HEADER PEPTIDE BINDING PROTEIN/PROTEIN BINDING 16-APR-13 4K76
TITLE CFTR ASSOCIATED LIGAND (CAL) PDZ DOMAIN BOUND TO PEPTIDE ICAL36-TRL
TITLE 2 (ANSRWPTTRL)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GOLGI-ASSOCIATED PDZ AND COILED-COIL MOTIF-CONTAINING
COMPND 3 PROTEIN;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 FRAGMENT: PDZ DOMAIN;
COMPND 6 SYNONYM: CFTR-ASSOCIATED LIGAND, FUSED IN GLIOBLASTOMA, PDZ PROTEIN
COMPND 7 INTERACTING SPECIFICALLY WITH TC10, PIST;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: ICAL36-TRL PEPTIDE;
COMPND 11 CHAIN: E, F, G, H;
COMPND 12 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: GOPC, CAL, FIG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET16B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES
KEYWDS PDZ DOMAIN, CAL, PIST, FIG, PDZ-PEPTIDE COMPLEX, CFTR ASSOCIATED
KEYWDS 2 LIGAND, CFTR, PEPTIDE BINDING PROTEIN-PROTEIN BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.F.AMACHER,D.R.MADDEN
REVDAT 2 20-SEP-23 4K76 1 REMARK
REVDAT 1 26-FEB-14 4K76 0
JRNL AUTH J.F.AMACHER,P.R.CUSHING,L.BROOKS,P.BOISGUERIN,D.R.MADDEN
JRNL TITL STEREOCHEMICAL PREFERENCES MODULATE AFFINITY AND SELECTIVITY
JRNL TITL 2 AMONG FIVE PDZ DOMAINS THAT BIND CFTR: COMPARATIVE
JRNL TITL 3 STRUCTURAL AND SEQUENCE ANALYSES.
JRNL REF STRUCTURE V. 22 82 2014
JRNL REFN ISSN 0969-2126
JRNL PMID 24210758
JRNL DOI 10.1016/J.STR.2013.09.019
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 30585
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 1493
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 19.2631 - 3.8824 0.97 2658 156 0.1708 0.2085
REMARK 3 2 3.8824 - 3.0857 0.96 2662 127 0.1569 0.1980
REMARK 3 3 3.0857 - 2.6968 0.96 2658 137 0.1647 0.2199
REMARK 3 4 2.6968 - 2.4508 0.96 2673 129 0.1879 0.2162
REMARK 3 5 2.4508 - 2.2754 0.96 2619 144 0.1848 0.2510
REMARK 3 6 2.2754 - 2.1415 0.96 2664 132 0.1640 0.2206
REMARK 3 7 2.1415 - 2.0343 0.96 2643 130 0.1626 0.2200
REMARK 3 8 2.0343 - 1.9459 0.95 2648 134 0.1676 0.2057
REMARK 3 9 1.9459 - 1.8710 0.94 2612 136 0.1771 0.2380
REMARK 3 10 1.8710 - 1.8065 0.96 2632 125 0.2015 0.2728
REMARK 3 11 1.8065 - 1.7500 0.94 2623 143 0.2163 0.2715
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.38
REMARK 3 K_SOL : 0.44
REMARK 3 B_SOL : 40.53
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.820
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) : -1.20320
REMARK 3 B22 (A**2) : -1.07380
REMARK 3 B33 (A**2) : 2.27700
REMARK 3 B12 (A**2) : 1.53670
REMARK 3 B13 (A**2) : -2.21050
REMARK 3 B23 (A**2) : 1.48750
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 : 0.006 2985
REMARK 3 ANGLE : 1.066 4037
REMARK 3 CHIRALITY : 0.066 466
REMARK 3 PLANARITY : 0.005 525
REMARK 3 DIHEDRAL : 14.718 1122
