HEADER RAN BINDING PROTEIN/PEPTIDE 22-APR-16 5JIU
TITLE THE CRYSTAL STRUCTURE OF RANBPM/9 IUS-SPRY DOMAIN IN COMPLEX WITH DDX-
TITLE 2 4 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAN-BINDING PROTEIN 9;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 108-350;
COMPND 5 SYNONYM: RANBP9,BPM-L,BPM90,RAN-BINDING PROTEIN M,RANBPM,RANBP7;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROBABLE ATP-DEPENDENT RNA HELICASE DDX4;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: UNP RESIDUES 201-220;
COMPND 11 SYNONYM: DEAD BOX PROTEIN 4,MVH,VASA HOMOLOG;
COMPND 12 EC: 3.6.4.13;
COMPND 13 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: RANBP9, RANBPM;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 14 ORGANISM_COMMON: MOUSE;
SOURCE 15 ORGANISM_TAXID: 10090
KEYWDS BETA SANDWICH, RAN BINDING PROTEIN, TRANSPORT PROTEIN, RAN BINDING
KEYWDS 2 PROTEIN-PEPTIDE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.K.HONG,K.-H.KIM,E.E.KIM
REVDAT 2 08-NOV-23 5JIU 1 JRNL REMARK
REVDAT 1 09-NOV-16 5JIU 0
JRNL AUTH S.K.HONG,K.H.KIM,E.J.SONG,E.E.KIM
JRNL TITL STRUCTURAL BASIS FOR THE INTERACTION BETWEEN THE IUS-SPRY
JRNL TITL 2 DOMAIN OF RANBPM AND DDX-4 IN GERM CELL DEVELOPMENT.
JRNL REF J.MOL.BIOL. V. 428 4330 2016
JRNL REFN ESSN 1089-8638
JRNL PMID 27622290
JRNL DOI 10.1016/J.JMB.2016.09.004
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.540
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 41717
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820
REMARK 3 FREE R VALUE TEST SET COUNT : 2011
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 32.0619 - 4.9451 0.98 2932 151 0.1346 0.1654
REMARK 3 2 4.9451 - 3.9273 0.97 2851 144 0.1215 0.1355
REMARK 3 3 3.9273 - 3.4315 0.99 2921 150 0.1488 0.1869
REMARK 3 4 3.4315 - 3.1181 0.99 2898 140 0.1719 0.2183
REMARK 3 5 3.1181 - 2.8947 0.99 2884 146 0.1802 0.1993
REMARK 3 6 2.8947 - 2.7242 0.99 2909 145 0.1908 0.2580
REMARK 3 7 2.7242 - 2.5878 0.99 2861 147 0.1873 0.2333
REMARK 3 8 2.5878 - 2.4752 0.98 2845 142 0.1939 0.2912
REMARK 3 9 2.4752 - 2.3799 0.97 2835 140 0.1960 0.2263
REMARK 3 10 2.3799 - 2.2978 0.96 2769 137 0.1996 0.2581
REMARK 3 11 2.2978 - 2.2260 0.96 2820 147 0.2015 0.2635
REMARK 3 12 2.2260 - 2.1624 0.96 2799 150 0.2176 0.2546
REMARK 3 13 2.1624 - 2.1055 0.94 2749 135 0.2428 0.2672
REMARK 3 14 2.1055 - 2.0541 0.92 2633 137 0.2681 0.2779
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.200
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 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 3480
REMARK 3 ANGLE : 1.068 4720
REMARK 3 CHIRALITY : 0.043 480
REMARK 3 PLANARITY : 0.006 628
REMARK 3 DIHEDRAL : 14.175 1276
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 5JIU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220655.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42894
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.2658
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: PHASER
