HEADER TRANSFERASE 20-SEP-00 1FVR
TITLE TIE2 KINASE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE TIE-2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KINASE DOMAIN;
COMPND 5 EC: 2.7.1.112;
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: UNIDENTIFIED BACULOVIRUS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 10469
KEYWDS TYROSINE KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.SHEWCHUK,A.M.HASSELL,B.ELLIS,W.D.HOLMES,R.DAVIS,E.L.HORNE,
AUTHOR 2 S.H.KADWELL,D.D.MCKEE,J.T.MOORE
REVDAT 5 07-FEB-24 1FVR 1 SEQADV
REVDAT 4 31-JAN-18 1FVR 1 REMARK
REVDAT 3 04-OCT-17 1FVR 1 REMARK
REVDAT 2 24-FEB-09 1FVR 1 VERSN
REVDAT 1 20-SEP-01 1FVR 0
JRNL AUTH L.M.SHEWCHUK,A.M.HASSELL,B.ELLIS,W.D.HOLMES,R.DAVIS,
JRNL AUTH 2 E.L.HORNE,S.H.KADWELL,D.D.MCKEE,J.T.MOORE
JRNL TITL STRUCTURE OF THE TIE2 RTK DOMAIN: SELF-INHIBITION BY THE
JRNL TITL 2 NUCLEOTIDE BINDING LOOP, ACTIVATION LOOP, AND C-TERMINAL
JRNL TITL 3 TAIL.
JRNL REF STRUCTURE FOLD.DES. V. 8 1105 2000
JRNL REFN ISSN 0969-2126
JRNL PMID 11080633
JRNL DOI 10.1016/S0969-2126(00)00516-5
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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) (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 39864
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) : 0.225
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4089
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 : 4760
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 441
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.90
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 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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.150
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 ; 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 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: NULL
REMARK 4
REMARK 4 1FVR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000011941.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JAN-00
REMARK 200 TEMPERATURE (KELVIN) : 118
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39864
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.20000
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: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5% PEG12000, 2.5% GLYCEROL, 100MM
REMARK 280 HEPES, 10MM SPERMIDINE, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 22K, TEMPERATURE 295.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 46.44350
REMARK 290 SMTRY3 2 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 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 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 MET A 798
REMARK 465 LYS A 799
REMARK 465 LYS A 800
REMARK 465 HIS A 801
REMARK 465 HIS A 802
REMARK 465 HIS A 803
REMARK 465 HIS A 804
REMARK 465 HIS A 805
REMARK 465 HIS A 806
REMARK 465 GLY A 807
REMARK 465 LYS A 808
REMARK 465 ASN A 809
REMARK 465 ASN A 810
REMARK 465 PRO A 811
REMARK 465 ASP A 812
REMARK 465 ALA A 861
REMARK 465 SER A 862
REMARK 465 LYS A 863
REMARK 465 ASP A 864
REMARK 465 ASP A 865
REMARK 465 HIS A 866
REMARK 465 THR A 996
REMARK 465 MET A 997
