HEADER METAL BINDING PROTEIN 04-NOV-16 5H52
TITLE STRUCTURE OF TITANIUM-BOUND HUMAN SERUM TRANSFERRIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEROTRANSFERRIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRANSFERRIN,BETA-1 METAL-BINDING GLOBULIN,SIDEROPHILIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS TRANSFERRIN TITANIUM CITRATE, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.P.CURTIN,M.WANG,H.SUN
REVDAT 4 08-NOV-23 5H52 1 REMARK
REVDAT 3 23-MAY-18 5H52 1 JRNL
REVDAT 2 25-APR-18 5H52 1 JRNL
REVDAT 1 08-NOV-17 5H52 0
JRNL AUTH J.P.CURTIN,M.WANG,T.CHENG,L.JIN,H.SUN
JRNL TITL THE ROLE OF CITRATE, LACTATE AND TRANSFERRIN IN DETERMINING
JRNL TITL 2 TITANIUM RELEASE FROM SURGICAL DEVICES INTO HUMAN SERUM.
JRNL REF J. BIOL. INORG. CHEM. V. 23 471 2018
JRNL REFN ESSN 1432-1327
JRNL PMID 29623422
JRNL DOI 10.1007/S00775-018-1557-5
REMARK 2
REMARK 2 RESOLUTION. 3.00 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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 103.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 21792
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1161
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1109
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.18
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.3460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5037
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 13
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.96000
REMARK 3 B22 (A**2) : -0.59000
REMARK 3 B33 (A**2) : -0.37000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.334
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.232
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.154
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5184 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7010 ; 1.986 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 646 ; 5.940 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 233 ;33.647 ;24.464
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 876 ;17.622 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;20.675 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 745 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3933 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2596 ; 7.721 ; 5.794
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3238 ;10.644 ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2587 ; 9.924 ; 6.047
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2618 ; 4.551 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2550 ;43.040 ; 5.000
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 92
REMARK 3 RESIDUE RANGE : A 247 A 331
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8846 13.5368 -10.9335
REMARK 3 T TENSOR
REMARK 3 T11: 0.0008 T22: 0.0299
REMARK 3 T33: 0.0333 T12: 0.0009
REMARK 3 T13: -0.0001 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.0104 L22: 0.0338
REMARK 3 L33: 0.0246 L12: 0.0171
REMARK 3 L13: -0.0114 L23: -0.0267
REMARK 3 S TENSOR
REMARK 3 S11: -0.0017 S12: 0.0095 S13: 0.0042
REMARK 3 S21: -0.0047 S22: 0.0062 S23: 0.0034
REMARK 3 S31: 0.0043 S32: 0.0053 S33: -0.0045
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 93 A 246
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0333 18.8154 18.7456