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 284:370
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5485 13.5526 20.2438
REMARK 3 T TENSOR
REMARK 3 T11: 0.0375 T22: 0.0694
REMARK 3 T33: 0.0713 T12: -0.0118
REMARK 3 T13: 0.0081 T23: 0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.0893 L22: 0.6303
REMARK 3 L33: 0.8467 L12: 0.0122
REMARK 3 L13: -0.2934 L23: 0.0447
REMARK 3 S TENSOR
REMARK 3 S11: -0.0149 S12: -0.0541 S13: 0.0507
REMARK 3 S21: 0.0189 S22: -0.0269 S23: 0.0550
REMARK 3 S31: -0.0230 S32: -0.0234 S33: 0.0116
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B AND RESID 284:370
REMARK 3 ORIGIN FOR THE GROUP (A): 17.0678 32.6254 0.8823
REMARK 3 T TENSOR
REMARK 3 T11: 0.0562 T22: 0.0878
REMARK 3 T33: 0.0679 T12: 0.0091
REMARK 3 T13: -0.0052 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 0.2955 L22: 0.2177
REMARK 3 L33: 0.1853 L12: 0.0778
REMARK 3 L13: -0.0958 L23: 0.1661
REMARK 3 S TENSOR
REMARK 3 S11: 0.0378 S12: 0.1434 S13: -0.0351
REMARK 3 S21: -0.0204 S22: -0.0215 S23: 0.0441
REMARK 3 S31: 0.0310 S32: -0.0477 S33: -0.0093
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C AND RESID 284:370
REMARK 3 ORIGIN FOR THE GROUP (A): 34.3949 7.3351 -4.1271
REMARK 3 T TENSOR
REMARK 3 T11: 0.0793 T22: 0.0998
REMARK 3 T33: 0.0687 T12: 0.0238
REMARK 3 T13: 0.0174 T23: 0.0251
REMARK 3 L TENSOR
REMARK 3 L11: 0.3491 L22: 0.0769
REMARK 3 L33: 0.6090 L12: -0.0333
REMARK 3 L13: 0.1312 L23: -0.1362
REMARK 3 S TENSOR
REMARK 3 S11: -0.0064 S12: -0.0145 S13: -0.0719
REMARK 3 S21: -0.0133 S22: 0.0324 S23: 0.0202
REMARK 3 S31: -0.1282 S32: 0.0512 S33: -0.0071
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D AND RESID 284:370
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9312 40.2742 23.8198
REMARK 3 T TENSOR
REMARK 3 T11: 0.0106 T22: -0.1464
REMARK 3 T33: -0.0087 T12: -0.0997
REMARK 3 T13: 0.0354 T23: 0.0983
REMARK 3 L TENSOR
REMARK 3 L11: 0.1738 L22: 0.5523
REMARK 3 L33: 0.4201 L12: -0.1589
REMARK 3 L13: -0.0138 L23: -0.4239
REMARK 3 S TENSOR
REMARK 3 S11: -0.2164 S12: 0.1282 S13: 0.0034
REMARK 3 S21: 0.3861 S22: 0.0385 S23: -0.3442
REMARK 3 S31: -0.4179 S32: -0.3820 S33: 0.0331
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 4K76 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078976.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8856
REMARK 200 MONOCHROMATOR : S1 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30591
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 19.262
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.950
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 32.4000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.950
