HEADER METAL TRANSPORT 13-JUN-06 2HAV
TITLE APO-HUMAN SERUM TRANSFERRIN (GLYCOSYLATED)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEROTRANSFERRIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TRANSFERRIN, SIDEROPHILIN, BETA-1-METAL-BINDING GLOBULIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS SEROTRANSFERRIN, HUMAN, IRON TRANSPORTER, APO, IRON-FREE, METAL
KEYWDS 2 TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR J.WALLY,S.J.EVERSE
REVDAT 5 30-AUG-23 2HAV 1 REMARK
REVDAT 4 13-JUL-11 2HAV 1 VERSN
REVDAT 3 24-FEB-09 2HAV 1 VERSN
REVDAT 2 05-SEP-06 2HAV 1 JRNL
REVDAT 1 27-JUN-06 2HAV 0
JRNL AUTH J.WALLY,P.J.HALBROOKS,C.VONRHEIN,M.A.ROULD,S.J.EVERSE,
JRNL AUTH 2 A.B.MASON,S.K.BUCHANAN
JRNL TITL THE CRYSTAL STRUCTURE OF IRON-FREE HUMAN SERUM TRANSFERRIN
JRNL TITL 2 PROVIDES INSIGHT INTO INTER-LOBE COMMUNICATION AND RECEPTOR
JRNL TITL 3 BINDING.
JRNL REF J.BIOL.CHEM. V. 281 24934 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16793765
JRNL DOI 10.1074/JBC.M604592200
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 39242
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 + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.232
REMARK 3 FREE R VALUE : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2094
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10486
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 115
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.009 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 1.570 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HAV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000038144.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-AUG-05
REMARK 200 TEMPERATURE (KELVIN) : 103
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49871
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: HUMAN APO-N-LOBE STRUCTURE (1BP5) AND THE RABBIT
REMARK 200 HOLO-C1-SUBDOMAIN (RESIDUES 342 TO 424 AND 579 TO 676 FROM 1JNF)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30 MG/ML PROTEIN, 0.2 M AMMONIUM
REMARK 280 CITRATE PH 7.0, 20% PEG-3350, 15% GLYCEROL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 294K
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 44.16200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 100.18100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.62900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 100.18100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.16200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.62900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER.