REMARK 3 T TENSOR
REMARK 3 T11: 0.0123 T22: 0.0251
REMARK 3 T33: 0.0478 T12: -0.0046
REMARK 3 T13: -0.0090 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.0187 L22: 0.0377
REMARK 3 L33: 0.0393 L12: -0.0254
REMARK 3 L13: -0.0253 L23: 0.0383
REMARK 3 S TENSOR
REMARK 3 S11: -0.0009 S12: -0.0009 S13: -0.0102
REMARK 3 S21: 0.0073 S22: -0.0013 S23: 0.0056
REMARK 3 S31: 0.0081 S32: -0.0010 S33: 0.0021
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 USED
REMARK 4
REMARK 4 5H52 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1300002042.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26553
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 103.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 13.50
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.8
REMARK 200 DATA REDUNDANCY IN SHELL : 8.80
REMARK 200 R MERGE FOR SHELL (I) : 1.66600
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.6.1, PHASER
REMARK 200 STARTING MODEL: 4X1B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PIPES-NA 0.1M, PEG 3350 17%, DISODIUM
REMARK 280 MALONATE 8MM, GLYCEROL 18%, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.92750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.92750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 69.48850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 78.33350
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 69.48850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 78.33350
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 53.92750
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 69.48850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 78.33350
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 53.92750
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 69.48850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 78.33350
REMARK 290 SMTRY3 8 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 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 465 ALA A 334
REMARK 465 PRO A 335
REMARK 465 THR A 336
REMARK 465 ASP A 337
REMARK 465 GLU A 338
REMARK 465 LYS A 414
REMARK 465 SER A 415
REMARK 465 ASP A 416
REMARK 465 ASN A 417
REMARK 465 CYS A 418
REMARK 465 GLU A 419
REMARK 465 ASP A 420
REMARK 465 THR A 421
REMARK 465 PRO A 422
REMARK 465 GLU A 423
REMARK 465 VAL A 612
REMARK 465 THR A 613
REMARK 465 ASP A 614
REMARK 465 CYS A 615
REMARK 465 SER A 616
REMARK 465 GLY A 617
REMARK 465 ASN A 618
REMARK 465 PHE A 619
REMARK 465 CYS A 620
REMARK 465 LEU A 621
REMARK 465 PHE A 622
REMARK 465 ARG A 623
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 LYS A 340 CG CD CE NZ
REMARK 470 LYS A 365 CG CD CE 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 TI 4TI A 703 O HOH A 805 1.85
REMARK 500 TI 4TI A 703 O HOH A 806 1.96
REMARK 500 O9 MLI A 701 TI 4TI A 702 2.03
REMARK 500 OH TYR A 188 TI 4TI A 703 2.06
REMARK 500 OH TYR A 517 TI 4TI A 702 2.07
REMARK 500 TI 4TI A 703 O6 CIT A 704 2.07
REMARK 500 O7 MLI A 701 TI 4TI A 702 2.08
REMARK 500 NE2 HIS A 585 TI 4TI A 702 2.10
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 318 CG GLU A 318 CD 0.133
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 LYS A 41 CD - CE - NZ ANGL. DEV. = -16.1 DEGREES
REMARK 500 LYS A 88 CD - CE - NZ ANGL. DEV. = 20.5 DEGREES