REMARK 200 STARTING MODEL: 5JI7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20~25% (W/V) PEG 3350, 0.1 M BIS-TRIS,
REMARK 280 PH 6.5, 0.2 M NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
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,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 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 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 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 61.65900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 61.65900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 45.99300
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 61.65900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 61.65900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 45.99300
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 61.65900
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 61.65900
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 45.99300
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 61.65900
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 61.65900
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 45.99300
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 LEU A 108
REMARK 465 ALA A 109
REMARK 465 ALA A 110
REMARK 465 GLY A 111
REMARK 465 PRO A 112
REMARK 465 GLY A 113
REMARK 465 PRO A 114
REMARK 465 ALA A 115
REMARK 465 GLY A 116
REMARK 465 GLY A 117
REMARK 465 ALA A 118
REMARK 465 PRO A 119
REMARK 465 THR A 120
REMARK 465 PRO A 121
REMARK 465 ALA A 122
REMARK 465 LEU A 123
REMARK 465 VAL A 124
REMARK 465 ALA A 125
REMARK 465 GLY A 126
REMARK 465 SER A 127
REMARK 465 SER A 128
REMARK 465 ALA A 129
REMARK 465 ALA A 130
REMARK 465 ALA A 131
REMARK 465 PRO A 132
REMARK 465 PHE A 133
REMARK 465 PRO A 134
REMARK 465 HIS A 135
REMARK 465 GLY A 136
REMARK 465 ASP A 137
REMARK 465 SER A 138
REMARK 465 ALA A 139
REMARK 465 LEU A 140
REMARK 465 GLN A 350
REMARK 465 LEU B 108
REMARK 465 ALA B 109
REMARK 465 ALA B 110
REMARK 465 GLY B 111
REMARK 465 PRO B 112
REMARK 465 GLY B 113
REMARK 465 PRO B 114
REMARK 465 ALA B 115
REMARK 465 GLY B 116
REMARK 465 GLY B 117
REMARK 465 ALA B 118
REMARK 465 PRO B 119
REMARK 465 THR B 120
REMARK 465 PRO B 121
REMARK 465 ALA B 122
REMARK 465 LEU B 123
REMARK 465 VAL B 124
REMARK 465 ALA B 125
REMARK 465 GLY B 126
REMARK 465 SER B 127
REMARK 465 SER B 128
REMARK 465 ALA B 129
REMARK 465 ALA B 130
REMARK 465 ALA B 131
REMARK 465 PRO B 132
REMARK 465 PHE B 133
REMARK 465 PRO B 134
REMARK 465 HIS B 135
REMARK 465 GLY B 136
REMARK 465 ASP B 137
REMARK 465 SER B 138
REMARK 465 ALA B 139
REMARK 465 LEU B 140
REMARK 465 GLN B 350
REMARK 465 LYS C 494
REMARK 465 SER C 495
REMARK 465 GLU C 496
REMARK 465 THR C 497
REMARK 465 GLU C 498
REMARK 465 GLY C 499
REMARK 465 GLY C 500
REMARK 465 GLY C 507
REMARK 465 PRO C 508
REMARK 465 LYS C 509
REMARK 465 VAL C 510
REMARK 465 THR C 511
REMARK 465 TYR C 512
REMARK 465 ILE C 513
REMARK 465 LYS D 494
REMARK 465 SER D 495
REMARK 465 GLU D 496
REMARK 465 THR D 497
REMARK 465 GLU D 498