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 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 SER A 415 N - CA - C ANGL. DEV. = 16.2 DEGREES
REMARK 500 PRO B 31 C - N - CA ANGL. DEV. = 11.6 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 VAL A 11 32.63 -99.77
REMARK 500 SER A 12 148.52 172.91
REMARK 500 ASP A 24 -70.69 -60.75
REMARK 500 VAL A 29 93.93 51.94
REMARK 500 ILE A 30 100.60 175.36
REMARK 500 PRO A 31 135.55 -33.54
REMARK 500 SER A 32 20.70 -64.39
REMARK 500 PRO A 35 150.61 -44.40
REMARK 500 ASN A 76 71.17 49.07
REMARK 500 PHE A 107 146.73 179.77
REMARK 500 LYS A 115 178.87 -59.53
REMARK 500 SER A 125 -80.44 -64.61
REMARK 500 TRP A 128 -63.86 -141.94
REMARK 500 CYS A 174 82.26 -157.59
REMARK 500 ASP A 221 -5.91 -48.84
REMARK 500 GLU A 237 31.28 -95.66
REMARK 500 CYS A 241 99.25 176.93
REMARK 500 LYS A 276 -15.28 -173.62
REMARK 500 ASP A 277 -34.75 -148.75
REMARK 500 LYS A 278 -24.50 -26.35
REMARK 500 SER A 279 141.76 -177.43
REMARK 500 PHE A 285 47.48 -103.87
REMARK 500 SER A 286 166.92 177.37
REMARK 500 LEU A 294 -45.79 70.44
REMARK 500 GLU A 328 -62.08 -103.10
REMARK 500 GLU A 333 32.79 -75.47
REMARK 500 PRO A 335 -108.61 -1.22
REMARK 500 THR A 336 -27.45 161.01
REMARK 500 ASN A 413 -143.89 -86.26
REMARK 500 LYS A 414 91.12 -3.82
REMARK 500 CYS A 418 -80.94 -12.71
REMARK 500 GLU A 419 -15.92 -38.91
REMARK 500 THR A 421 88.80 -178.38
REMARK 500 PHE A 427 113.36 23.57
REMARK 500 SER A 435 34.67 -91.23
REMARK 500 ASP A 438 10.51 44.56
REMARK 500 TRP A 441 -70.74 -44.92
REMARK 500 ASP A 442 23.83 -66.09
REMARK 500 ALA A 453 145.54 156.41
REMARK 500 THR A 457 -74.13 -64.46
REMARK 500 TRP A 460 -80.01 -142.99
REMARK 500 ASN A 469 9.95 -68.60
REMARK 500 ILE A 471 -69.36 175.91
REMARK 500 ASN A 472 56.89 76.28
REMARK 500 GLU A 478 50.97 -105.78
REMARK 500 PHE A 479 -41.91 -131.50
REMARK 500 LYS A 490 -17.96 -46.69
REMARK 500 SER A 492 163.42 -42.40
REMARK 500 MET A 499 -149.05 -85.63
REMARK 500 ASN A 504 49.86 -91.15
REMARK 500
REMARK 500 THIS ENTRY HAS 154 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR B 85 0.06 SIDE CHAIN
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 CIT B 9201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 9202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 9203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 9204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 9205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 9206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 9207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 9101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 9102
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 9103