REMARK 465 GLY A 998
REMARK 465 ARG A 999
REMARK 465 GLU A 1122
REMARK 465 ALA A 1123
REMARK 465 ALA A 1124
REMARK 465 MET B 798
REMARK 465 LYS B 799
REMARK 465 LYS B 800
REMARK 465 HIS B 801
REMARK 465 HIS B 802
REMARK 465 HIS B 803
REMARK 465 HIS B 804
REMARK 465 HIS B 805
REMARK 465 HIS B 806
REMARK 465 GLY B 807
REMARK 465 LYS B 808
REMARK 465 ASN B 809
REMARK 465 ASN B 810
REMARK 465 PRO B 811
REMARK 465 ASP B 812
REMARK 465 ALA B 861
REMARK 465 SER B 862
REMARK 465 LYS B 863
REMARK 465 ASP B 864
REMARK 465 ASP B 865
REMARK 465 HIS B 866
REMARK 465 THR B 996
REMARK 465 MET B 997
REMARK 465 GLY B 998
REMARK 465 GLU B 1122
REMARK 465 ALA B 1123
REMARK 465 ALA B 1124
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 PRO A 813 CG CD
REMARK 470 LYS A 858 CG CD CE NZ
REMARK 470 TYR A 860 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 867 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 995 CG CD CE NZ
REMARK 470 ARG A1099 CG CD NE CZ NH1 NH2
REMARK 470 SER A1119 OG
REMARK 470 PRO B 813 CG CD
REMARK 470 LYS B 858 CG CD CE NZ
REMARK 470 TYR B 860 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 867 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 895 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 994 CG CD CE NZ
REMARK 470 LYS B 995 CG CD CE NZ
REMARK 470 ARG B 999 CG CD NE CZ NH1 NH2
REMARK 470 ARG B1099 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 832 77.30 -150.51
REMARK 500 ASP A 923 70.14 -158.16
REMARK 500 ARG A 963 -26.26 81.63
REMARK 500 LYS A 994 -72.61 -40.14
REMARK 500 TYR A1108 -122.99 58.07
REMARK 500 LYS A1110 135.60 -171.63
REMARK 500 GLU B 832 77.04 -155.40
REMARK 500 ARG B 918 73.63 -68.43
REMARK 500 ASP B 923 68.13 -165.37
REMARK 500 ARG B 963 -19.06 80.81
REMARK 500 ASP B 964 52.10 -145.13
REMARK 500 LYS B1100 138.60 -4.61
REMARK 500 TYR B1108 -127.07 58.15
REMARK 500 ALA B1120 53.68 -90.76
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FVR A 808 1124 UNP Q02763 TIE2_HUMAN 808 1124
DBREF 1FVR B 808 1124 UNP Q02763 TIE2_HUMAN 808 1124
SEQADV 1FVR MET A 798 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR LYS A 799 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR LYS A 800 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR HIS A 801 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR HIS A 802 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR HIS A 803 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR HIS A 804 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR HIS A 805 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR HIS A 806 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR GLY A 807 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR MET B 798 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR LYS B 799 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR LYS B 800 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR HIS B 801 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR HIS B 802 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR HIS B 803 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR HIS B 804 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR HIS B 805 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR HIS B 806 UNP Q02763 EXPRESSION TAG
