HEADER IMMUNE SYSTEM 30-AUG-00 1FP5
TITLE CRYSTAL STRUCTURE ANALYSIS OF THE HUMAN IGE-FC CEPSILON3-
TITLE 2 CEPSILON4 FRAGMENT.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IGE HEAVY CHAIN EPSILON-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CEPSILON3-CEPSILON4;
COMPND 5 SYNONYM: IGE-FC;
COMPND 6 ENGINEERED: 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: TRICHOPLUSIA NI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PACGP67A
KEYWDS ANTIBODY, FC, IMMUNOGLOBIN FOLD, "CLOSED" IGE-FC, IMMUNE
KEYWDS 2 SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR B.A.WURZBURG,S.C.GARMAN,T.S.JARDETZKY
REVDAT 3 24-FEB-09 1FP5 1 VERSN
REVDAT 2 30-JAN-02 1FP5 1 AUTHOR JRNL
REVDAT 1 27-SEP-00 1FP5 0
JRNL AUTH B.A.WURZBURG,S.C.GARMAN,T.S.JARDETZKY
JRNL TITL STRUCTURE OF THE HUMAN IGE-FC C EPSILON 3-C
JRNL TITL 2 EPSILON 4 REVEALS CONFORMATIONAL FLEXIBILITY IN
JRNL TITL 3 THE ANTIBODY EFFECTOR DOMAINS.
JRNL REF IMMUNITY V. 13 375 2000
JRNL REFN ISSN 1074-7613
JRNL PMID 11021535
JRNL DOI 10.1016/S1074-7613(00)00037-6
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
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) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 12322
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1269
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1618
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 145
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.73500
REMARK 3 B22 (A**2) : 2.73500
REMARK 3 B33 (A**2) : -5.47000
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.77
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.21
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.95
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) : NULL ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; 3.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 3.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DENSITY FOR THE CEPSILON4 AB LOOP
REMARK 3 WAS PARTICULARLY POOR, ESPECIALLY FROM RESIDUES 453-457, AND
REMARK 3 THIS REGION OF THE LOOP WAS BUILT STERICALLY. THE B-FACTORS
REMARK 3 WERE GENERALLY HIGHER AND THE ELECTRON DENSITY GENERALLY
REMARK 3 POORER FOR THE BC- DE- AND FG-LOOPS OF THE CEPSILON3 DOMAIN
REMARK 3 THAT BIND TO THE HIGH AFFINITY RECEPTOR. THE RESIDUE K435 SITS
REMARK 3 AT THE INTERDOMAIN INTERFACE AND THE SIDE CHAIN MAY PARTIALLY
REMARK 3 FILL A GAP IN THE SPACE BETWEEN THE DOMAINS. THIS IS NOT
REMARK 3 OBVIOUS FROM THE STRUCTURE, HOWEVER, AS ALL OF THE ATOMS COULD
REMARK 3 NOT BE MODELED FOR THIS RESIDUE. THE STRUCTURE CONTAINS TWO
REMARK 3 CIS-PROLINES : P471 AND P533 THERE ARE N-LINKED CARBOHYDRATES
REMARK 3 ATTACHED TO THE PROTEIN AT RESIDUES N371 AND N394. SOME
REMARK 3 ELECTRON DENSITY IS OBSERVED FOR THE CARBOHYDRATE ATTACHED TO
REMARK 3 N394, BUT NO ELECTRON DENSITY IS OBSERVED FOR THE CARBOHYDRATE
REMARK 3 ATTACHED TO N371. CARBOHYDRATES WERE NOT MODELED IN THE
REMARK 3 STRUCTURE AND SO THEY ARE NOT PRESENT IN THE PDB FILE.
REMARK 4
REMARK 4 1FP5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-00.