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 9104
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BP5 RELATED DB: PDB
REMARK 900 APO HUMAN SERUM TRANSFERRIN N-LOBE
DBREF 2HAV A 4 679 UNP P02787 TRFE_HUMAN 23 698
DBREF 2HAV B 4 679 UNP P02787 TRFE_HUMAN 23 698
SEQRES 1 A 676 LYS THR VAL ARG TRP CYS ALA VAL SER GLU HIS GLU ALA
SEQRES 2 A 676 THR LYS CYS GLN SER PHE ARG ASP HIS MET LYS SER VAL
SEQRES 3 A 676 ILE PRO SER ASP GLY PRO SER VAL ALA CYS VAL LYS LYS
SEQRES 4 A 676 ALA SER TYR LEU ASP CYS ILE ARG ALA ILE ALA ALA ASN
SEQRES 5 A 676 GLU ALA ASP ALA VAL THR LEU ASP ALA GLY LEU VAL TYR
SEQRES 6 A 676 ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS PRO VAL VAL
SEQRES 7 A 676 ALA GLU PHE TYR GLY SER LYS GLU ASP PRO GLN THR PHE
SEQRES 8 A 676 TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP SER GLY PHE
SEQRES 9 A 676 GLN MET ASN GLN LEU ARG GLY LYS LYS SER CYS HIS THR
SEQRES 10 A 676 GLY LEU GLY ARG SER ALA GLY TRP ASN ILE PRO ILE GLY
SEQRES 11 A 676 LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG LYS PRO LEU
SEQRES 12 A 676 GLU LYS ALA VAL ALA ASN PHE PHE SER GLY SER CYS ALA
SEQRES 13 A 676 PRO CYS ALA ASP GLY THR ASP PHE PRO GLN LEU CYS GLN
SEQRES 14 A 676 LEU CYS PRO GLY CYS GLY CYS SER THR LEU ASN GLN TYR
SEQRES 15 A 676 PHE GLY TYR SER GLY ALA PHE LYS CYS LEU LYS ASP GLY
SEQRES 16 A 676 ALA GLY ASP VAL ALA PHE VAL LYS HIS SER THR ILE PHE
SEQRES 17 A 676 GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP GLN TYR GLU
SEQRES 18 A 676 LEU LEU CYS LEU ASP ASN THR ARG LYS PRO VAL ASP GLU
SEQRES 19 A 676 TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO SER HIS THR
SEQRES 20 A 676 VAL VAL ALA ARG SER MET GLY GLY LYS GLU ASP LEU ILE
SEQRES 21 A 676 TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS PHE GLY LYS
SEQRES 22 A 676 ASP LYS SER LYS GLU PHE GLN LEU PHE SER SER PRO HIS
SEQRES 23 A 676 GLY LYS ASP LEU LEU PHE LYS ASP SER ALA HIS GLY PHE
SEQRES 24 A 676 LEU LYS VAL PRO PRO ARG MET ASP ALA LYS MET TYR LEU
SEQRES 25 A 676 GLY TYR GLU TYR VAL THR ALA ILE ARG ASN LEU ARG GLU
SEQRES 26 A 676 GLY THR CYS PRO GLU ALA PRO THR ASP GLU CYS LYS PRO
SEQRES 27 A 676 VAL LYS TRP CYS ALA LEU SER HIS HIS GLU ARG LEU LYS
SEQRES 28 A 676 CYS ASP GLU TRP SER VAL ASN SER VAL GLY LYS ILE GLU
SEQRES 29 A 676 CYS VAL SER ALA GLU THR THR GLU ASP CYS ILE ALA LYS
SEQRES 30 A 676 ILE MET ASN GLY GLU ALA ASP ALA MET SER LEU ASP GLY
SEQRES 31 A 676 GLY PHE VAL TYR ILE ALA GLY LYS CYS GLY LEU VAL PRO
SEQRES 32 A 676 VAL LEU ALA GLU ASN TYR ASN LYS SER ASP ASN CYS GLU
SEQRES 33 A 676 ASP THR PRO GLU ALA GLY TYR PHE ALA VAL ALA VAL VAL