REMARK 500 CYS A 174 CA - CB - SG ANGL. DEV. = 9.9 DEGREES
REMARK 500 GLU A 318 OE1 - CD - OE2 ANGL. DEV. = -9.3 DEGREES
REMARK 500 ARG A 327 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 PRO A 341 C - N - CD ANGL. DEV. = -43.4 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 56.34 -111.36
REMARK 500 ASN A 55 30.62 70.16
REMARK 500 SER A 87 141.04 -174.28
REMARK 500 SER A 125 -71.37 -61.17
REMARK 500 TRP A 128 -64.80 -144.84
REMARK 500 CYS A 174 81.63 -157.62
REMARK 500 CYS A 241 73.97 -160.16
REMARK 500 LYS A 259 71.80 -108.31
REMARK 500 LEU A 294 -5.35 66.43
REMARK 500 LYS A 340 -135.84 51.94
REMARK 500 ALA A 436 84.96 -67.90
REMARK 500 TRP A 460 -62.76 -141.61
REMARK 500 LYS A 527 -34.42 -139.40
REMARK 500 VAL A 533 -158.10 -138.99
REMARK 500 THR A 626 -95.73 -117.78
REMARK 500 LEU A 630 -56.45 64.19
REMARK 500 ASP A 634 35.53 -94.66
REMARK 500 HIS A 642 -113.40 54.43
REMARK 500 ARG A 644 47.94 -100.04
REMARK 500 ARG A 678 85.12 -151.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4TI A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4TI A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT A 704
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 NATURAL VARIANT AT THIS POSITION
DBREF 5H52 A 1 679 UNP P02787 TRFE_HUMAN 20 698
SEQADV 5H52 VAL A 429 UNP P02787 ILE 448 SEE SEQUENCE DETAILS
SEQRES 1 A 679 VAL PRO ASP LYS THR VAL ARG TRP CYS ALA VAL SER GLU
SEQRES 2 A 679 HIS GLU ALA THR LYS CYS GLN SER PHE ARG ASP HIS MET
SEQRES 3 A 679 LYS SER VAL ILE PRO SER ASP GLY PRO SER VAL ALA CYS
SEQRES 4 A 679 VAL LYS LYS ALA SER TYR LEU ASP CYS ILE ARG ALA ILE
SEQRES 5 A 679 ALA ALA ASN GLU ALA ASP ALA VAL THR LEU ASP ALA GLY
SEQRES 6 A 679 LEU VAL TYR ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS
SEQRES 7 A 679 PRO VAL VAL ALA GLU PHE TYR GLY SER LYS GLU ASP PRO
SEQRES 8 A 679 GLN THR PHE TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP
SEQRES 9 A 679 SER GLY PHE GLN MET ASN GLN LEU ARG GLY LYS LYS SER
SEQRES 10 A 679 CYS HIS THR GLY LEU GLY ARG SER ALA GLY TRP ASN ILE
SEQRES 11 A 679 PRO ILE GLY LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG
SEQRES 12 A 679 LYS PRO LEU GLU LYS ALA VAL ALA ASN PHE PHE SER GLY
SEQRES 13 A 679 SER CYS ALA PRO CYS ALA ASP GLY THR ASP PHE PRO GLN
SEQRES 14 A 679 LEU CYS GLN LEU CYS PRO GLY CYS GLY CYS SER THR LEU
SEQRES 15 A 679 ASN GLN TYR PHE GLY TYR SER GLY ALA PHE LYS CYS LEU
SEQRES 16 A 679 LYS ASP GLY ALA GLY ASP VAL ALA PHE VAL LYS HIS SER
SEQRES 17 A 679 THR ILE PHE GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP
SEQRES 18 A 679 GLN TYR GLU LEU LEU CYS LEU ASP ASN THR ARG LYS PRO
SEQRES 19 A 679 VAL ASP GLU TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO
SEQRES 20 A 679 SER HIS THR VAL VAL ALA ARG SER MET GLY GLY LYS GLU
SEQRES 21 A 679 ASP LEU ILE TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS
SEQRES 22 A 679 PHE GLY LYS ASP LYS SER LYS GLU PHE GLN LEU PHE SER
SEQRES 23 A 679 SER PRO HIS GLY LYS ASP LEU LEU PHE LYS ASP SER ALA
SEQRES 24 A 679 HIS GLY PHE LEU LYS VAL PRO PRO ARG MET ASP ALA LYS
SEQRES 25 A 679 MET TYR LEU GLY TYR GLU TYR VAL THR ALA ILE ARG ASN
SEQRES 26 A 679 LEU ARG GLU GLY THR CYS PRO GLU ALA PRO THR ASP GLU
SEQRES 27 A 679 CYS LYS PRO VAL LYS TRP CYS ALA LEU SER HIS HIS GLU
