU ASP LEU
SEQRES 4 A 291 GLY ILE LEU ASP THR PHE ASP ALA LEU LYS LEU ASN ASP
SEQRES 5 A 291 LYS VAL VAL GLY VAL PRO ALA LYS ASN LEU PRO LYS TYR
SEQRES 6 A 291 LEU GLN GLN PHE LYS ASN LYS PRO SER VAL GLY GLY VAL
SEQRES 7 A 291 GLN GLN VAL ASP PHE GLU ALA ILE ASN ALA LEU LYS PRO
SEQRES 8 A 291 ASP LEU ILE ILE ILE SER GLY ARG GLN SER LYS PHE TYR
SEQRES 9 A 291 ASP LYS LEU LYS GLU ILE ALA PRO THR LEU PHE VAL GLY
SEQRES 10 A 291 LEU ASP ASN ALA ASN PHE LEU SER SER PHE GLU ASN ASN
SEQRES 11 A 291 VAL LEU SER VAL ALA LYS LEU TYR GLY LEU GLU LYS GLU
SEQRES 12 A 291 ALA LEU GLU LYS ILE SER ASP ILE LYS ASN GLU ILE GLU
SEQRES 13 A 291 LYS ALA LYS SER ILE VAL ASP GLU ASP LYS LYS ALA LEU
SEQRES 14 A 291 ILE ILE LEU THR ASN SER ASN LYS ILE SER ALA PHE GLY
SEQRES 15 A 291 PRO GLN SER ARG PHE GLY ILE ILE HIS ASP VAL LEU GLY
SEQRES 16 A 291 ILE ASN ALA VAL ASP GLU ASN ILE LYS VAL GLY THR LEU
SEQRES 17 A 291 GLY LYS SER ILE ASN SER GLU PHE ILE LEU GLU LYS ASN
SEQRES 18 A 291 PRO ASP TYR ILE PHE VAL VAL ASP ARG ASN VAL ILE LEU
SEQRES 19 A 291 GLY ASN LYS GLU ARG ALA GLN GLY ILE LEU ASP ASN ALA
SEQRES 20 A 291 LEU VAL ALA LYS THR LYS ALA ALA GLN ASN LYS LYS ILE
SEQRES 21 A 291 ILE TYR LEU ASP PRO GLU TYR TRP TYR LEU ALA SER GLY
SEQRES 22 A 291 ASN GLY LEU GLU SER LEU LYS THR MET ILE LEU GLU ILE
SEQRES 23 A 291 LYS ASN ALA VAL LYS
SEQRES 1 B 291 GLY PRO ALA MET LEU PRO ILE SER MET SER ASP GLU GLY
SEQRES 2 B 291 ASP SER PHE LEU VAL LYS ASP SER LEU GLY GLU ASN LYS
SEQRES 3 B 291 ILE PRO LYS ASN PRO SER LYS VAL VAL ILE LEU ASP LEU
SEQRES 4 B 291 GLY ILE LEU ASP THR PHE ASP ALA LEU LYS LEU ASN ASP
SEQRES 5 B 291 LYS VAL VAL GLY VAL PRO ALA LYS ASN LEU PRO LYS TYR
SEQRES 6 B 291 LEU GLN GLN PHE LYS ASN LYS PRO SER VAL GLY GLY VAL
SEQRES 7 B 291 GLN GLN VAL ASP PHE GLU ALA ILE ASN ALA LEU LYS PRO
SEQRES 8 B 291 ASP LEU ILE ILE ILE SER GLY ARG GLN SER LYS PHE TYR
SEQRES 9 B 291 ASP LYS LEU LYS GLU ILE ALA PRO THR LEU PHE VAL GLY
SEQRES 10 B 291 LEU ASP ASN ALA ASN PHE LEU SER SER PHE GLU ASN ASN
SEQRES 11 B 291 VAL LEU SER VAL ALA LYS LEU TYR GLY LEU GLU LYS GLU
