HEADER SIGNALING PROTEIN 28-APR-13 4KFW
TITLE STRUCTURAL INSIGHT INTO GOLGI MEMBRANE STACKING BY GRASP65 AND GRASP55
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GOLGI REASSEMBLY STACKING PROTEIN 2;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: GORASP2, RCG_26651;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GOLGI STACKING PROTEIN, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR X.LIU,J.HU
REVDAT 4 20-MAR-24 4KFW 1 REMARK
REVDAT 3 15-NOV-17 4KFW 1 REMARK
REVDAT 2 22-JAN-14 4KFW 1 JRNL
REVDAT 1 21-AUG-13 4KFW 0
JRNL AUTH Y.FENG,W.YU,X.LI,S.LIN,Y.ZHOU,J.HU,X.LIU
JRNL TITL STRUCTURAL INSIGHT INTO GOLGI MEMBRANE STACKING BY GRASP65
JRNL TITL 2 AND GRASP55 PROTEINS
JRNL REF J.BIOL.CHEM. V. 288 28418 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 23940043
JRNL DOI 10.1074/JBC.M113.478024
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 14320
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 717
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 41.8153 - 4.6154 0.98 2881 145 0.1777 0.2436
REMARK 3 2 4.6154 - 3.6641 0.97 2691 144 0.1812 0.2739
REMARK 3 3 3.6641 - 3.2011 0.97 2632 145 0.2023 0.3181
REMARK 3 4 3.2011 - 2.9085 1.00 2724 131 0.2271 0.3287
REMARK 3 5 2.9085 - 2.7000 1.00 2675 152 0.2538 0.3480
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 : 0.29
REMARK 3 B_SOL : 41.28
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.840
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) : -0.02610
REMARK 3 B22 (A**2) : -0.02610
REMARK 3 B33 (A**2) : 0.05230
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 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 3303
REMARK 3 ANGLE : 1.112 4482
REMARK 3 CHIRALITY : 0.074 491
REMARK 3 PLANARITY : 0.004 590
REMARK 3 DIHEDRAL : 18.060 1198
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -41.0705 16.2534 -17.6074
REMARK 3 T TENSOR
REMARK 3 T11: 0.2593 T22: 0.3087
REMARK 3 T33: 0.2962 T12: 0.0205
REMARK 3 T13: -0.0297 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.3384 L22: 0.5553
REMARK 3 L33: 0.7512 L12: -0.2463
REMARK 3 L13: 0.4393 L23: -0.4478
REMARK 3 S TENSOR
REMARK 3 S11: -0.0248 S12: -0.1118 S13: 0.0141
REMARK 3 S21: 0.0451 S22: 0.0173 S23: 0.0932
REMARK 3 S31: 0.0035 S32: -0.0822 S33: 0.0000
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 4KFW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000079287.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BSRF
REMARK 200 BEAMLINE : 3W1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : 0.9793
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14443
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.390
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS (PH 8.5) 25% PEG3350 0.2 M
REMARK 280 (NH4)2AC, LIQUID DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.57650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.53850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.53850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 108.86475
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.53850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.53850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 36.28825
