HEADER METAL TRANSPORT 22-MAR-18 6CTC
TITLE CRYSTAL STRUCTURE OF HUMAN TRANSFERRIN BOUND TO TRIFERIC FPC IRON
TITLE 2 PYROPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEROTRANSFERRIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRANSFERRIN,BETA-1 METAL-BINDING GLOBULIN,SIDEROPHILIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TF, PRO1400;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS IRON, PYROPHOSPHATE, TRANSFERRIN, TRIFERIC IRON, FPC, TRANSFUSION,
KEYWDS 2 BLOOD, PLASMA, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR T.E.EDWARDS,R.PRATT
REVDAT 3 04-OCT-23 6CTC 1 JRNL
REVDAT 2 28-NOV-18 6CTC 1 JRNL
REVDAT 1 24-OCT-18 6CTC 0
JRNL AUTH R.PRATT,G.J.HANDELMAN,T.E.EDWARDS,A.GUPTA
JRNL TITL FERRIC PYROPHOSPHATE CITRATE: INTERACTIONS WITH TRANSFERRIN.
JRNL REF BIOMETALS V. 31 1081 2018
JRNL REFN ESSN 1572-8773
JRNL PMID 30311019
JRNL DOI 10.1007/S10534-018-0142-2
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 23438
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.140
REMARK 3 FREE R VALUE TEST SET COUNT : 1204
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 34.3790 - 5.4023 0.99 2595 153 0.1617 0.2107
REMARK 3 2 5.4023 - 4.2906 1.00 2509 129 0.1445 0.1985
REMARK 3 3 4.2906 - 3.7490 1.00 2463 144 0.1602 0.2318
REMARK 3 4 3.7490 - 3.4065 1.00 2484 123 0.1764 0.2705
REMARK 3 5 3.4065 - 3.1625 1.00 2427 145 0.2031 0.3192
REMARK 3 6 3.1625 - 2.9762 1.00 2447 118 0.2351 0.3175
REMARK 3 7 2.9762 - 2.8272 1.00 2431 148 0.2348 0.3264
REMARK 3 8 2.8272 - 2.7042 1.00 2451 111 0.2422 0.3384
REMARK 3 9 2.7042 - 2.6001 1.00 2427 133 0.2677 0.3992
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.570
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 55.43
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 316 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.9767 11.2303 7.6382
REMARK 3 T TENSOR
REMARK 3 T11: 0.4472 T22: 0.4382
REMARK 3 T33: 0.5158 T12: 0.0143
REMARK 3 T13: 0.0584 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 1.5298 L22: 0.7341
REMARK 3 L33: 2.7836 L12: 0.2073
REMARK 3 L13: -1.2012 L23: 0.4172
REMARK 3 S TENSOR
REMARK 3 S11: 0.0475 S12: -0.0554 S13: 0.1300
REMARK 3 S21: -0.1388 S22: 0.1230 S23: -0.2692
REMARK 3 S31: -0.0847 S32: 0.3856 S33: -0.0773
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 317 THROUGH 679 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7953 -8.1786 -1.9652
REMARK 3 T TENSOR
REMARK 3 T11: 0.4250 T22: 0.4502
REMARK 3 T33: 0.3641 T12: -0.0625
REMARK 3 T13: 0.0054 T23: 0.0527
REMARK 3 L TENSOR
REMARK 3 L11: 1.9112 L22: 1.3780
REMARK 3 L33: 2.0055 L12: 0.5771
REMARK 3 L13: 1.3935 L23: 0.9973
REMARK 3 S TENSOR
REMARK 3 S11: 0.2205 S12: -0.3052 S13: -0.1883
REMARK 3 S21: 0.1489 S22: -0.1309 S23: 0.0114
REMARK 3 S31: 0.2258 S32: -0.2555 S33: -0.0642
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6CTC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1000233356.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23450