SEQRES 12 B 291 ALA LEU GLU LYS ILE SER ASP ILE LYS ASN GLU ILE GLU
SEQRES 13 B 291 LYS ALA LYS SER ILE VAL ASP GLU ASP LYS LYS ALA LEU
SEQRES 14 B 291 ILE ILE LEU THR ASN SER ASN LYS ILE SER ALA PHE GLY
SEQRES 15 B 291 PRO GLN SER ARG PHE GLY ILE ILE HIS ASP VAL LEU GLY
SEQRES 16 B 291 ILE ASN ALA VAL ASP GLU ASN ILE LYS VAL GLY THR LEU
SEQRES 17 B 291 GLY LYS SER ILE ASN SER GLU PHE ILE LEU GLU LYS ASN
SEQRES 18 B 291 PRO ASP TYR ILE PHE VAL VAL ASP ARG ASN VAL ILE LEU
SEQRES 19 B 291 GLY ASN LYS GLU ARG ALA GLN GLY ILE LEU ASP ASN ALA
SEQRES 20 B 291 LEU VAL ALA LYS THR LYS ALA ALA GLN ASN LYS LYS ILE
SEQRES 21 B 291 ILE TYR LEU ASP PRO GLU TYR TRP TYR LEU ALA SER GLY
SEQRES 22 B 291 ASN GLY LEU GLU SER LEU LYS THR MET ILE LEU GLU ILE
SEQRES 23 B 291 LYS ASN ALA VAL LYS
SEQRES 1 C 291 GLY PRO ALA MET LEU PRO ILE SER MET SER ASP GLU GLY
SEQRES 2 C 291 ASP SER PHE LEU VAL LYS ASP SER LEU GLY GLU ASN LYS
SEQRES 3 C 291 ILE PRO LYS ASN PRO SER LYS VAL VAL ILE LEU ASP LEU
SEQRES 4 C 291 GLY ILE LEU ASP THR PHE ASP ALA LEU LYS LEU ASN ASP
SEQRES 5 C 291 LYS VAL VAL GLY VAL PRO ALA LYS ASN LEU PRO LYS TYR
SEQRES 6 C 291 LEU GLN GLN PHE LYS ASN LYS PRO SER VAL GLY GLY VAL
SEQRES 7 C 291 GLN GLN VAL ASP PHE GLU ALA ILE ASN ALA LEU LYS PRO
SEQRES 8 C 291 ASP LEU ILE ILE ILE SER GLY ARG GLN SER LYS PHE TYR
SEQRES 9 C 291 ASP LYS LEU LYS GLU ILE ALA PRO THR LEU PHE VAL GLY
SEQRES 10 C 291 LEU ASP ASN ALA ASN PHE LEU SER SER PHE GLU ASN ASN
SEQRES 11 C 291 VAL LEU SER VAL ALA LYS LEU TYR GLY LEU GLU LYS GLU
SEQRES 12 C 291 ALA LEU GLU LYS ILE SER ASP ILE LYS ASN GLU ILE GLU
SEQRES 13 C 291 LYS ALA LYS SER ILE VAL ASP GLU ASP LYS LYS ALA LEU
SEQRES 14 C 291 ILE ILE LEU THR ASN SER ASN LYS ILE SER ALA PHE GLY
SEQRES 15 C 291 PRO GLN SER ARG PHE GLY ILE ILE HIS ASP VAL LEU GLY
SEQRES 16 C 291 ILE ASN ALA VAL ASP GLU ASN ILE LYS VAL GLY THR LEU
SEQRES 17 C 291 GLY LYS SER ILE ASN SER GLU PHE ILE LEU GLU LYS ASN
SEQRES 18 C 291 PRO ASP TYR ILE PHE VAL VAL ASP ARG ASN VAL ILE LEU
SEQRES 19 C 291 GLY ASN LYS GLU ARG ALA GLN GLY ILE LEU ASP ASN ALA
SEQRES 20 C 291 LEU VAL ALA LYS THR LYS ALA ALA GLN ASN LYS LYS ILE