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 4E34 (CAL PDZ BOUND TO ICAL36 PEPTIDE)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 APPLY THE FOLLOWING TO CHAINS: A, E
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H
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 ALA E 1
REMARK 465 ASN E 2
REMARK 465 ALA F 1
REMARK 465 ALA G 1
REMARK 465 ASN G 2
REMARK 465 SER G 3
REMARK 465 ALA H 1
REMARK 465 ASN H 2
REMARK 465 SER H 3
REMARK 465 ARG H 4
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 D 308 7.56 -65.88
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 GOL F 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4K6Y RELATED DB: PDB
REMARK 900 RELATED ID: 4K72 RELATED DB: PDB
REMARK 900 RELATED ID: 4K75 RELATED DB: PDB
REMARK 900 RELATED ID: 4K78 RELATED DB: PDB
REMARK 900 RELATED ID: 4JOP RELATED DB: PDB
REMARK 900 RELATED ID: 4JOR RELATED DB: PDB
DBREF 4K76 A 284 370 UNP Q9HD26 GOPC_HUMAN 284 370
DBREF 4K76 B 284 370 UNP Q9HD26 GOPC_HUMAN 284 370
DBREF 4K76 C 284 370 UNP Q9HD26 GOPC_HUMAN 284 370
DBREF 4K76 D 284 370 UNP Q9HD26 GOPC_HUMAN 284 370
DBREF 4K76 E 1 10 PDB 4K76 4K76 1 10
DBREF 4K76 F 1 10 PDB 4K76 4K76 1 10
DBREF 4K76 G 1 10 PDB 4K76 4K76 1 10
DBREF 4K76 H 1 10 PDB 4K76 4K76 1 10
SEQRES 1 A 87 GLY PRO ILE ARG LYS VAL LEU LEU LEU LYS GLU ASP HIS
SEQRES 2 A 87 GLU GLY LEU GLY ILE SER ILE THR GLY GLY LYS GLU HIS
SEQRES 3 A 87 GLY VAL PRO ILE LEU ILE SER GLU ILE HIS PRO GLY GLN
SEQRES 4 A 87 PRO ALA ASP ARG CYS GLY GLY LEU HIS VAL GLY ASP ALA
SEQRES 5 A 87 ILE LEU ALA VAL ASN GLY VAL ASN LEU ARG ASP THR LYS
SEQRES 6 A 87 HIS LYS GLU ALA VAL THR ILE LEU SER GLN GLN ARG GLY
SEQRES 7 A 87 GLU ILE GLU PHE GLU VAL VAL TYR VAL
SEQRES 1 B 87 GLY PRO ILE ARG LYS VAL LEU LEU LEU LYS GLU ASP HIS
SEQRES 2 B 87 GLU GLY LEU GLY ILE SER ILE THR GLY GLY LYS GLU HIS
SEQRES 3 B 87 GLY VAL PRO ILE LEU ILE SER GLU ILE HIS PRO GLY GLN
SEQRES 4 B 87 PRO ALA ASP ARG CYS GLY GLY LEU HIS VAL GLY ASP ALA
SEQRES 5 B 87 ILE LEU ALA VAL ASN GLY VAL ASN LEU ARG ASP THR LYS
SEQRES 6 B 87 HIS LYS GLU ALA VAL THR ILE LEU SER GLN GLN ARG GLY
SEQRES 7 B 87 GLU ILE GLU PHE GLU VAL VAL TYR VAL
SEQRES 1 C 87 GLY PRO ILE ARG LYS VAL LEU LEU LEU LYS GLU ASP HIS
SEQRES 2 C 87 GLU GLY LEU GLY ILE SER ILE THR GLY GLY LYS GLU HIS
SEQRES 3 C 87 GLY VAL PRO ILE LEU ILE SER GLU ILE HIS PRO GLY GLN
SEQRES 4 C 87 PRO ALA ASP ARG CYS GLY GLY LEU HIS VAL GLY ASP ALA
SEQRES 5 C 87 ILE LEU ALA VAL ASN GLY VAL ASN LEU ARG ASP THR LYS
SEQRES 6 C 87 HIS LYS GLU ALA VAL THR ILE LEU SER GLN GLN ARG GLY
SEQRES 7 C 87 GLU ILE GLU PHE GLU VAL VAL TYR VAL
SEQRES 1 D 87 GLY PRO ILE ARG LYS VAL LEU LEU LEU LYS GLU ASP HIS
SEQRES 2 D 87 GLU GLY LEU GLY ILE SER ILE THR GLY GLY LYS GLU HIS
SEQRES 3 D 87 GLY VAL PRO ILE LEU ILE SER GLU ILE HIS PRO GLY GLN
SEQRES 4 D 87 PRO ALA ASP ARG CYS GLY GLY LEU HIS VAL GLY ASP ALA
