HEADER CYTOKINE 13-SEP-13 4MPL
TITLE CRYSTAL STRUCTURE OF BMP9 AT 1.90 ANGSTROM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GROWTH/DIFFERENTIATION FACTOR 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 321-429;
COMPND 5 SYNONYM: GDF-2, BONE MORPHOGENETIC PROTEIN 9, BMP-9;
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 GENE: BMP9, GDF2;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCEP4
KEYWDS GROWTH FACTOR/CYTOKINE, CYTOKINE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.LI,N.W.MORRELL,Z.WEI
REVDAT 4 02-JUN-21 4MPL 1 SOURCE SEQADV
REVDAT 3 24-DEC-14 4MPL 1 JRNL
REVDAT 2 29-OCT-14 4MPL 1 JRNL
REVDAT 1 17-SEP-14 4MPL 0
JRNL AUTH Z.WEI,R.M.SALMON,P.D.UPTON,N.W.MORRELL,W.LI
JRNL TITL REGULATION OF BONE MORPHOGENETIC PROTEIN 9 (BMP9) BY
JRNL TITL 2 REDOX-DEPENDENT PROTEOLYSIS.
JRNL REF J.BIOL.CHEM. V. 289 31150 2014
JRNL REFN ISSN 0021-9258
JRNL PMID 25237187
JRNL DOI 10.1074/JBC.M114.579771
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 15087
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.199
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 : 769
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 40.1787 - 3.2486 0.99 3034 144 0.1799 0.1784
REMARK 3 2 3.2486 - 2.5786 0.99 2854 177 0.2012 0.2436
REMARK 3 3 2.5786 - 2.2527 0.99 2837 159 0.2101 0.2615
REMARK 3 4 2.2527 - 2.0467 0.99 2813 138 0.2288 0.2808
REMARK 3 5 2.0467 - 1.9000 0.98 2780 151 0.2667 0.3090
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.080
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.79
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.60
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 : 0.008 864
REMARK 3 ANGLE : 1.180 1174
REMARK 3 CHIRALITY : 0.093 129
REMARK 3 PLANARITY : 0.005 149
REMARK 3 DIHEDRAL : 12.950 309
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4MPL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1000082206.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15096
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.170
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 7.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 8.00
REMARK 200 R MERGE FOR SHELL (I) : 0.75200
REMARK 200 R SYM FOR SHELL (I) : 0.75200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.2
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.12M MAGNESIUM NITRATE, 12% PEG3350,
REMARK 280 PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 35.63500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 35.63500
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.94500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 35.63500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.47250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 35.63500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 109.41750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 35.63500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 109.41750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.63500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 36.47250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 35.63500
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 35.63500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 72.94500
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 SMTRY1 9 1.000000 0.000000 0.000000 35.63500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 35.63500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 72.94500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 35.63500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 109.41750
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 35.63500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 36.47250
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 35.63500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 36.47250
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 35.63500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 109.41750
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 35.63500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 35.63500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 72.94500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
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 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -35.63500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 36.47250
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 270 LIES ON A SPECIAL POSITION.
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 SER A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 ALA A 2
REMARK 465 GLY A 3
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 GLU A 31 CD OE1 OE2
REMARK 470 ASP A 47 CG OD1 OD2
REMARK 470 ASP A 48 CG OD1 OD2
REMARK 470 VAL A 49 CG1 CG2
REMARK 470 LYS A 87 CD CE NZ
REMARK 470 MET A 90 CG SD CE
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 HOH A 246 O HOH A 248 2.13
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 HIS A 7 75.49 -154.61
REMARK 500 TYR A 35 172.19 58.29
REMARK 500 ASP A 88 -158.18 -74.23
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4MPL A 2 110 UNP Q9UK05 GDF2_HUMAN 321 429
SEQADV 4MPL SER A -5 UNP Q9UK05 EXPRESSION TAG
SEQADV 4MPL HIS A -4 UNP Q9UK05 EXPRESSION TAG
SEQADV 4MPL HIS A -3 UNP Q9UK05 EXPRESSION TAG
SEQADV 4MPL HIS A -2 UNP Q9UK05 EXPRESSION TAG
SEQADV 4MPL HIS A -1 UNP Q9UK05 EXPRESSION TAG
SEQADV 4MPL HIS A 0 UNP Q9UK05 EXPRESSION TAG
SEQADV 4MPL HIS A 1 UNP Q9UK05 EXPRESSION TAG
SEQRES 1 A 116 SER HIS HIS HIS HIS HIS HIS ALA GLY ALA GLY SER HIS
SEQRES 2 A 116 CYS GLN LYS THR SER LEU ARG VAL ASN PHE GLU ASP ILE
SEQRES 3 A 116 GLY TRP ASP SER TRP ILE ILE ALA PRO LYS GLU TYR GLU
SEQRES 4 A 116 ALA TYR GLU CYS LYS GLY GLY CYS PHE PHE PRO LEU ALA
SEQRES 5 A 116 ASP ASP VAL THR PRO THR LYS HIS ALA ILE VAL GLN THR
SEQRES 6 A 116 LEU VAL HIS LEU LYS PHE PRO THR LYS VAL GLY LYS ALA
SEQRES 7 A 116 CYS CYS VAL PRO THR LYS LEU SER PRO ILE SER VAL LEU
SEQRES 8 A 116 TYR LYS ASP ASP MET GLY VAL PRO THR LEU LYS TYR HIS
SEQRES 9 A 116 TYR GLU GLY MET SER VAL ALA GLU CYS GLY CYS ARG
FORMUL 2 HOH *91(H2 O)
HELIX 1 1 THR A 52 PHE A 65 1 14
SHEET 1 A 2 GLN A 9 THR A 11 0
SHEET 2 A 2 GLU A 36 LYS A 38 -1 O LYS A 38 N GLN A 9
SHEET 1 B 2 ARG A 14 ASN A 16 0
SHEET 2 B 2 GLU A 31 GLU A 33 -1 O TYR A 32 N VAL A 15
SHEET 1 C 3 ILE A 26 ALA A 28 0
SHEET 2 C 3 CYS A 74 LYS A 87 -1 O LEU A 85 N ALA A 28
SHEET 3 C 3 PRO A 93 CYS A 109 -1 O LYS A 96 N VAL A 84
SSBOND 1 CYS A 8 CYS A 74 1555 1555 2.02
SSBOND 2 CYS A 37 CYS A 107 1555 1555 2.03
SSBOND 3 CYS A 41 CYS A 109 1555 1555 2.00
SSBOND 4 CYS A 73 CYS A 73 1555 6545 2.03
CISPEP 1 ALA A 28 PRO A 29 0 -3.20
CISPEP 2 PHE A 43 PRO A 44 0 3.50
CRYST1 71.270 71.270 145.890 90.00 90.00 90.00 I 41 2 2 16
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 0.014031 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014031 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006854 0.00000
(ATOM LINES ARE NOT SHOWN.)
END