REMARK 100 THE RCSB ID CODE IS RCSB011788.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-AUG-99
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 5ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.906
REMARK 200 MONOCHROMATOR : SI (111), CRYOGENICALLY-COOLED
REMARK 200 OPTICS : 1MM X 1MM SLITS, 25 M FROM
REMARK 200 CRYSTAL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12322
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.25700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM ACETATE PH 4.6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 52.80000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 52.80000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 52.80000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 52.80000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 52.80000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.80000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 52.80000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.80000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
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 300 REMARK: THE ASYMMETRIC UNIT CONTAINS ONE CHAIN OF THE FC
REMARK 300 HOMODIMER. THE BIOLOGICAL DIMER CAN BE GENERATED FROM CHAIN A.
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: DIMERIC
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 BIOMT1 2 0.000000 -1.000000 0.000000 105.60000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 105.60000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 47.10000
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 ALA A 326
REMARK 465 ASP A 327
REMARK 465 PRO A 328
REMARK 465 CYS A 329
REMARK 465 ASP A 330
REMARK 465 SER A 331
REMARK 465 ASN A 332
REMARK 465 PRO A 333
REMARK 465 ARG A 334
REMARK 465 GLY A 335
REMARK 465 ASN A 544
REMARK 465 PRO A 545
REMARK 465 GLY A 546
REMARK 465 LYS A 547
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 391 CG CD CE NZ
REMARK 470 ARG A 408 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 435 CG CD CE NZ
REMARK 470 GLU A 444 CG CD OE1 OE2
REMARK 470 ARG A 457 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 518 CG CD OE1 NE2
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 GLY A 368 N - CA - C ANGL. DEV. = -15.3 DEGREES
REMARK 500 GLY A 455 N - CA - C ANGL. DEV. = -17.8 DEGREES
REMARK 500 SER A 456 N - CA - C ANGL. DEV. = 19.2 DEGREES
REMARK 500 ARG A 457 N - CA - C ANGL. DEV. = -24.1 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 ILE A 350 -64.50 -90.89
REMARK 500 ARG A 393 4.09 -53.65
REMARK 500 PRO A 426 -71.20 -59.66
REMARK 500 PRO A 454 176.94 -35.80
REMARK 500 ARG A 457 120.45 -171.25
REMARK 500 LYS A 459 106.42 172.09
REMARK 500 PRO A 471 -177.94 -62.01
REMARK 500 ASN A 481 -113.76 80.39
REMARK 500 ALA A 488 -13.07 -47.31
REMARK 500 THR A 498 -158.10 -145.80
REMARK 500 GLN A 535 41.63 35.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F6A RELATED DB: PDB
REMARK 900 1F6A CONTAINS THE SAME FC PROTEIN IN COMPLEX WITH ITS HIGH
REMARK 900 AFFINITY RECEPTOR, THE FC EPSILON RI ALPHA (SOLUBLE