SEQRES 5 D 87 ILE LEU ALA VAL ASN GLY VAL ASN LEU ARG ASP THR LYS
SEQRES 6 D 87 HIS LYS GLU ALA VAL THR ILE LEU SER GLN GLN ARG GLY
SEQRES 7 D 87 GLU ILE GLU PHE GLU VAL VAL TYR VAL
SEQRES 1 E 10 ALA ASN SER ARG TRP PRO THR THR ARG LEU
SEQRES 1 F 10 ALA ASN SER ARG TRP PRO THR THR ARG LEU
SEQRES 1 G 10 ALA ASN SER ARG TRP PRO THR THR ARG LEU
SEQRES 1 H 10 ALA ASN SER ARG TRP PRO THR THR ARG LEU
HET GOL F 101 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 GOL C3 H8 O3
FORMUL 10 HOH *267(H2 O)
HELIX 1 1 LYS A 307 GLY A 310 5 4
HELIX 2 2 GLN A 322 GLY A 328 1 7
HELIX 3 3 LYS A 348 GLN A 359 1 12
HELIX 4 4 LYS B 307 GLY B 310 5 4
HELIX 5 5 LYS B 348 GLN B 358 1 11
HELIX 6 6 LYS C 307 GLY C 310 5 4
HELIX 7 7 LYS C 348 GLN C 358 1 11
HELIX 8 8 LYS D 307 GLY D 310 5 4
HELIX 9 9 GLN D 322 GLY D 328 1 7
HELIX 10 10 LYS D 348 GLN D 358 1 11
SHEET 1 A 4 ILE A 286 LYS A 293 0
SHEET 2 A 4 GLY A 361 VAL A 368 -1 O ILE A 363 N LEU A 291
SHEET 3 A 4 ALA A 335 VAL A 339 -1 N ALA A 335 O VAL A 368
SHEET 4 A 4 VAL A 342 ASN A 343 -1 O VAL A 342 N VAL A 339
SHEET 1 B 3 VAL A 311 ILE A 318 0
SHEET 2 B 3 ILE A 301 GLY A 306 -1 N SER A 302 O SER A 316
SHEET 3 B 3 THR E 7 LEU E 10 -1 O LEU E 10 N ILE A 301
SHEET 1 C 4 ILE B 286 LYS B 293 0
SHEET 2 C 4 GLY B 361 VAL B 368 -1 O VAL B 367 N ARG B 287
SHEET 3 C 4 ALA B 335 VAL B 339 -1 N ALA B 338 O GLU B 366
SHEET 4 C 4 VAL B 342 ASN B 343 -1 O VAL B 342 N VAL B 339
SHEET 1 D 3 VAL B 311 ILE B 318 0
SHEET 2 D 3 ILE B 301 GLY B 306 -1 N THR B 304 O LEU B 314
SHEET 3 D 3 THR F 7 ARG F 9 -1 O THR F 8 N ILE B 303
SHEET 1 E 4 ARG C 287 LEU C 292 0
SHEET 2 E 4 GLU C 362 TYR C 369 -1 O VAL C 367 N ARG C 287
SHEET 3 E 4 ASP C 334 VAL C 339 -1 N ALA C 335 O VAL C 368
SHEET 4 E 4 VAL C 342 ASN C 343 -1 O VAL C 342 N VAL C 339
SHEET 1 F 3 VAL C 311 ILE C 318 0
SHEET 2 F 3 ILE C 301 GLY C 306 -1 N THR C 304 O LEU C 314
SHEET 3 F 3 THR G 8 LEU G 10 -1 O LEU G 10 N ILE C 301
SHEET 1 G 4 ARG D 287 LEU D 292 0
SHEET 2 G 4 GLU D 362 TYR D 369 -1 O VAL D 367 N ARG D 287
SHEET 3 G 4 ASP D 334 VAL D 339 -1 N ALA D 335 O VAL D 368
SHEET 4 G 4 VAL D 342 ASN D 343 -1 O VAL D 342 N VAL D 339
SHEET 1 H 3 VAL D 311 ILE D 318 0
SHEET 2 H 3 ILE D 301 GLY D 306 -1 N THR D 304 O LEU D 314
SHEET 3 H 3 THR H 7 LEU H 10 -1 O LEU H 10 N ILE D 301
SSBOND 1 CYS A 327 CYS C 327 1555 1555 2.03
SSBOND 2 CYS B 327 CYS D 327 1555 1555 2.04
SITE 1 AC1 5 ILE B 315 GLY B 333 SER F 3 ARG F 4
SITE 2 AC1 5 HOH F 206
CRYST1 32.762 50.169 55.183 68.81 75.79 87.93 P 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 0.030523 -0.001102 -0.007866 0.00000
SCALE2 0.000000 0.019945 -0.007793 0.00000
SCALE3 0.000000 0.000000 0.020069 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