SEQRES 21 C 291 ILE TYR LEU ASP PRO GLU TYR TRP TYR LEU ALA SER GLY
SEQRES 22 C 291 ASN GLY LEU GLU SER LEU LYS THR MET ILE LEU GLU ILE
SEQRES 23 C 291 LYS ASN ALA VAL LYS
HET FE A 401 1
HET 5LC A 402 27
HET FE B 401 1
HET 5LC B 402 27
HET FE C 401 1
HET 5LC C 402 27
HETNAM FE FE (III) ION
HETNAM 5LC N,N'-PENTANE-1,5-DIYLBIS(2,3-DIHYDROXYBENZAMIDE)
FORMUL 4 FE 3(FE 3+)
FORMUL 5 5LC 3(C19 H22 N2 O6)
FORMUL 10 HOH *167(H2 O)
HELIX 1 AA1 ASP A 57 LEU A 67 1 11
HELIX 2 AA2 LEU A 69 ASP A 71 5 3
HELIX 3 AA3 PRO A 77 LEU A 81 5 5
HELIX 4 AA4 PRO A 82 LYS A 89 5 8
HELIX 5 AA5 ASP A 101 LYS A 109 1 9
HELIX 6 AA6 SER A 116 LYS A 121 5 6
HELIX 7 AA7 PHE A 122 ALA A 130 1 9
HELIX 8 AA8 ASN A 141 TYR A 157 1 17
HELIX 9 AA9 LEU A 159 SER A 179 1 21
HELIX 10 AB1 GLY A 207 VAL A 212 1 6
HELIX 11 AB2 ASN A 232 ASN A 240 1 9
HELIX 12 AB3 ARG A 249 GLY A 254 1 6
HELIX 13 AB4 ARG A 258 LEU A 263 1 6
HELIX 14 AB5 ASN A 265 LYS A 270 1 6
HELIX 15 AB6 THR A 271 ASN A 276 1 6
HELIX 16 AB7 ASP A 283 TYR A 288 1 6
HELIX 17 AB8 GLU A 296 VAL A 309 1 14
HELIX 18 AB9 ASP B 57 LEU B 67 1 11
HELIX 19 AC1 LEU B 69 ASP B 71 5 3
HELIX 20 AC2 PRO B 77 LEU B 81 5 5
HELIX 21 AC3 PRO B 82 LYS B 89 5 8
HELIX 22 AC4 ASP B 101 LEU B 108 1 8
HELIX 23 AC5 SER B 116 LYS B 121 5 6
HELIX 24 AC6 PHE B 122 ALA B 130 1 9
HELIX 25 AC7 ASN B 141 LEU B 156 1 16
HELIX 26 AC8 LEU B 159 SER B 179 1 21
HELIX 27 AC9 GLY B 207 VAL B 212 1 6
HELIX 28 AD1 ASN B 232 ASN B 240 1 9
HELIX 29 AD2 ARG B 249 GLY B 254 1 6
HELIX 30 AD3 ARG B 258 LEU B 263 1 6
HELIX 31 AD4 ASN B 265 LYS B 270 1 6
HELIX 32 AD5 THR B 271 ASN B 276 1 6
HELIX 33 AD6 ASP B 283 TYR B 288 1 6
HELIX 34 AD7 GLU B 296 VAL B 309 1 14
HELIX 35 AD8 ASP C 57 LEU C 67 1 11
HELIX 36 AD9 LEU C 69 ASP C 71 5 3
HELIX 37 AE1 PRO C 77 LEU C 81 5 5
HELIX 38 AE2 PRO C 82 LYS C 89 5 8
HELIX 39 AE3 ASP C 101 LYS C 109 1 9
HELIX 40 AE4 SER C 116 LYS C 121 5 6
HELIX 41 AE5 PHE C 122 ALA C 130 1 9
HELIX 42 AE6 ASN C 141 TYR C 157 1 17
HELIX 43 AE7 LEU C 159 ILE C 180 1 22
HELIX 44 AE8 GLY C 207 VAL C 212 1 6
HELIX 45 AE9 ASN C 232 ASN C 240 1 9