SEQRES 28 A 679 ARG LEU LYS CYS ASP GLU TRP SER VAL ASN SER VAL GLY
SEQRES 29 A 679 LYS ILE GLU CYS VAL SER ALA GLU THR THR GLU ASP CYS
SEQRES 30 A 679 ILE ALA LYS ILE MET ASN GLY GLU ALA ASP ALA MET SER
SEQRES 31 A 679 LEU ASP GLY GLY PHE VAL TYR ILE ALA GLY LYS CYS GLY
SEQRES 32 A 679 LEU VAL PRO VAL LEU ALA GLU ASN TYR ASN LYS SER ASP
SEQRES 33 A 679 ASN CYS GLU ASP THR PRO GLU ALA GLY TYR PHE ALA VAL
SEQRES 34 A 679 ALA VAL VAL LYS LYS SER ALA SER ASP LEU THR TRP ASP
SEQRES 35 A 679 ASN LEU LYS GLY LYS LYS SER CYS HIS THR ALA VAL GLY
SEQRES 36 A 679 ARG THR ALA GLY TRP ASN ILE PRO MET GLY LEU LEU TYR
SEQRES 37 A 679 ASN LYS ILE ASN HIS CYS ARG PHE ASP GLU PHE PHE SER
SEQRES 38 A 679 GLU GLY CYS ALA PRO GLY SER LYS LYS ASP SER SER LEU
SEQRES 39 A 679 CYS LYS LEU CYS MET GLY SER GLY LEU ASN LEU CYS GLU
SEQRES 40 A 679 PRO ASN ASN LYS GLU GLY TYR TYR GLY TYR THR GLY ALA
SEQRES 41 A 679 PHE ARG CYS LEU VAL GLU LYS GLY ASP VAL ALA PHE VAL
SEQRES 42 A 679 LYS HIS GLN THR VAL PRO GLN ASN THR GLY GLY LYS ASN
SEQRES 43 A 679 PRO ASP PRO TRP ALA LYS ASN LEU ASN GLU LYS ASP TYR
SEQRES 44 A 679 GLU LEU LEU CYS LEU ASP GLY THR ARG LYS PRO VAL GLU
SEQRES 45 A 679 GLU TYR ALA ASN CYS HIS LEU ALA ARG ALA PRO ASN HIS
SEQRES 46 A 679 ALA VAL VAL THR ARG LYS ASP LYS GLU ALA CYS VAL HIS
SEQRES 47 A 679 LYS ILE LEU ARG GLN GLN GLN HIS LEU PHE GLY SER ASN
SEQRES 48 A 679 VAL THR ASP CYS SER GLY ASN PHE CYS LEU PHE ARG SER
SEQRES 49 A 679 GLU THR LYS ASP LEU LEU PHE ARG ASP ASP THR VAL CYS
SEQRES 50 A 679 LEU ALA LYS LEU HIS ASP ARG ASN THR TYR GLU LYS TYR
SEQRES 51 A 679 LEU GLY GLU GLU TYR VAL LYS ALA VAL GLY ASN LEU ARG
SEQRES 52 A 679 LYS CYS SER THR SER SER LEU LEU GLU ALA CYS THR PHE
SEQRES 53 A 679 ARG ARG PRO
HET MLI A 701 7
HET 4TI A 702 1
HET 4TI A 703 1
HET CIT A 704 13
HETNAM MLI MALONATE ION
HETNAM 4TI TITANIUM ION
HETNAM CIT CITRIC ACID
FORMUL 2 MLI C3 H2 O4 2-
FORMUL 3 4TI 2(TI 4+)
FORMUL 5 CIT C6 H8 O7
FORMUL 6 HOH *13(H2 O)
HELIX 1 AA1 SER A 12 ILE A 30 1 19
HELIX 2 AA2 SER A 44 ALA A 54 1 11
HELIX 3 AA3 ASP A 63 LEU A 72 1 10
HELIX 4 AA4 GLN A 108 LEU A 112 5 5
HELIX 5 AA5 TRP A 128 TYR A 136 1 9
HELIX 6 AA6 CYS A 137 LEU A 139 5 3
HELIX 7 AA7 PRO A 145 ASN A 152 1 8
HELIX 8 AA8 PHE A 167 GLN A 172 5 6
HELIX 9 AA9 CYS A 174 GLY A 178 5 5
HELIX 10 AB1 PHE A 186 ASP A 197 1 12
HELIX 11 AB2 SER A 208 LEU A 214 1 7
HELIX 12 AB3 ASN A 216 ASP A 221 1 6
HELIX 13 AB4 ASP A 236 CYS A 241 5 6
HELIX 14 AB5 LYS A 259 GLY A 275 1 17
HELIX 15 AB6 ASP A 310 GLY A 316 1 7
HELIX 16 AB7 GLY A 316 GLY A 329 1 14
HELIX 17 AB8 SER A 348 VAL A 363 1 16
HELIX 18 AB9 THR A 373 ASN A 383 1 11
HELIX 19 AC1 ASP A 392 CYS A 402 1 11
HELIX 20 AC2 TRP A 460 ASN A 472 1 13
HELIX 21 AC3 ARG A 475 PHE A 479 5 5
HELIX 22 AC4 SER A 492 LYS A 496 5 5
HELIX 23 AC5 SER A 501 LEU A 505 5 5
HELIX 24 AC6 TYR A 515 LYS A 527 1 13
HELIX 25 AC7 GLN A 536 ASN A 541 1 6
HELIX 26 AC8 ASN A 555 LYS A 557 5 3
HELIX 27 AC9 GLU A 572 CYS A 577 5 6
HELIX 28 AD1 ARG A 590 ASP A 592 5 3
HELIX 29 AD2 LYS A 593 GLY A 609 1 17
HELIX 30 AD3 THR A 646 GLY A 652 1 7
HELIX 31 AD4 GLY A 652 LYS A 664 1 13
HELIX 32 AD5 SER A 668 ARG A 678 1 11
SHEET 1 AA1 2 THR A 5 ALA A 10 0
SHEET 2 AA1 2 SER A 36 LYS A 41 1 O ALA A 38 N TRP A 8
SHEET 1 AA2 4 VAL A 60 LEU A 62 0