SEQADV 1FVR GLY B 807 UNP Q02763 EXPRESSION TAG
SEQRES 1 A 327 MET LYS LYS HIS HIS HIS HIS HIS HIS GLY LYS ASN ASN
SEQRES 2 A 327 PRO ASP PRO THR ILE TYR PRO VAL LEU ASP TRP ASN ASP
SEQRES 3 A 327 ILE LYS PHE GLN ASP VAL ILE GLY GLU GLY ASN PHE GLY
SEQRES 4 A 327 GLN VAL LEU LYS ALA ARG ILE LYS LYS ASP GLY LEU ARG
SEQRES 5 A 327 MET ASP ALA ALA ILE LYS ARG MET LYS GLU TYR ALA SER
SEQRES 6 A 327 LYS ASP ASP HIS ARG ASP PHE ALA GLY GLU LEU GLU VAL
SEQRES 7 A 327 LEU CYS LYS LEU GLY HIS HIS PRO ASN ILE ILE ASN LEU
SEQRES 8 A 327 LEU GLY ALA CYS GLU HIS ARG GLY TYR LEU TYR LEU ALA
SEQRES 9 A 327 ILE GLU TYR ALA PRO HIS GLY ASN LEU LEU ASP PHE LEU
SEQRES 10 A 327 ARG LYS SER ARG VAL LEU GLU THR ASP PRO ALA PHE ALA
SEQRES 11 A 327 ILE ALA ASN SER THR ALA SER THR LEU SER SER GLN GLN
SEQRES 12 A 327 LEU LEU HIS PHE ALA ALA ASP VAL ALA ARG GLY MET ASP
SEQRES 13 A 327 TYR LEU SER GLN LYS GLN PHE ILE HIS ARG ASP LEU ALA
SEQRES 14 A 327 ALA ARG ASN ILE LEU VAL GLY GLU ASN TYR VAL ALA LYS
SEQRES 15 A 327 ILE ALA ASP PHE GLY LEU SER ARG GLY GLN GLU VAL TYR
SEQRES 16 A 327 VAL LYS LYS THR MET GLY ARG LEU PRO VAL ARG TRP MET
SEQRES 17 A 327 ALA ILE GLU SER LEU ASN TYR SER VAL TYR THR THR ASN
SEQRES 18 A 327 SER ASP VAL TRP SER TYR GLY VAL LEU LEU TRP GLU ILE
SEQRES 19 A 327 VAL SER LEU GLY GLY THR PRO TYR CYS GLY MET THR CYS
SEQRES 20 A 327 ALA GLU LEU TYR GLU LYS LEU PRO GLN GLY TYR ARG LEU
SEQRES 21 A 327 GLU LYS PRO LEU ASN CYS ASP ASP GLU VAL TYR ASP LEU
SEQRES 22 A 327 MET ARG GLN CYS TRP ARG GLU LYS PRO TYR GLU ARG PRO
SEQRES 23 A 327 SER PHE ALA GLN ILE LEU VAL SER LEU ASN ARG MET LEU
SEQRES 24 A 327 GLU GLU ARG LYS THR TYR VAL ASN THR THR LEU TYR GLU
SEQRES 25 A 327 LYS PHE THR TYR ALA GLY ILE ASP CYS SER ALA GLU GLU
SEQRES 26 A 327 ALA ALA
SEQRES 1 B 327 MET LYS LYS HIS HIS HIS HIS HIS HIS GLY LYS ASN ASN
SEQRES 2 B 327 PRO ASP PRO THR ILE TYR PRO VAL LEU ASP TRP ASN ASP
SEQRES 3 B 327 ILE LYS PHE GLN ASP VAL ILE GLY GLU GLY ASN PHE GLY
SEQRES 4 B 327 GLN VAL LEU LYS ALA ARG ILE LYS LYS ASP GLY LEU ARG
SEQRES 5 B 327 MET ASP ALA ALA ILE LYS ARG MET LYS GLU TYR ALA SER
SEQRES 6 B 327 LYS ASP ASP HIS ARG ASP PHE ALA GLY GLU LEU GLU VAL
SEQRES 7 B 327 LEU CYS LYS LEU GLY HIS HIS PRO ASN ILE ILE ASN LEU
SEQRES 8 B 327 LEU GLY ALA CYS GLU HIS ARG GLY TYR LEU TYR LEU ALA
SEQRES 9 B 327 ILE GLU TYR ALA PRO HIS GLY ASN LEU LEU ASP PHE LEU
SEQRES 10 B 327 ARG LYS SER ARG VAL LEU GLU THR ASP PRO ALA PHE ALA
SEQRES 11 B 327 ILE ALA ASN SER THR ALA SER THR LEU SER SER GLN GLN
SEQRES 12 B 327 LEU LEU HIS PHE ALA ALA ASP VAL ALA ARG GLY MET ASP
SEQRES 13 B 327 TYR LEU SER GLN LYS GLN PHE ILE HIS ARG ASP LEU ALA
SEQRES 14 B 327 ALA ARG ASN ILE LEU VAL GLY GLU ASN TYR VAL ALA LYS
SEQRES 15 B 327 ILE ALA ASP PHE GLY LEU SER ARG GLY GLN GLU VAL TYR
SEQRES 16 B 327 VAL LYS LYS THR MET GLY ARG LEU PRO VAL ARG TRP MET
SEQRES 17 B 327 ALA ILE GLU SER LEU ASN TYR SER VAL TYR THR THR ASN
SEQRES 18 B 327 SER ASP VAL TRP SER TYR GLY VAL LEU LEU TRP GLU ILE
SEQRES 19 B 327 VAL SER LEU GLY GLY THR PRO TYR CYS GLY MET THR CYS