HELIX 46 AF1 ARG C 249 GLY C 254 1 6
HELIX 47 AF2 ARG C 258 LEU C 263 1 6
HELIX 48 AF3 ASN C 265 LYS C 270 1 6
HELIX 49 AF4 THR C 271 ASN C 276 1 6
HELIX 50 AF5 ASP C 283 TYR C 288 1 6
HELIX 51 AF6 GLU C 296 LYS C 310 1 15
SHEET 1 AA1 3 SER A 27 ASP A 30 0
SHEET 2 AA1 3 SER A 34 ASP A 39 -1 O LYS A 38 N SER A 27
SHEET 3 AA1 3 GLY A 42 PRO A 47 -1 O ASN A 44 N VAL A 37
SHEET 1 AA2 4 VAL A 73 GLY A 75 0
SHEET 2 AA2 4 VAL A 53 ILE A 55 1 N VAL A 53 O VAL A 74
SHEET 3 AA2 4 LEU A 112 ILE A 115 1 O ILE A 114 N VAL A 54
SHEET 4 AA2 4 THR A 132 PHE A 134 1 O LEU A 133 N ILE A 115
SHEET 1 AA3 4 ASN A 216 ALA A 217 0
SHEET 2 AA3 4 LYS A 186 ASN A 193 1 N ALA A 187 O ASN A 216
SHEET 3 AA3 4 LYS A 196 PHE A 200 -1 O LYS A 196 N ASN A 193
SHEET 4 AA3 4 LYS A 229 ILE A 231 -1 O LYS A 229 N ALA A 199
SHEET 1 AA4 4 ASN A 216 ALA A 217 0
SHEET 2 AA4 4 LYS A 186 ASN A 193 1 N ALA A 187 O ASN A 216
SHEET 3 AA4 4 TYR A 243 ASP A 248 1 O VAL A 247 N ILE A 190
SHEET 4 AA4 4 ILE A 279 LEU A 282 1 O ILE A 280 N ILE A 244
SHEET 1 AA5 3 SER B 27 ASP B 30 0
SHEET 2 AA5 3 SER B 34 ASP B 39 -1 O LYS B 38 N SER B 27
SHEET 3 AA5 3 GLY B 42 PRO B 47 -1 O ILE B 46 N PHE B 35
SHEET 1 AA6 4 VAL B 73 GLY B 75 0
SHEET 2 AA6 4 VAL B 53 ILE B 55 1 N VAL B 53 O VAL B 74
SHEET 3 AA6 4 LEU B 112 ILE B 115 1 O ILE B 114 N VAL B 54
SHEET 4 AA6 4 THR B 132 PHE B 134 1 O LEU B 133 N ILE B 115
SHEET 1 AA7 4 ASN B 216 ALA B 217 0
SHEET 2 AA7 4 LYS B 186 ASN B 193 1 N ALA B 187 O ASN B 216
SHEET 3 AA7 4 LYS B 196 PHE B 200 -1 O PHE B 200 N ILE B 189
SHEET 4 AA7 4 LYS B 229 ILE B 231 -1 O LYS B 229 N ALA B 199
SHEET 1 AA8 4 ASN B 216 ALA B 217 0
SHEET 2 AA8 4 LYS B 186 ASN B 193 1 N ALA B 187 O ASN B 216
SHEET 3 AA8 4 TYR B 243 ASP B 248 1 O PHE B 245 N ILE B 190
SHEET 4 AA8 4 ILE B 279 LEU B 282 1 O ILE B 280 N ILE B 244
SHEET 1 AA9 3 SER C 27 ASP C 30 0
SHEET 2 AA9 3 SER C 34 LYS C 38 -1 O LYS C 38 N SER C 27
SHEET 3 AA9 3 GLU C 43 PRO C 47 -1 O ASN C 44 N VAL C 37
SHEET 1 AB1 4 VAL C 73 GLY C 75 0
SHEET 2 AB1 4 VAL C 53 ILE C 55 1 N ILE C 55 O GLY C 75
SHEET 3 AB1 4 LEU C 112 ILE C 115 1 O LEU C 112 N VAL C 54