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.53850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.53850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 108.86475
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.53850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.53850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 36.28825
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 72.57650
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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 1
REMARK 465 GLY A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 GLN A 5
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 SER B 4
REMARK 465 GLN B 5
REMARK 465 SER B 6
REMARK 465 VAL B 7
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 7 -56.90 -132.49
REMARK 500 GLU A 8 94.23 43.07
REMARK 500 ILE A 9 79.80 -117.70
REMARK 500 PRO A 10 88.38 -40.01
REMARK 500 PHE A 36 -37.13 78.94
REMARK 500 CYS A 103 -177.73 -177.42
REMARK 500 LEU A 116 -125.86 -98.13
REMARK 500 HIS A 132 -38.72 69.47
REMARK 500 MET A 143 12.78 93.36
REMARK 500 GLU A 145 -137.49 -97.35
REMARK 500 SER A 146 85.96 -58.50
REMARK 500 GLU A 147 -163.70 -67.91
REMARK 500 ASP A 148 115.54 91.69
REMARK 500 LEU A 199 0.86 81.17
REMARK 500 ARG A 205 -93.17 -160.60
REMARK 500 GLU A 208 115.94 77.85
REMARK 500 PRO B 10 -116.80 -91.57
REMARK 500 PHE B 36 -47.96 75.86
REMARK 500 ASP B 51 93.57 -67.82
REMARK 500 LEU B 116 -131.80 -103.16
REMARK 500 HIS B 132 -27.60 65.11
REMARK 500 MET B 143 165.80 -49.74
REMARK 500 ASN B 144 -28.72 84.23
REMARK 500 ASN B 181 88.22 -151.63
REMARK 500 SER B 182 -8.21 -56.56
REMARK 500 LEU B 199 5.02 80.55
REMARK 500 ARG B 205 100.98 68.41
REMARK 500 PRO B 206 -71.70 -58.40
REMARK 500 PHE B 207 -50.67 120.03
REMARK 500 GLU B 209 -11.63 -44.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KFV RELATED DB: PDB
DBREF 4KFW A 1 215 UNP Q68G33 Q68G33_RAT 1 215
DBREF 4KFW B 1 215 UNP Q68G33 Q68G33_RAT 1 215
SEQRES 1 A 215 MET GLY SER SER GLN SER VAL GLU ILE PRO GLY GLY GLY
SEQRES 2 A 215 THR GLU GLY TYR HIS VAL LEU ARG VAL GLN GLU ASN SER
SEQRES 3 A 215 PRO GLY HIS ARG ALA GLY LEU GLU PRO PHE PHE ASP PHE
SEQRES 4 A 215 ILE VAL SER ILE ASN GLY SER ARG LEU ASN LYS ASP ASN
SEQRES 5 A 215 ASP THR LEU LYS ASP LEU LEU LYS ALA ASN VAL GLU LYS
SEQRES 6 A 215 PRO VAL LYS MET LEU ILE TYR SER SER LYS THR LEU GLU
SEQRES 7 A 215 LEU ARG GLU ALA SER VAL THR PRO SER ASN LEU TRP GLY
SEQRES 8 A 215 GLY GLN GLY LEU LEU GLY VAL SER ILE ARG PHE CYS SER
SEQRES 9 A 215 PHE ASP GLY ALA ASN GLU ASN VAL TRP HIS VAL LEU GLU
SEQRES 10 A 215 VAL GLU SER ASN SER PRO ALA ALA LEU ALA GLY LEU ARG
SEQRES 11 A 215 PRO HIS SER ASP TYR ILE ILE GLY ALA ASP THR VAL MET
SEQRES 12 A 215 ASN GLU SER GLU ASP LEU PHE SER LEU ILE GLU THR HIS
SEQRES 13 A 215 GLU ALA LYS PRO LEU LYS LEU TYR VAL TYR ASN THR ASP
SEQRES 14 A 215 THR ASP ASN CYS ARG GLU VAL ILE ILE THR PRO ASN SER
SEQRES 15 A 215 ALA TRP GLY GLY GLU GLY SER LEU GLY CYS GLY ILE GLY
SEQRES 16 A 215 TYR GLY TYR LEU HIS ARG ILE PRO THR ARG PRO PHE GLU
SEQRES 17 A 215 GLU GLY LYS LYS ILE SER LEU
SEQRES 1 B 215 MET GLY SER SER GLN SER VAL GLU ILE PRO GLY GLY GLY