REMARK 900 ECTODOMAIN).
DBREF 1FP5 A 330 547 UNP P01854 IGHE_HUMAN 357 574
SEQADV 1FP5 ALA A 326 UNP P01854 CLONING ARTIFACT
SEQADV 1FP5 ASP A 327 UNP P01854 CLONING ARTIFACT
SEQADV 1FP5 PRO A 328 UNP P01854 CLONING ARTIFACT
SEQADV 1FP5 CYS A 329 UNP P01854 CLONING ARTIFACT
SEQRES 1 A 222 ALA ASP PRO CYS ASP SER ASN PRO ARG GLY VAL SER ALA
SEQRES 2 A 222 TYR LEU SER ARG PRO SER PRO PHE ASP LEU PHE ILE ARG
SEQRES 3 A 222 LYS SER PRO THR ILE THR CYS LEU VAL VAL ASP LEU ALA
SEQRES 4 A 222 PRO SER LYS GLY THR VAL ASN LEU THR TRP SER ARG ALA
SEQRES 5 A 222 SER GLY LYS PRO VAL ASN HIS SER THR ARG LYS GLU GLU
SEQRES 6 A 222 LYS GLN ARG ASN GLY THR LEU THR VAL THR SER THR LEU
SEQRES 7 A 222 PRO VAL GLY THR ARG ASP TRP ILE GLU GLY GLU THR TYR
SEQRES 8 A 222 GLN CYS ARG VAL THR HIS PRO HIS LEU PRO ARG ALA LEU
SEQRES 9 A 222 MET ARG SER THR THR LYS THR SER GLY PRO ARG ALA ALA
SEQRES 10 A 222 PRO GLU VAL TYR ALA PHE ALA THR PRO GLU TRP PRO GLY
SEQRES 11 A 222 SER ARG ASP LYS ARG THR LEU ALA CYS LEU ILE GLN ASN
SEQRES 12 A 222 PHE MET PRO GLU ASP ILE SER VAL GLN TRP LEU HIS ASN
SEQRES 13 A 222 GLU VAL GLN LEU PRO ASP ALA ARG HIS SER THR THR GLN
SEQRES 14 A 222 PRO ARG LYS THR LYS GLY SER GLY PHE PHE VAL PHE SER
SEQRES 15 A 222 ARG LEU GLU VAL THR ARG ALA GLU TRP GLU GLN LYS ASP
SEQRES 16 A 222 GLU PHE ILE CYS ARG ALA VAL HIS GLU ALA ALA SER PRO
SEQRES 17 A 222 SER GLN THR VAL GLN ARG ALA VAL SER VAL ASN PRO GLY
SEQRES 18 A 222 LYS
FORMUL 2 HOH *145(H2 O)
HELIX 1 1 SER A 344 ILE A 350 1 7
HELIX 2 2 GLY A 406 GLU A 412 1 7
HELIX 3 3 PRO A 486 ALA A 488 5 3
HELIX 4 4 THR A 512 GLU A 517 1 6
HELIX 5 5 GLN A 518 ASP A 520 5 3
SHEET 1 A 4 SER A 337 SER A 341 0
SHEET 2 A 4 THR A 355 ASP A 362 -1 O THR A 357 N SER A 341
SHEET 3 A 4 THR A 396 PRO A 404 -1 N LEU A 397 O ASP A 362
SHEET 4 A 4 THR A 386 GLN A 392 -1 O THR A 386 N THR A 402
SHEET 1 B 3 ASN A 371 ARG A 376 0
SHEET 2 B 3 TYR A 416 THR A 421 -1 N GLN A 417 O SER A 375
SHEET 3 B 3 LEU A 429 THR A 433 -1 O LEU A 429 N VAL A 420
SHEET 1 C 4 GLU A 444 ALA A 449 0
SHEET 2 C 4 ARG A 460 PHE A 469 -1 O ALA A 463 N PHE A 448
SHEET 3 C 4 PHE A 503 VAL A 511 -1 N PHE A 503 O PHE A 469
SHEET 4 C 4 HIS A 490 THR A 492 -1 O SER A 491 N ARG A 508
SHEET 1 D 4 GLU A 444 ALA A 449 0
SHEET 2 D 4 ARG A 460 PHE A 469 -1 O ALA A 463 N PHE A 448
SHEET 3 D 4 PHE A 503 VAL A 511 -1 N PHE A 503 O PHE A 469
SHEET 4 D 4 ARG A 496 LYS A 497 -1 N ARG A 496 O PHE A 504
SHEET 1 E 4 VAL A 483 GLN A 484 0
SHEET 2 E 4 SER A 475 HIS A 480 -1 N HIS A 480 O VAL A 483
SHEET 3 E 4 PHE A 522 VAL A 527 -1 N ILE A 523 O LEU A 479
SHEET 4 E 4 THR A 536 ALA A 540 -1 O VAL A 537 N ALA A 526
SSBOND 1 CYS A 358 CYS A 418 1555 1555 2.05
SSBOND 2 CYS A 464 CYS A 524 1555 1555 2.06
CISPEP 1 MET A 470 PRO A 471 0 -0.10
CISPEP 2 SER A 532 PRO A 533 0 1.12
CRYST1 105.600 105.600 47.100 90.00 90.00 90.00 P 4 21 2 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 0.009470 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009470 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021231 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