SHEET 4 AB1 4 THR C 132 PHE C 134 1 O LEU C 133 N ILE C 113
SHEET 1 AB2 4 ASN C 216 ALA C 217 0
SHEET 2 AB2 4 LYS C 186 ASN C 193 1 N ALA C 187 O ASN C 216
SHEET 3 AB2 4 LYS C 196 PHE C 200 -1 O LYS C 196 N ASN C 193
SHEET 4 AB2 4 LYS C 229 ILE C 231 -1 O LYS C 229 N ALA C 199
SHEET 1 AB3 4 ASN C 216 ALA C 217 0
SHEET 2 AB3 4 LYS C 186 ASN C 193 1 N ALA C 187 O ASN C 216
SHEET 3 AB3 4 TYR C 243 ASP C 248 1 O VAL C 247 N ILE C 190
SHEET 4 AB3 4 ILE C 279 LEU C 282 1 O ILE C 280 N VAL C 246
LINK OH TYR A 288 FE FE A 401 1555 1555 1.88
LINK FE FE A 401 O23 5LC A 402 1555 1555 2.13
LINK FE FE A 401 O24 5LC A 402 1555 1555 2.13
LINK FE FE A 401 O26 5LC A 402 1555 1555 2.07
LINK FE FE A 401 O25 5LC A 402 1555 1555 2.14
LINK FE FE A 401 O HOH A 511 1555 1555 2.15
LINK OH TYR B 288 FE FE B 401 1555 1555 2.04
LINK FE FE B 401 O23 5LC B 402 1555 1555 2.18
LINK FE FE B 401 O24 5LC B 402 1555 1555 1.95
LINK FE FE B 401 O25 5LC B 402 1555 1555 2.09
LINK FE FE B 401 O26 5LC B 402 1555 1555 1.91
LINK FE FE B 401 O HOH B 503 1555 1555 2.02
LINK OH TYR C 288 FE FE C 401 1555 1555 1.94
LINK FE FE C 401 O23 5LC C 402 1555 1555 2.06
LINK FE FE C 401 O24 5LC C 402 1555 1555 2.10
LINK FE FE C 401 O25 5LC C 402 1555 1555 2.02
LINK FE FE C 401 O26 5LC C 402 1555 1555 1.93
SITE 1 AC1 3 TYR A 288 5LC A 402 HOH A 511
SITE 1 AC2 10 VAL A 97 GLN A 98 ARG A 118 LYS A 121
SITE 2 AC2 10 ARG A 205 ARG A 249 TYR A 288 FE A 401
SITE 3 AC2 10 HOH A 511 MET C 23
SITE 1 AC3 3 TYR B 288 5LC B 402 HOH B 503
SITE 1 AC4 9 GLN B 98 ARG B 118 LYS B 121 ARG B 205
SITE 2 AC4 9 ARG B 249 TYR B 288 FE B 401 HOH B 501
SITE 3 AC4 9 HOH B 503
SITE 1 AC5 2 TYR C 288 5LC C 402
SITE 1 AC6 10 ASP B 39 SER B 40 GLN C 98 ARG C 118
SITE 2 AC6 10 LYS C 121 ASN C 193 ARG C 205 ARG C 249
SITE 3 AC6 10 TYR C 288 FE C 401
CRYST1 58.696 62.881 69.867 82.09 74.67 77.60 P 1 3
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 0.017037 -0.003747 -0.004366 0.00000
SCALE2 0.000000 0.016283 -0.001402 0.00000
SCALE3 0.000000 0.000000 0.014896 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