SEQRES 2 B 215 THR GLU GLY TYR HIS VAL LEU ARG VAL GLN GLU ASN SER
SEQRES 3 B 215 PRO GLY HIS ARG ALA GLY LEU GLU PRO PHE PHE ASP PHE
SEQRES 4 B 215 ILE VAL SER ILE ASN GLY SER ARG LEU ASN LYS ASP ASN
SEQRES 5 B 215 ASP THR LEU LYS ASP LEU LEU LYS ALA ASN VAL GLU LYS
SEQRES 6 B 215 PRO VAL LYS MET LEU ILE TYR SER SER LYS THR LEU GLU
SEQRES 7 B 215 LEU ARG GLU ALA SER VAL THR PRO SER ASN LEU TRP GLY
SEQRES 8 B 215 GLY GLN GLY LEU LEU GLY VAL SER ILE ARG PHE CYS SER
SEQRES 9 B 215 PHE ASP GLY ALA ASN GLU ASN VAL TRP HIS VAL LEU GLU
SEQRES 10 B 215 VAL GLU SER ASN SER PRO ALA ALA LEU ALA GLY LEU ARG
SEQRES 11 B 215 PRO HIS SER ASP TYR ILE ILE GLY ALA ASP THR VAL MET
SEQRES 12 B 215 ASN GLU SER GLU ASP LEU PHE SER LEU ILE GLU THR HIS
SEQRES 13 B 215 GLU ALA LYS PRO LEU LYS LEU TYR VAL TYR ASN THR ASP
SEQRES 14 B 215 THR ASP ASN CYS ARG GLU VAL ILE ILE THR PRO ASN SER
SEQRES 15 B 215 ALA TRP GLY GLY GLU GLY SER LEU GLY CYS GLY ILE GLY
SEQRES 16 B 215 TYR GLY TYR LEU HIS ARG ILE PRO THR ARG PRO PHE GLU
SEQRES 17 B 215 GLU GLY LYS LYS ILE SER LEU
FORMUL 3 HOH *91(H2 O)
HELIX 1 1 SER A 26 ALA A 31 1 6
HELIX 2 2 ASP A 53 ASN A 62 1 10
HELIX 3 3 SER A 122 GLY A 128 1 7
HELIX 4 4 ASP A 148 HIS A 156 1 9
HELIX 5 5 GLY B 28 GLY B 32 5 5
HELIX 6 6 ASP B 53 ASN B 62 1 10
HELIX 7 7 GLY B 107 ASN B 111 5 5
HELIX 8 8 SER B 122 GLY B 128 1 7
HELIX 9 9 ASP B 148 HIS B 156 1 9
SHEET 1 A 4 SER A 46 ARG A 47 0
SHEET 2 A 4 ASP A 38 ILE A 43 -1 N ILE A 43 O SER A 46
SHEET 3 A 4 VAL A 67 SER A 73 -1 O LEU A 70 N SER A 42
SHEET 4 A 4 LEU A 79 VAL A 84 -1 O VAL A 84 N VAL A 67
SHEET 1 B 4 SER A 46 ARG A 47 0
SHEET 2 B 4 ASP A 38 ILE A 43 -1 N ILE A 43 O SER A 46
SHEET 3 B 4 GLU A 15 VAL A 22 -1 N VAL A 19 O ASP A 38
SHEET 4 B 4 VAL A 98 SER A 104 -1 O SER A 99 N LEU A 20
SHEET 1 C10 ASN A 172 ILE A 178 0
SHEET 2 C10 LEU A 161 ASN A 167 -1 N LEU A 163 O VAL A 176
SHEET 3 C10 ASP A 134 ASP A 140 -1 N TYR A 135 O TYR A 166
SHEET 4 C10 TRP A 113 VAL A 118 -1 N TRP A 113 O ILE A 136
SHEET 5 C10 CYS A 192 GLY A 197 -1 O GLY A 195 N HIS A 114
SHEET 6 C10 CYS B 192 GLY B 197 -1 O ILE B 194 N TYR A 196
SHEET 7 C10 TRP B 113 VAL B 118 -1 N HIS B 114 O GLY B 195
SHEET 8 C10 ASP B 134 ALA B 139 -1 O ILE B 136 N TRP B 113
SHEET 9 C10 LEU B 161 ASN B 167 -1 O TYR B 166 N TYR B 135
SHEET 10 C10 CYS B 173 ILE B 178 -1 O VAL B 176 N LEU B 163
SHEET 1 D 4 SER B 46 ARG B 47 0
SHEET 2 D 4 ASP B 38 ILE B 43 -1 N ILE B 43 O SER B 46
SHEET 3 D 4 VAL B 67 SER B 73 -1 O LEU B 70 N VAL B 41
SHEET 4 D 4 LEU B 79 VAL B 84 -1 O VAL B 84 N VAL B 67
SHEET 1 E 4 SER B 46 ARG B 47 0
SHEET 2 E 4 ASP B 38 ILE B 43 -1 N ILE B 43 O SER B 46
SHEET 3 E 4 GLU B 15 HIS B 18 -1 N TYR B 17 O ILE B 40
SHEET 4 E 4 PHE B 102 SER B 104 -1 O CYS B 103 N GLY B 16
SHEET 1 F 2 ARG B 21 VAL B 22 0
SHEET 2 F 2 VAL B 98 SER B 99 -1 O SER B 99 N ARG B 21
CISPEP 1 ARG A 205 PRO A 206 0 -1.68
CISPEP 2 PHE B 207 GLU B 208 0 -5.40
CRYST1 83.077 83.077 145.153 90.00 90.00 90.00 P 43 21 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 0.012037 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012037 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006889 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