REMARK 465 GLY D 499
REMARK 465 GLY D 500
REMARK 465 GLY D 507
REMARK 465 PRO D 508
REMARK 465 LYS D 509
REMARK 465 VAL D 510
REMARK 465 THR D 511
REMARK 465 TYR D 512
REMARK 465 ILE D 513
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 581 O HOH B 583 2.18
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 LYS A 194 36.24 -142.07
REMARK 500 ASN A 242 42.34 -82.44
REMARK 500 TYR A 271 -57.68 -140.65
REMARK 500 ASN B 242 38.29 -87.02
REMARK 500 TYR B 271 -57.24 -138.17
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 CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JI7 RELATED DB: PDB
REMARK 900 RELATED ID: 5JI9 RELATED DB: PDB
REMARK 900 RELATED ID: 5JIA RELATED DB: PDB
DBREF 5JIU A 108 350 UNP Q96S59 RANB9_HUMAN 108 350
DBREF 5JIU B 108 350 UNP Q96S59 RANB9_HUMAN 108 350
DBREF 5JIU C 494 513 UNP Q61496 DDX4_MOUSE 201 220
DBREF 5JIU D 494 513 UNP Q61496 DDX4_MOUSE 201 220
SEQRES 1 A 243 LEU ALA ALA GLY PRO GLY PRO ALA GLY GLY ALA PRO THR
SEQRES 2 A 243 PRO ALA LEU VAL ALA GLY SER SER ALA ALA ALA PRO PHE
SEQRES 3 A 243 PRO HIS GLY ASP SER ALA LEU ASN GLU GLN GLU LYS GLU
SEQRES 4 A 243 LEU GLN ARG ARG LEU LYS ARG LEU TYR PRO ALA VAL ASP
SEQRES 5 A 243 GLU GLN GLU THR PRO LEU PRO ARG SER TRP SER PRO LYS
SEQRES 6 A 243 ASP LYS PHE SER TYR ILE GLY LEU SER GLN ASN ASN LEU
SEQRES 7 A 243 ARG VAL HIS TYR LYS GLY HIS GLY LYS THR PRO LYS ASP
SEQRES 8 A 243 ALA ALA SER VAL ARG ALA THR HIS PRO ILE PRO ALA ALA
SEQRES 9 A 243 CYS GLY ILE TYR TYR PHE GLU VAL LYS ILE VAL SER LYS
SEQRES 10 A 243 GLY ARG ASP GLY TYR MET GLY ILE GLY LEU SER ALA GLN
SEQRES 11 A 243 GLY VAL ASN MET ASN ARG LEU PRO GLY TRP ASP LYS HIS
SEQRES 12 A 243 SER TYR GLY TYR HIS GLY ASP ASP GLY HIS SER PHE CYS
SEQRES 13 A 243 SER SER GLY THR GLY GLN PRO TYR GLY PRO THR PHE THR
SEQRES 14 A 243 THR GLY ASP VAL ILE GLY CYS CYS VAL ASN LEU ILE ASN
SEQRES 15 A 243 ASN THR CYS PHE TYR THR LYS ASN GLY HIS SER LEU GLY
SEQRES 16 A 243 ILE ALA PHE THR ASP LEU PRO PRO ASN LEU TYR PRO THR
SEQRES 17 A 243 VAL GLY LEU GLN THR PRO GLY GLU VAL VAL ASP ALA ASN
SEQRES 18 A 243 PHE GLY GLN HIS PRO PHE VAL PHE ASP ILE GLU ASP TYR
SEQRES 19 A 243 MET ARG GLU TRP ARG THR LYS ILE GLN
SEQRES 1 B 243 LEU ALA ALA GLY PRO GLY PRO ALA GLY GLY ALA PRO THR
SEQRES 2 B 243 PRO ALA LEU VAL ALA GLY SER SER ALA ALA ALA PRO PHE
SEQRES 3 B 243 PRO HIS GLY ASP SER ALA LEU ASN GLU GLN GLU LYS GLU
SEQRES 4 B 243 LEU GLN ARG ARG LEU LYS ARG LEU TYR PRO ALA VAL ASP
SEQRES 5 B 243 GLU GLN GLU THR PRO LEU PRO ARG SER TRP SER PRO LYS
SEQRES 6 B 243 ASP LYS PHE SER TYR ILE GLY LEU SER GLN ASN ASN LEU
SEQRES 7 B 243 ARG VAL HIS TYR LYS GLY HIS GLY LYS THR PRO LYS ASP
SEQRES 8 B 243 ALA ALA SER VAL ARG ALA THR HIS PRO ILE PRO ALA ALA
SEQRES 9 B 243 CYS GLY ILE TYR TYR PHE GLU VAL LYS ILE VAL SER LYS
SEQRES 10 B 243 GLY ARG ASP GLY TYR MET GLY ILE GLY LEU SER ALA GLN
SEQRES 11 B 243 GLY VAL ASN MET ASN ARG LEU PRO GLY TRP ASP LYS HIS
SEQRES 12 B 243 SER TYR GLY TYR HIS GLY ASP ASP GLY HIS SER PHE CYS