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 34.376
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.038
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.5500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.25
REMARK 200 R MERGE FOR SHELL (I) : 0.48400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4H0W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: APO HUMAN TRANSFERRIN (PROSPEC PRO-325
REMARK 280 PURIFIED BY Q-SEPHAROSE) AT 56 MG/ML (0.76 MM) AGAINST MORPHEUS
REMARK 280 SCREEN CONDITION D4 12.5% PEG 1000, 12.5% PEG3350, 12.5% MPD,
REMARK 280 0.02 M EACH 1,6-HEXANEDIOL, 1-BUTANOL, RS-1,2-PROPANEDIOL, 2-
REMARK 280 PROPANOL, 1,4-BUTANEDIOL, 1,3-PROPANEDIOL, 0.1 M MES/IMIDAZOLE
REMARK 280 PH 6.5, CRYSTAL TRACKING ID 246352D4, UNIQUE PUCK ID SUV0-5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 37.18500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.21500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.08000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.21500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.18500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.08000
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 4 CG CD CE NZ
REMARK 470 GLU A 13 CG CD OE1 OE2
REMARK 470 LYS A 27 CG CD CE NZ
REMARK 470 LYS A 41 CG CD CE NZ
REMARK 470 GLU A 56 CG CD OE1 OE2
REMARK 470 LYS A 88 CG CD CE NZ
REMARK 470 GLU A 89 CG CD OE1 OE2
REMARK 470 LYS A 102 CG CD CE NZ
REMARK 470 LYS A 144 CG CD CE NZ
REMARK 470 LYS A 148 CG CD CE NZ
REMARK 470 THR A 165 OG1 CG2
REMARK 470 GLN A 169 CG CD OE1 NE2
REMARK 470 LEU A 182 CG CD1 CD2
REMARK 470 LYS A 196 CG CD CE NZ
REMARK 470 MET A 256 CG SD CE
REMARK 470 LEU A 262 CG CD1 CD2
REMARK 470 GLU A 272 CG CD OE1 OE2
REMARK 470 LYS A 276 CG CD CE NZ
REMARK 470 LYS A 280 CG CD CE NZ
REMARK 470 GLU A 281 CG CD OE1 OE2
REMARK 470 LYS A 291 CG CD CE NZ
REMARK 470 PRO A 332 CG CD
REMARK 470 GLU A 333 CG CD OE1 OE2
REMARK 470 GLU A 338 CG CD OE1 OE2
REMARK 470 LYS A 340 CG CD CE NZ
REMARK 470 ASN A 361 CG OD1 ND2
REMARK 470 VAL A 363 CG1 CG2
REMARK 470 LYS A 414 CG CD CE NZ
REMARK 470 ASP A 416 CG OD1 OD2
REMARK 470 ASN A 417 CG OD1 ND2
REMARK 470 LYS A 433 CG CD CE NZ
REMARK 470 LYS A 434 CG CD CE NZ
REMARK 470 ASP A 442 CG OD1 OD2
REMARK 470 LYS A 489 CG CD CE NZ
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 GLN A 536 CG CD OE1 NE2
REMARK 470 LYS A 557 CG CD CE NZ
REMARK 470 THR A 567 OG1 CG2
REMARK 470 LYS A 591 CG CD CE NZ
REMARK 470 GLN A 603 CG CD OE1 NE2
REMARK 470 THR A 613 OG1 CG2
REMARK 470 ASP A 614 CG OD1 OD2
REMARK 470 PHE A 619 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 621 CG CD1 CD2
REMARK 470 ARG A 623 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 625 CG CD OE1 OE2
REMARK 470 LYS A 640 CG CD CE NZ
REMARK 470 ASP A 643 CG OD1 OD2
REMARK 470 ARG A 644 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 657 CG CD CE NZ
REMARK 470 ASN A 661 CG OD1 ND2