SHEET 2 AA2 4 THR A 250 ARG A 254 -1 O THR A 250 N LEU A 62
SHEET 3 AA2 4 LEU A 77 PHE A 84 -1 N LYS A 78 O ALA A 253
SHEET 4 AA2 4 GLY A 301 LYS A 304 -1 O LEU A 303 N ALA A 82
SHEET 1 AA3 6 GLY A 156 CYS A 158 0
SHEET 2 AA3 6 LYS A 116 HIS A 119 1 N HIS A 119 O CYS A 158
SHEET 3 AA3 6 VAL A 202 LYS A 206 1 O VAL A 202 N CYS A 118
SHEET 4 AA3 6 PHE A 94 LYS A 102 -1 N VAL A 100 O ALA A 203
SHEET 5 AA3 6 TYR A 223 LEU A 226 -1 O GLU A 224 N VAL A 101
SHEET 6 AA3 6 ARG A 232 PRO A 234 -1 O LYS A 233 N LEU A 225
SHEET 1 AA4 5 GLY A 156 CYS A 158 0
SHEET 2 AA4 5 LYS A 116 HIS A 119 1 N HIS A 119 O CYS A 158
SHEET 3 AA4 5 VAL A 202 LYS A 206 1 O VAL A 202 N CYS A 118
SHEET 4 AA4 5 PHE A 94 LYS A 102 -1 N VAL A 100 O ALA A 203
SHEET 5 AA4 5 ALA A 244 PRO A 247 -1 O VAL A 246 N TYR A 95
SHEET 1 AA5 2 VAL A 342 ALA A 346 0
SHEET 2 AA5 2 ILE A 366 SER A 370 1 O VAL A 369 N ALA A 346
SHEET 1 AA6 4 MET A 389 LEU A 391 0
SHEET 2 AA6 4 ALA A 586 THR A 589 -1 O VAL A 588 N MET A 389
SHEET 3 AA6 4 VAL A 405 ASN A 411 -1 N LEU A 408 O VAL A 587
SHEET 4 AA6 4 CYS A 637 LYS A 640 -1 O ALA A 639 N ALA A 409
SHEET 1 AA7 6 GLU A 482 CYS A 484 0
SHEET 2 AA7 6 LYS A 448 HIS A 451 1 N HIS A 451 O CYS A 484
SHEET 3 AA7 6 VAL A 530 LYS A 534 1 O PHE A 532 N CYS A 450
SHEET 4 AA7 6 PHE A 427 LYS A 433 -1 N VAL A 431 O ALA A 531
SHEET 5 AA7 6 TYR A 559 LEU A 562 -1 O GLU A 560 N VAL A 432
SHEET 6 AA7 6 ARG A 568 PRO A 570 -1 O LYS A 569 N LEU A 561
SHEET 1 AA8 5 GLU A 482 CYS A 484 0
SHEET 2 AA8 5 LYS A 448 HIS A 451 1 N HIS A 451 O CYS A 484
SHEET 3 AA8 5 VAL A 530 LYS A 534 1 O PHE A 532 N CYS A 450
SHEET 4 AA8 5 PHE A 427 LYS A 433 -1 N VAL A 431 O ALA A 531
SHEET 5 AA8 5 ALA A 580 ARG A 581 -1 O ALA A 580 N ALA A 428
SSBOND 1 CYS A 9 CYS A 48 1555 1555 2.14
SSBOND 2 CYS A 19 CYS A 39 1555 1555 2.16
SSBOND 3 CYS A 118 CYS A 194 1555 1555 2.10
SSBOND 4 CYS A 137 CYS A 331 1555 1555 2.10
SSBOND 5 CYS A 158 CYS A 174 1555 1555 1.98
SSBOND 6 CYS A 161 CYS A 179 1555 1555 2.02
SSBOND 7 CYS A 171 CYS A 177 1555 1555 2.03
SSBOND 8 CYS A 227 CYS A 241 1555 1555 2.01
SSBOND 9 CYS A 339 CYS A 596 1555 1555 2.05
SSBOND 10 CYS A 345 CYS A 377 1555 1555 2.04
SSBOND 11 CYS A 355 CYS A 368 1555 1555 2.06
SSBOND 12 CYS A 402 CYS A 674 1555 1555 2.01
SSBOND 13 CYS A 450 CYS A 523 1555 1555 2.09
SSBOND 14 CYS A 474 CYS A 665 1555 1555 2.08
SSBOND 15 CYS A 484 CYS A 498 1555 1555 2.06
SSBOND 16 CYS A 495 CYS A 506 1555 1555 2.06
SSBOND 17 CYS A 563 CYS A 577 1555 1555 2.03
CISPEP 1 ALA A 73 PRO A 74 0 8.56
CISPEP 2 GLU A 141 PRO A 142 0 2.89
CISPEP 3 LYS A 144 PRO A 145 0 -0.94
CISPEP 4 GLY A 258 LYS A 259 0 7.48
SITE 1 AC1 10 ASP A 392 TYR A 426 THR A 452 ARG A 456
SITE 2 AC1 10 THR A 457 ALA A 458 GLY A 459 TYR A 517
SITE 3 AC1 10 HIS A 585 4TI A 702
SITE 1 AC2 5 ASP A 392 TYR A 426 TYR A 517 HIS A 585
SITE 2 AC2 5 MLI A 701
SITE 1 AC3 4 TYR A 188 CIT A 704 HOH A 805 HOH A 806
SITE 1 AC4 6 TYR A 95 SER A 125 ALA A 126 TYR A 188
SITE 2 AC4 6 4TI A 703 HOH A 806
CRYST1 138.977 156.667 107.855 90.00 90.00 90.00 C 2 2 21 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 0.007195 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006383 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009272 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