SEQRES 13 B 243 SER SER GLY THR GLY GLN PRO TYR GLY PRO THR PHE THR
SEQRES 14 B 243 THR GLY ASP VAL ILE GLY CYS CYS VAL ASN LEU ILE ASN
SEQRES 15 B 243 ASN THR CYS PHE TYR THR LYS ASN GLY HIS SER LEU GLY
SEQRES 16 B 243 ILE ALA PHE THR ASP LEU PRO PRO ASN LEU TYR PRO THR
SEQRES 17 B 243 VAL GLY LEU GLN THR PRO GLY GLU VAL VAL ASP ALA ASN
SEQRES 18 B 243 PHE GLY GLN HIS PRO PHE VAL PHE ASP ILE GLU ASP TYR
SEQRES 19 B 243 MET ARG GLU TRP ARG THR LYS ILE GLN
SEQRES 1 C 20 LYS SER GLU THR GLU GLY GLY GLU SER SER ASP SER GLN
SEQRES 2 C 20 GLY PRO LYS VAL THR TYR ILE
SEQRES 1 D 20 LYS SER GLU THR GLU GLY GLY GLU SER SER ASP SER GLN
SEQRES 2 D 20 GLY PRO LYS VAL THR TYR ILE
HET CL A 401 1
HET CL B 401 1
HETNAM CL CHLORIDE ION
FORMUL 5 CL 2(CL 1-)
FORMUL 7 HOH *276(H2 O)
HELIX 1 AA1 ASN A 141 TYR A 155 1 15
HELIX 2 AA2 PRO A 209 CYS A 212 5 4
HELIX 3 AA3 ASP A 337 ILE A 349 1 13
HELIX 4 AA4 GLU B 142 TYR B 155 1 14
HELIX 5 AA5 PRO B 209 CYS B 212 5 4
HELIX 6 AA6 ASP B 337 ILE B 349 1 13
SHEET 1 AA1 7 TRP A 169 LYS A 174 0
SHEET 2 AA1 7 ALA A 200 ALA A 204 -1 O ARG A 203 N SER A 170
SHEET 3 AA1 7 TYR A 313 LEU A 318 -1 O LEU A 318 N ALA A 200
SHEET 4 AA1 7 GLY A 231 SER A 235 -1 N GLY A 231 O GLY A 317
SHEET 5 AA1 7 SER A 251 HIS A 255 -1 O TYR A 252 N LEU A 234
SHEET 6 AA1 7 HIS A 260 CYS A 263 -1 O PHE A 262 N GLY A 253
SHEET 7 AA1 7 GLN A 269 PRO A 270 -1 O GLN A 269 N SER A 261
SHEET 1 AA2 7 ILE A 178 SER A 181 0
SHEET 2 AA2 7 ARG A 186 TYR A 189 -1 O HIS A 188 N GLY A 179
SHEET 3 AA2 7 GLU A 323 ASN A 328 -1 O VAL A 325 N VAL A 187
SHEET 4 AA2 7 ILE A 214 LYS A 224 -1 N GLU A 218 O ASN A 328
SHEET 5 AA2 7 VAL A 280 ASN A 286 -1 O VAL A 285 N TYR A 215
SHEET 6 AA2 7 THR A 291 LYS A 296 -1 O PHE A 293 N CYS A 284
SHEET 7 AA2 7 HIS A 299 PHE A 305 -1 O ALA A 304 N CYS A 292
SHEET 1 AA3 7 TRP B 169 LYS B 174 0
SHEET 2 AA3 7 ALA B 200 ALA B 204 -1 O ARG B 203 N SER B 170
SHEET 3 AA3 7 TYR B 313 LEU B 318 -1 O LEU B 318 N ALA B 200
SHEET 4 AA3 7 GLY B 231 SER B 235 -1 N SER B 235 O TYR B 313
SHEET 5 AA3 7 SER B 251 HIS B 255 -1 O TYR B 252 N LEU B 234
SHEET 6 AA3 7 HIS B 260 CYS B 263 -1 O PHE B 262 N GLY B 253
SHEET 7 AA3 7 GLN B 269 PRO B 270 -1 O GLN B 269 N SER B 261
SHEET 1 AA4 7 ILE B 178 SER B 181 0
SHEET 2 AA4 7 ARG B 186 TYR B 189 -1 O ARG B 186 N SER B 181
SHEET 3 AA4 7 GLU B 323 ASN B 328 -1 O VAL B 325 N VAL B 187
SHEET 4 AA4 7 ILE B 214 LYS B 224 -1 N GLU B 218 O ASN B 328
SHEET 5 AA4 7 VAL B 280 ASN B 286 -1 O ILE B 281 N VAL B 219
SHEET 6 AA4 7 THR B 291 LYS B 296 -1 O PHE B 293 N CYS B 284
SHEET 7 AA4 7 HIS B 299 PHE B 305 -1 O ALA B 304 N CYS B 292
SITE 1 AC1 4 ARG A 150 ARG A 153 HOH A 563 HOH A 595
SITE 1 AC2 4 ARG B 150 ARG B 153 HOH B 583 HOH B 590
CRYST1 123.318 123.318 91.986 90.00 90.00 90.00 I 4 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 0.008109 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008109 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010871 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