SEQRES 34 A 676 LYS LYS SER ALA SER ASP LEU THR TRP ASP ASN LEU LYS
SEQRES 35 A 676 GLY LYS LYS SER CYS HIS THR ALA VAL GLY ARG THR ALA
SEQRES 36 A 676 GLY TRP ASN ILE PRO MET GLY LEU LEU TYR ASN LYS ILE
SEQRES 37 A 676 ASN HIS CYS ARG PHE ASP GLU PHE PHE SER GLU GLY CYS
SEQRES 38 A 676 ALA PRO GLY SER LYS LYS ASP SER SER LEU CYS LYS LEU
SEQRES 39 A 676 CYS MET GLY SER GLY LEU ASN LEU CYS GLU PRO ASN ASN
SEQRES 40 A 676 LYS GLU GLY TYR TYR GLY TYR THR GLY ALA PHE ARG CYS
SEQRES 41 A 676 LEU VAL GLU LYS GLY ASP VAL ALA PHE VAL LYS HIS GLN
SEQRES 42 A 676 THR VAL PRO GLN ASN THR GLY GLY LYS ASN PRO ASP PRO
SEQRES 43 A 676 TRP ALA LYS ASN LEU ASN GLU LYS ASP TYR GLU LEU LEU
SEQRES 44 A 676 CYS LEU ASP GLY THR ARG LYS PRO VAL GLU GLU TYR ALA
SEQRES 45 A 676 ASN CYS HIS LEU ALA ARG ALA PRO ASN HIS ALA VAL VAL
SEQRES 46 A 676 THR ARG LYS ASP LYS GLU ALA CYS VAL HIS LYS ILE LEU
SEQRES 47 A 676 ARG GLN GLN GLN HIS LEU PHE GLY SER ASN VAL THR ASP
SEQRES 48 A 676 CYS SER GLY ASN PHE CYS LEU PHE ARG SER GLU THR LYS
SEQRES 49 A 676 ASP LEU LEU PHE ARG ASP ASP THR VAL CYS LEU ALA LYS
SEQRES 50 A 676 LEU HIS ASP ARG ASN THR TYR GLU LYS TYR LEU GLY GLU
SEQRES 51 A 676 GLU TYR VAL LYS ALA VAL GLY ASN LEU ARG LYS CYS SER
SEQRES 52 A 676 THR SER SER LEU LEU GLU ALA CYS THR PHE ARG ARG PRO
SEQRES 1 B 676 LYS THR VAL ARG TRP CYS ALA VAL SER GLU HIS GLU ALA
SEQRES 2 B 676 THR LYS CYS GLN SER PHE ARG ASP HIS MET LYS SER VAL
SEQRES 3 B 676 ILE PRO SER ASP GLY PRO SER VAL ALA CYS VAL LYS LYS
SEQRES 4 B 676 ALA SER TYR LEU ASP CYS ILE ARG ALA ILE ALA ALA ASN
SEQRES 5 B 676 GLU ALA ASP ALA VAL THR LEU ASP ALA GLY LEU VAL TYR
SEQRES 6 B 676 ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS PRO VAL VAL
SEQRES 7 B 676 ALA GLU PHE TYR GLY SER LYS GLU ASP PRO GLN THR PHE
SEQRES 8 B 676 TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP SER GLY PHE
SEQRES 9 B 676 GLN MET ASN GLN LEU ARG GLY LYS LYS SER CYS HIS THR
SEQRES 10 B 676 GLY LEU GLY ARG SER ALA GLY TRP ASN ILE PRO ILE GLY
SEQRES 11 B 676 LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG LYS PRO LEU
SEQRES 12 B 676 GLU LYS ALA VAL ALA ASN PHE PHE SER GLY SER CYS ALA
SEQRES 13 B 676 PRO CYS ALA ASP GLY THR ASP PHE PRO GLN LEU CYS GLN
SEQRES 14 B 676 LEU CYS PRO GLY CYS GLY CYS SER THR LEU ASN GLN TYR
SEQRES 15 B 676 PHE GLY TYR SER GLY ALA PHE LYS CYS LEU LYS ASP GLY
SEQRES 16 B 676 ALA GLY ASP VAL ALA PHE VAL LYS HIS SER THR ILE PHE
SEQRES 17 B 676 GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP GLN TYR GLU
SEQRES 18 B 676 LEU LEU CYS LEU ASP ASN THR ARG LYS PRO VAL ASP GLU