REMARK 470 ARG A 663 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 664 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 O ASN A 417 OG1 THR A 421 2.12
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 ASN A 55 19.66 56.44
REMARK 500 ASP A 58 -39.09 -132.14
REMARK 500 ASP A 90 71.20 -163.64
REMARK 500 SER A 125 -78.88 -76.64
REMARK 500 TRP A 128 -69.26 -155.60
REMARK 500 PHE A 167 76.92 -116.48
REMARK 500 CYS A 241 73.83 -156.32
REMARK 500 LYS A 259 35.54 75.96
REMARK 500 LEU A 294 -44.34 72.18
REMARK 500 SER A 348 -168.29 75.69
REMARK 500 LEU A 439 125.51 -38.62
REMARK 500 ASN A 443 73.11 -169.83
REMARK 500 ALA A 453 149.60 -178.68
REMARK 500 TRP A 460 -62.31 -148.63
REMARK 500 LYS A 527 -31.85 -132.86
REMARK 500 ASP A 565 8.10 -66.31
REMARK 500 ASN A 584 156.67 -49.19
REMARK 500 PHE A 608 19.13 -140.29
REMARK 500 ASP A 614 90.20 57.60
REMARK 500 SER A 624 90.53 -64.56
REMARK 500 GLU A 625 -139.95 -99.51
REMARK 500 LEU A 630 -59.37 75.66
REMARK 500 HIS A 642 -128.69 53.69
REMARK 500 SER A 668 109.45 -57.55
REMARK 500 ARG A 678 87.32 -154.96
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 701 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 188 OH
REMARK 620 2 POP A 704 O3 79.6
REMARK 620 3 POP A 704 P2 125.2 75.6
REMARK 620 4 POP A 704 O4 159.1 84.5 36.2
REMARK 620 5 POP A 704 O6 94.9 86.7 36.3 70.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A 702 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 392 OD1
REMARK 620 2 TYR A 426 OH 92.1
REMARK 620 3 TYR A 517 OH 171.0 95.7
REMARK 620 4 HIS A 585 NE2 96.1 90.6 88.3
REMARK 620 5 CO3 A 703 O2 85.5 152.8 85.5 116.6
REMARK 620 6 CO3 A 703 O3 83.7 89.9 91.8 179.4 62.8
REMARK 620 N 1 2 3 4 5
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 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO3 A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue POP A 704
DBREF 6CTC A 1 679 UNP P02787 TRFE_HUMAN 20 698
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 ILE
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 FE A 701 1
HET FE A 702 1
HET CO3 A 703 4
HET POP A 704 9
HETNAM FE FE (III) ION
HETNAM CO3 CARBONATE ION
HETNAM POP PYROPHOSPHATE 2-
FORMUL 2 FE 2(FE 3+)
FORMUL 4 CO3 C O3 2-
FORMUL 5 POP H2 O7 P2 2-
FORMUL 6 HOH *62(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 PHE A 186 ASP A 197 1 12
HELIX 10 AB1 HIS A 207 GLU A 212 1 6
HELIX 11 AB2 ASN A 216 ASP A 221 1 6
HELIX 12 AB3 ASP A 236 CYS A 241 5 6
HELIX 13 AB4 LYS A 259 GLY A 275 1 17
HELIX 14 AB5 ASP A 310 GLY A 316 1 7
HELIX 15 AB6 GLY A 316 GLY A 329 1 14
HELIX 16 AB7 SER A 348 SER A 362 1 15
HELIX 17 AB8 THR A 373 GLY A 384 1 12
HELIX 18 AB9 ASP A 392 CYS A 402 1 11
HELIX 19 AC1 ASN A 417 THR A 421 5 5
HELIX 20 AC2 TRP A 460 ASN A 472 1 13
HELIX 21 AC3 ARG A 475 PHE A 480 1 6
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 THR A 542 1 7
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 LYS A 593 GLY A 609 1 17