SEQRES 20 B 327 ALA GLU LEU TYR GLU LYS LEU PRO GLN GLY TYR ARG LEU
SEQRES 21 B 327 GLU LYS PRO LEU ASN CYS ASP ASP GLU VAL TYR ASP LEU
SEQRES 22 B 327 MET ARG GLN CYS TRP ARG GLU LYS PRO TYR GLU ARG PRO
SEQRES 23 B 327 SER PHE ALA GLN ILE LEU VAL SER LEU ASN ARG MET LEU
SEQRES 24 B 327 GLU GLU ARG LYS THR TYR VAL ASN THR THR LEU TYR GLU
SEQRES 25 B 327 LYS PHE THR TYR ALA GLY ILE ASP CYS SER ALA GLU GLU
SEQRES 26 B 327 ALA ALA
FORMUL 3 HOH *441(H2 O)
HELIX 1 1 ASP A 820 ILE A 824 5 5
HELIX 2 2 GLY A 833 PHE A 835 5 3
HELIX 3 3 ARG A 867 CYS A 877 1 11
HELIX 4 4 ASN A 909 LYS A 916 1 8
HELIX 5 5 ARG A 918 ASP A 923 1 6
HELIX 6 6 ASP A 923 ASN A 930 1 8
HELIX 7 7 SER A 937 LYS A 958 1 22
HELIX 8 8 ALA A 966 ARG A 968 5 3
HELIX 9 9 GLU A 974 TYR A 976 5 3
HELIX 10 10 ALA A 1006 SER A 1013 1 8
HELIX 11 11 THR A 1016 SER A 1033 1 18
HELIX 12 12 THR A 1043 LEU A 1051 1 9
HELIX 13 13 PRO A 1052 GLY A 1054 5 3
HELIX 14 14 ASP A 1064 TRP A 1075 1 12
HELIX 15 15 LYS A 1078 ARG A 1082 5 5
HELIX 16 16 SER A 1084 GLU A 1098 1 15
HELIX 17 17 ASP A 1117 GLU A 1121 5 5
HELIX 18 18 ASP B 820 ILE B 824 5 5
HELIX 19 19 GLY B 833 PHE B 835 5 3
HELIX 20 20 ARG B 867 LYS B 878 1 12
HELIX 21 21 ASN B 909 SER B 917 1 9
HELIX 22 22 ARG B 918 ASP B 923 1 6
HELIX 23 23 ASP B 923 ASN B 930 1 8
HELIX 24 24 SER B 937 GLN B 957 1 21
HELIX 25 25 ALA B 966 ARG B 968 5 3
HELIX 26 26 GLU B 974 TYR B 976 5 3
HELIX 27 27 PRO B 1001 MET B 1005 5 5
HELIX 28 28 ALA B 1006 SER B 1013 1 8
HELIX 29 29 THR B 1016 SER B 1033 1 18
HELIX 30 30 THR B 1043 LEU B 1051 1 9
HELIX 31 31 PRO B 1052 GLY B 1054 5 3
HELIX 32 32 ASP B 1064 TRP B 1075 1 12
HELIX 33 33 LYS B 1078 ARG B 1082 5 5
HELIX 34 34 SER B 1084 GLU B 1098 1 15
SHEET 1 A 5 LYS A 825 GLY A 831 0
SHEET 2 A 5 GLN A 837 LYS A 845 -1 N VAL A 838 O ILE A 830
SHEET 3 A 5 LEU A 848 LYS A 858 -1 O LEU A 848 N LYS A 845
SHEET 4 A 5 TYR A 897 ILE A 902 -1 N LEU A 898 O MET A 857
SHEET 5 A 5 LEU A 888 HIS A 894 -1 N LEU A 889 O ALA A 901
SHEET 1 B 2 PHE A 960 ILE A 961 0
SHEET 2 B 2 SER A 986 ARG A 987 -1 O SER A 986 N ILE A 961
SHEET 1 C 2 ILE A 970 VAL A 972 0
SHEET 2 C 2 ALA A 978 ILE A 980 -1 N LYS A 979 O LEU A 971
SHEET 1 D 2 VAL A 991 TYR A 992 0
SHEET 2 D 2 VAL A1014 TYR A1015 -1 N TYR A1015 O VAL A 991
SHEET 1 E 5 LYS B 825 GLY B 831 0
SHEET 2 E 5 GLN B 837 LYS B 845 -1 N VAL B 838 O ILE B 830
SHEET 3 E 5 LEU B 848 LYS B 858 -1 O LEU B 848 N LYS B 845
SHEET 4 E 5 TYR B 897 ILE B 902 -1 N LEU B 898 O MET B 857
SHEET 5 E 5 LEU B 888 HIS B 894 -1 N LEU B 889 O ALA B 901
SHEET 1 F 2 PHE B 960 ILE B 961 0
SHEET 2 F 2 SER B 986 ARG B 987 -1 O SER B 986 N ILE B 961
SHEET 1 G 2 ILE B 970 VAL B 972 0
SHEET 2 G 2 ALA B 978 ILE B 980 -1 O LYS B 979 N LEU B 971
SHEET 1 H 2 VAL B 991 TYR B 992 0
SHEET 2 H 2 VAL B1014 TYR B1015 -1 O TYR B1015 N VAL B 991
CISPEP 1 TYR A 816 PRO A 817 0 -0.12
CISPEP 2 TYR B 816 PRO B 817 0 -0.06
CRYST1 66.494 92.887 70.798 90.00 108.93 90.00 P 1 21 1 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 0.015039 0.000000 0.005157 0.00000
SCALE2 0.000000 0.010766 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014932 0.00000
(ATOM LINES ARE NOT SHOWN.)
END