SEQRES 19 B 676 TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO SER HIS THR
SEQRES 20 B 676 VAL VAL ALA ARG SER MET GLY GLY LYS GLU ASP LEU ILE
SEQRES 21 B 676 TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS PHE GLY LYS
SEQRES 22 B 676 ASP LYS SER LYS GLU PHE GLN LEU PHE SER SER PRO HIS
SEQRES 23 B 676 GLY LYS ASP LEU LEU PHE LYS ASP SER ALA HIS GLY PHE
SEQRES 24 B 676 LEU LYS VAL PRO PRO ARG MET ASP ALA LYS MET TYR LEU
SEQRES 25 B 676 GLY TYR GLU TYR VAL THR ALA ILE ARG ASN LEU ARG GLU
SEQRES 26 B 676 GLY THR CYS PRO GLU ALA PRO THR ASP GLU CYS LYS PRO
SEQRES 27 B 676 VAL LYS TRP CYS ALA LEU SER HIS HIS GLU ARG LEU LYS
SEQRES 28 B 676 CYS ASP GLU TRP SER VAL ASN SER VAL GLY LYS ILE GLU
SEQRES 29 B 676 CYS VAL SER ALA GLU THR THR GLU ASP CYS ILE ALA LYS
SEQRES 30 B 676 ILE MET ASN GLY GLU ALA ASP ALA MET SER LEU ASP GLY
SEQRES 31 B 676 GLY PHE VAL TYR ILE ALA GLY LYS CYS GLY LEU VAL PRO
SEQRES 32 B 676 VAL LEU ALA GLU ASN TYR ASN LYS SER ASP ASN CYS GLU
SEQRES 33 B 676 ASP THR PRO GLU ALA GLY TYR PHE ALA VAL ALA VAL VAL
SEQRES 34 B 676 LYS LYS SER ALA SER ASP LEU THR TRP ASP ASN LEU LYS
SEQRES 35 B 676 GLY LYS LYS SER CYS HIS THR ALA VAL GLY ARG THR ALA
SEQRES 36 B 676 GLY TRP ASN ILE PRO MET GLY LEU LEU TYR ASN LYS ILE
SEQRES 37 B 676 ASN HIS CYS ARG PHE ASP GLU PHE PHE SER GLU GLY CYS
SEQRES 38 B 676 ALA PRO GLY SER LYS LYS ASP SER SER LEU CYS LYS LEU
SEQRES 39 B 676 CYS MET GLY SER GLY LEU ASN LEU CYS GLU PRO ASN ASN
SEQRES 40 B 676 LYS GLU GLY TYR TYR GLY TYR THR GLY ALA PHE ARG CYS
SEQRES 41 B 676 LEU VAL GLU LYS GLY ASP VAL ALA PHE VAL LYS HIS GLN
SEQRES 42 B 676 THR VAL PRO GLN ASN THR GLY GLY LYS ASN PRO ASP PRO
SEQRES 43 B 676 TRP ALA LYS ASN LEU ASN GLU LYS ASP TYR GLU LEU LEU
SEQRES 44 B 676 CYS LEU ASP GLY THR ARG LYS PRO VAL GLU GLU TYR ALA
SEQRES 45 B 676 ASN CYS HIS LEU ALA ARG ALA PRO ASN HIS ALA VAL VAL
SEQRES 46 B 676 THR ARG LYS ASP LYS GLU ALA CYS VAL HIS LYS ILE LEU
SEQRES 47 B 676 ARG GLN GLN GLN HIS LEU PHE GLY SER ASN VAL THR ASP
SEQRES 48 B 676 CYS SER GLY ASN PHE CYS LEU PHE ARG SER GLU THR LYS
SEQRES 49 B 676 ASP LEU LEU PHE ARG ASP ASP THR VAL CYS LEU ALA LYS
SEQRES 50 B 676 LEU HIS ASP ARG ASN THR TYR GLU LYS TYR LEU GLY GLU
SEQRES 51 B 676 GLU TYR VAL LYS ALA VAL GLY ASN LEU ARG LYS CYS SER
SEQRES 52 B 676 THR SER SER LEU LEU GLU ALA CYS THR PHE ARG ARG PRO
HET CIT A9202 13
HET CIT A9203 13
HET CIT A9207 13
HET GOL A9101 6
HET GOL A9103 6
HET GOL A9104 6
HET CIT B9201 13
HET CIT B9204 13
HET CIT B9205 13
HET CIT B9206 13
HET GOL B9102 6
HETNAM CIT CITRIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 CIT 7(C6 H8 O7)
FORMUL 6 GOL 4(C3 H8 O3)
HELIX 1 1 SER A 12 MET A 26 1 15