HELIX 29 AD2 THR A 646 LEU A 662 1 17
HELIX 30 AD3 ARG A 663 SER A 666 5 4
HELIX 31 AD4 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 VAL A 40 N ALA A 10
SHEET 1 AA2 4 VAL A 60 LEU A 62 0
SHEET 2 AA2 4 THR A 250 ARG A 254 -1 O VAL A 252 N VAL A 60
SHEET 3 AA2 4 LEU A 77 PHE A 84 -1 N VAL A 81 O VAL A 251
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 98 O VAL A 205
SHEET 5 AA3 6 TYR A 223 LEU A 226 -1 O LEU A 226 N ALA A 99
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 98 O VAL A 205
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 LEU A 347 0
SHEET 2 AA5 2 ILE A 366 ALA A 371 1 O GLU A 367 N TRP A 344
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 TYR A 426 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 TYR A 426 LYS A 433 -1 N VAL A 431 O ALA A 531
SHEET 5 AA8 5 ALA A 580 ALA A 582 -1 O ALA A 580 N ALA A 428
SSBOND 1 CYS A 9 CYS A 48 1555 1555 2.06
SSBOND 2 CYS A 19 CYS A 39 1555 1555 2.06
SSBOND 3 CYS A 118 CYS A 194 1555 1555 2.04
SSBOND 4 CYS A 137 CYS A 331 1555 1555 2.05
SSBOND 5 CYS A 158 CYS A 174 1555 1555 2.03
SSBOND 6 CYS A 161 CYS A 179 1555 1555 2.04
SSBOND 7 CYS A 171 CYS A 177 1555 1555 2.02
SSBOND 8 CYS A 227 CYS A 241 1555 1555 2.02
SSBOND 9 CYS A 339 CYS A 596 1555 1555 2.02
SSBOND 10 CYS A 345 CYS A 377 1555 1555 2.12
SSBOND 11 CYS A 355 CYS A 368 1555 1555 2.05
SSBOND 12 CYS A 402 CYS A 674 1555 1555 2.03
SSBOND 13 CYS A 418 CYS A 637 1555 1555 2.05
SSBOND 14 CYS A 450 CYS A 523 1555 1555 2.01
SSBOND 15 CYS A 474 CYS A 665 1555 1555 2.03
SSBOND 16 CYS A 484 CYS A 498 1555 1555 2.04
SSBOND 17 CYS A 495 CYS A 506 1555 1555 2.02
SSBOND 18 CYS A 563 CYS A 577 1555 1555 2.03
SSBOND 19 CYS A 615 CYS A 620 1555 1555 2.02
LINK OH TYR A 188 FE FE A 701 1555 1555 2.54
LINK OD1 ASP A 392 FE FE A 702 1555 1555 2.06
LINK OH TYR A 426 FE FE A 702 1555 1555 2.13
LINK OH TYR A 517 FE FE A 702 1555 1555 1.95
LINK NE2 HIS A 585 FE FE A 702 1555 1555 2.19
LINK FE FE A 701 O3 POP A 704 1555 1555 2.56
LINK FE FE A 701 P2 POP A 704 1555 1555 2.55
LINK FE FE A 701 O4 POP A 704 1555 1555 2.14
LINK FE FE A 701 O6 POP A 704 1555 1555 2.14
LINK FE FE A 702 O2 CO3 A 703 1555 1555 2.47
LINK FE FE A 702 O3 CO3 A 703 1555 1555 1.77
CISPEP 1 ALA A 73 PRO A 74 0 4.66
CISPEP 2 GLU A 141 PRO A 142 0 -2.34
CISPEP 3 LYS A 144 PRO A 145 0 -0.23
SITE 1 AC1 3 ARG A 124 TYR A 188 POP A 704
SITE 1 AC2 5 ASP A 392 TYR A 426 TYR A 517 HIS A 585
SITE 2 AC2 5 CO3 A 703
SITE 1 AC3 9 ASP A 392 TYR A 426 THR A 452 ARG A 456
SITE 2 AC3 9 THR A 457 ALA A 458 GLY A 459 TYR A 517
SITE 3 AC3 9 FE A 702
SITE 1 AC4 10 ASP A 63 TYR A 95 ARG A 124 SER A 125
SITE 2 AC4 10 TYR A 188 LYS A 206 LYS A 296 FE A 701
SITE 3 AC4 10 HOH A 813 HOH A 838
CRYST1 74.370 90.160 110.430 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 0.013446 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011091 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009056 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