HELIX 2 2 SER A 44 ALA A 54 1 11
HELIX 3 3 ASP A 63 LEU A 72 1 10
HELIX 4 4 GLN A 108 LEU A 112 5 5
HELIX 5 5 TRP A 128 TYR A 136 1 9
HELIX 6 6 CYS A 137 LEU A 139 5 3
HELIX 7 7 PRO A 145 PHE A 154 1 10
HELIX 8 8 PHE A 167 CYS A 171 5 5
HELIX 9 9 CYS A 174 GLY A 178 5 5
HELIX 10 10 PHE A 186 ASP A 197 1 12
HELIX 11 11 THR A 209 LEU A 214 1 6
HELIX 12 12 ASN A 216 ASP A 221 1 6
HELIX 13 13 PRO A 234 CYS A 241 5 8
HELIX 14 14 LYS A 259 PHE A 274 1 16
HELIX 15 15 ASP A 310 GLY A 316 1 7
HELIX 16 16 GLY A 316 GLY A 329 1 14
HELIX 17 17 SER A 348 VAL A 363 1 16
HELIX 18 18 THR A 373 GLY A 384 1 12
HELIX 19 19 ASP A 392 CYS A 402 1 11
HELIX 20 20 ASN A 417 THR A 421 5 5
HELIX 21 21 THR A 440 LEU A 444 5 5
HELIX 22 22 TRP A 460 LEU A 467 1 8
HELIX 23 23 TYR A 468 ILE A 471 5 4
HELIX 24 24 ARG A 475 PHE A 479 5 5
HELIX 25 25 TYR A 515 LYS A 527 1 13
HELIX 26 26 GLN A 536 ASN A 541 1 6
HELIX 27 27 ASP A 548 LYS A 552 5 5
HELIX 28 28 ASN A 555 LYS A 557 5 3
HELIX 29 29 GLU A 572 CYS A 577 5 6
HELIX 30 30 LYS A 593 GLY A 609 1 17
HELIX 31 31 THR A 646 GLY A 652 1 7
HELIX 32 32 GLY A 652 ARG A 663 1 12
HELIX 33 33 SER A 668 ARG A 678 1 11
HELIX 34 34 SER B 12 SER B 28 1 17
HELIX 35 35 SER B 44 ALA B 54 1 11
HELIX 36 36 ASP B 63 LEU B 72 1 10
HELIX 37 37 GLN B 108 LEU B 112 5 5
HELIX 38 38 TRP B 128 LEU B 135 1 8
HELIX 39 39 TYR B 136 LEU B 139 5 4
HELIX 40 40 PRO B 145 PHE B 154 1 10
HELIX 41 41 PHE B 167 GLN B 172 5 6
HELIX 42 42 PHE B 186 ASP B 197 1 12
HELIX 43 43 HIS B 207 GLU B 212 1 6
HELIX 44 44 ASN B 216 ASP B 221 1 6
HELIX 45 45 GLU B 237 CYS B 241 5 5
HELIX 46 46 LYS B 259 GLY B 275 1 17
HELIX 47 47 ASP B 310 GLY B 316 1 7
HELIX 48 48 GLY B 316 GLY B 329 1 14
HELIX 49 49 SER B 348 SER B 362 1 15
HELIX 50 50 THR B 373 ASN B 383 1 11
HELIX 51 51 ASP B 392 CYS B 402 1 11
HELIX 52 52 TRP B 460 LEU B 467 1 8
HELIX 53 53 LEU B 467 ASN B 472 1 6
HELIX 54 54 ARG B 475 PHE B 479 5 5
HELIX 55 55 SER B 501 LEU B 505 5 5
HELIX 56 56 TYR B 515 LYS B 527 1 13
HELIX 57 57 THR B 537 ASN B 541 5 5
HELIX 58 58 PRO B 570 CYS B 577 5 8
HELIX 59 59 LYS B 593 GLY B 609 1 17
HELIX 60 60 THR B 646 GLY B 652 1 7
HELIX 61 61 GLY B 652 SER B 666 1 15
HELIX 62 62 SER B 668 ARG B 678 1 11
SHEET 1 A 2 THR A 5 ALA A 10 0
SHEET 2 A 2 SER A 36 LYS A 41 1 O VAL A 40 N TRP A 8
SHEET 1 B 4 VAL A 60 LEU A 62 0
SHEET 2 B 4 HIS A 249 ARG A 254 -1 O THR A 250 N LEU A 62
SHEET 3 B 4 LEU A 77 PHE A 84 -1 N VAL A 80 O VAL A 251
SHEET 4 B 4 GLY A 301 LYS A 304 -1 O LEU A 303 N ALA A 82
SHEET 1 C 5 GLY A 156 CYS A 158 0
SHEET 2 C 5 LYS A 116 HIS A 119 1 N HIS A 119 O CYS A 158
SHEET 3 C 5 VAL A 202 LYS A 206 1 O VAL A 202 N LYS A 116
SHEET 4 C 5 PHE A 94 LYS A 102 -1 N VAL A 100 O ALA A 203
SHEET 5 C 5 TYR A 223 LEU A 225 -1 O GLU A 224 N VAL A 101
SHEET 1 D 5 GLY A 156 CYS A 158 0
SHEET 2 D 5 LYS A 116 HIS A 119 1 N HIS A 119 O CYS A 158
SHEET 3 D 5 VAL A 202 LYS A 206 1 O VAL A 202 N LYS A 116
SHEET 4 D 5 PHE A 94 LYS A 102 -1 N VAL A 100 O ALA A 203
SHEET 5 D 5 ALA A 244 PRO A 247 -1 O VAL A 246 N TYR A 95
SHEET 1 E 2 VAL A 342 ALA A 346 0
SHEET 2 E 2 ILE A 366 SER A 370 1 O VAL A 369 N ALA A 346
SHEET 1 F 4 ALA A 388 LEU A 391 0
SHEET 2 F 4 ALA A 586 THR A 589 -1 O ALA A 586 N LEU A 391
SHEET 3 F 4 VAL A 405 ASN A 411 -1 N LEU A 408 O VAL A 587
SHEET 4 F 4 CYS A 637 LYS A 640 -1 O ALA A 639 N ALA A 409
SHEET 1 G 6 GLU A 482 CYS A 484 0
SHEET 2 G 6 LYS A 448 HIS A 451 1 N SER A 449 O GLU A 482
SHEET 3 G 6 VAL A 530 LYS A 534 1 O PHE A 532 N CYS A 450
SHEET 4 G 6 ALA A 428 LYS A 433 -1 N VAL A 431 O ALA A 531
SHEET 5 G 6 TYR A 559 LEU A 562 -1 O GLU A 560 N VAL A 432
SHEET 6 G 6 ARG A 568 PRO A 570 -1 O LYS A 569 N LEU A 561
SHEET 1 H 2 THR B 5 ALA B 10 0
SHEET 2 H 2 SER B 36 LYS B 41 1 O VAL B 40 N ALA B 10
SHEET 1 I 4 VAL B 60 LEU B 62 0
SHEET 2 I 4 THR B 250 ARG B 254 -1 O THR B 250 N LEU B 62
SHEET 3 I 4 LEU B 77 PHE B 84 -1 N VAL B 81 O VAL B 251
SHEET 4 I 4 GLY B 301 LYS B 304 -1 O LEU B 303 N ALA B 82
SHEET 1 J 5 SER B 157 CYS B 158 0
SHEET 2 J 5 SER B 117 HIS B 119 1 N SER B 117 O CYS B 158
SHEET 3 J 5 VAL B 202 LYS B 206 1 O VAL B 202 N CYS B 118
SHEET 4 J 5 PHE B 94 LYS B 102 -1 N VAL B 98 O VAL B 205
SHEET 5 J 5 TYR B 223 LEU B 226 -1 O GLU B 224 N VAL B 101
SHEET 1 K 5 SER B 157 CYS B 158 0
SHEET 2 K 5 SER B 117 HIS B 119 1 N SER B 117 O CYS B 158
SHEET 3 K 5 VAL B 202 LYS B 206 1 O VAL B 202 N CYS B 118
SHEET 4 K 5 PHE B 94 LYS B 102 -1 N VAL B 98 O VAL B 205
SHEET 5 K 5 ALA B 244 PRO B 247 -1 O VAL B 246 N TYR B 95
SHEET 1 L 2 VAL B 342 ALA B 346 0
SHEET 2 L 2 ILE B 366 SER B 370 1 O VAL B 369 N ALA B 346
SHEET 1 M 4 ALA B 388 LEU B 391 0
SHEET 2 M 4 ALA B 586 THR B 589 -1 O ALA B 586 N LEU B 391
SHEET 3 M 4 VAL B 405 ASN B 411 -1 N VAL B 405 O THR B 589
SHEET 4 M 4 CYS B 637 LYS B 640 -1 O ALA B 639 N ALA B 409
SHEET 1 N 5 GLU B 482 CYS B 484 0
SHEET 2 N 5 LYS B 448 HIS B 451 1 N HIS B 451 O CYS B 484
SHEET 3 N 5 VAL B 530 LYS B 534 1 O VAL B 530 N CYS B 450
SHEET 4 N 5 ALA B 428 LYS B 433 -1 N VAL B 429 O VAL B 533
SHEET 5 N 5 TYR B 559 GLU B 560 -1 O GLU B 560 N VAL B 432
SSBOND 1 CYS A 9 CYS A 48 1555 1555 2.04
SSBOND 2 CYS A 19 CYS A 39 1555 1555 2.04
SSBOND 3 CYS A 118 CYS A 194 1555 1555 2.04
SSBOND 4 CYS A 137 CYS A 331 1555 1555 2.04
SSBOND 5 CYS A 158 CYS A 174 1555 1555 2.04
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 2.03
SSBOND 9 CYS A 339 CYS A 596 1555 1555 2.04
SSBOND 10 CYS A 345 CYS A 377 1555 1555 2.03
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 2.04
SSBOND 14 CYS A 450 CYS A 523 1555 1555 2.04
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 2.04
SSBOND 18 CYS A 563 CYS A 577 1555 1555 2.03
SSBOND 19 CYS A 615 CYS A 620 1555 1555 2.03
SSBOND 20 CYS B 9 CYS B 48 1555 1555 2.04
SSBOND 21 CYS B 19 CYS B 39 1555 1555 2.04
SSBOND 22 CYS B 118 CYS B 194 1555 1555 2.03
SSBOND 23 CYS B 137 CYS B 331 1555 1555 2.04
SSBOND 24 CYS B 158 CYS B 174 1555 1555 2.04
SSBOND 25 CYS B 161 CYS B 179 1555 1555 2.04
SSBOND 26 CYS B 171 CYS B 177 1555 1555 2.03
SSBOND 27 CYS B 227 CYS B 241 1555 1555 2.03
SSBOND 28 CYS B 339 CYS B 596 1555 1555 2.03
SSBOND 29 CYS B 345 CYS B 377 1555 1555 2.03
SSBOND 30 CYS B 355 CYS B 368 1555 1555 2.04
SSBOND 31 CYS B 402 CYS B 674 1555 1555 2.04
SSBOND 32 CYS B 418 CYS B 637 1555 1555 2.03
SSBOND 33 CYS B 450 CYS B 523 1555 1555 2.03
SSBOND 34 CYS B 474 CYS B 665 1555 1555 2.04
SSBOND 35 CYS B 484 CYS B 498 1555 1555 2.03
SSBOND 36 CYS B 495 CYS B 506 1555 1555 2.03
SSBOND 37 CYS B 563 CYS B 577 1555 1555 2.03
SSBOND 38 CYS B 615 CYS B 620 1555 1555 2.04
CISPEP 1 ALA A 73 PRO A 74 0 0.13
CISPEP 2 GLU A 141 PRO A 142 0 0.39
CISPEP 3 LYS A 144 PRO A 145 0 -0.11
CISPEP 4 ALA B 73 PRO B 74 0 -0.09
CISPEP 5 GLU B 141 PRO B 142 0 0.05
CISPEP 6 LYS B 144 PRO B 145 0 -0.15
SITE 1 AC1 6 SER A 348 HIS A 349 HIS A 350 SER B 348
SITE 2 AC1 6 HIS B 349 HIS B 350
SITE 1 AC2 7 TYR A 426 ARG A 456 THR A 457 ALA A 458
SITE 2 AC2 7 TYR A 517 HIS A 585 ARG A 632
SITE 1 AC3 5 TYR A 515 GLY A 516 TYR A 517 THR A 518
SITE 2 AC3 5 GLY A 519
SITE 1 AC4 4 TYR B 426 ARG B 456 THR B 457 ARG B 632
SITE 1 AC5 5 ARG B 456 TYR B 515 GLY B 516 TYR B 517
SITE 2 AC5 5 THR B 518
SITE 1 AC6 7 TYR B 95 THR B 120 ARG B 124 SER B 125
SITE 2 AC6 7 ALA B 126 GLY B 127 TYR B 188
SITE 1 AC7 6 TYR A 95 ARG A 124 SER A 125 TYR A 188
SITE 2 AC7 6 LYS A 206 LYS A 296
SITE 1 AC8 3 ARG A 124 GLY A 187 TYR A 188
SITE 1 AC9 4 ARG B 124 PHE B 186 GLY B 187 TYR B 188
SITE 1 BC1 6 CYS A 563 LEU A 564 ASP A 565 ASN A 576
SITE 2 BC1 6 CYS A 577 HIS A 578
SITE 1 BC2 5 CYS A 227 LEU A 228 ASP A 229 CYS A 241
SITE 2 BC2 5 HIS A 242
CRYST1 88.324 103.258 200.362 90.00 90.00 90.00 P 21 21 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 0.011322 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009684 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004991 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
