HEADER VIRAL PROTEIN 07-JAN-16 5HFM
TITLE GP41-TARGETING HIV-1 FUSION INHIBITORS WITH HOOK-LIKE ILE-ASP-LEU TAIL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP160,GP41 CHR REGION;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: UNP RESIDUES 539-581;
COMPND 5 SYNONYM: ENV POLYPROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_COMMON: HIV-1;
SOURCE 4 ORGANISM_TAXID: 11676;
SOURCE 5 STRAIN: ISOLATE LW123;
SOURCE 6 GENE: ENV;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HIV-1 FUSION INHIBITOR, ILE-ASP-LEU TAIL, HOOK-LIKE TAIL, VIRAL
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHU,S.YE,R.ZHANG
REVDAT 2 20-MAR-24 5HFM 1 REMARK
REVDAT 1 11-JAN-17 5HFM 0
JRNL AUTH Y.ZHU,S.SU,L.QIN,Q.WANG,L.SHI,Z.MA,J.TANG,S.JIANG,L.LU,S.YE,
JRNL AUTH 2 R.ZHANG
JRNL TITL RATIONAL IMPROVEMENT OF GP41-TARGETING HIV-1 FUSION
JRNL TITL 2 INHIBITORS: AN INNOVATIVELY DESIGNED ILE-ASP-LEU TAIL WITH
JRNL TITL 3 ALTERNATIVE CONFORMATIONS
JRNL REF SCI REP V. 6 31983 2016
JRNL REFN ESSN 2045-2322
JRNL PMID 27666394
JRNL DOI 10.1038/SREP31983
REMARK 2
REMARK 2 RESOLUTION. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 18969
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 969
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 33.8541 - 4.3929 0.88 2461 133 0.1754 0.1937
REMARK 3 2 4.3929 - 3.4879 0.95 2630 155 0.1635 0.2228
REMARK 3 3 3.4879 - 3.0473 0.96 2683 147 0.2111 0.2497
REMARK 3 4 3.0473 - 2.7689 0.95 2657 151 0.2337 0.2709
REMARK 3 5 2.7689 - 2.5705 0.94 2649 137 0.2539 0.3631
REMARK 3 6 2.5705 - 2.4190 0.92 2569 135 0.2580 0.3438
REMARK 3 7 2.4190 - 2.2979 0.84 2351 111 0.2728 0.3802
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) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.880
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 : 0.003 3832
REMARK 3 ANGLE : 0.497 5134
REMARK 3 CHIRALITY : 0.032 566
REMARK 3 PLANARITY : 0.001 656
REMARK 3 DIHEDRAL : 18.175 1496
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 5HFM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000216818.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-AUG-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.2
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18969
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.298
REMARK 200 RESOLUTION RANGE LOW (A) : 33.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 200 DATA REDUNDANCY : 1.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M SODIUM POTASSIUM PHOSPHATE, PH
REMARK 280 8.2, VAPOR DIFFUSION, TEMPERATURE 289K
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
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, 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 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 GLY A 535
REMARK 465 PRO A 536
REMARK 465 MET A 537
REMARK 465 LEU A 581
REMARK 465 SER A 622
REMARK 465 GLY B 535
REMARK 465 PRO B 536
REMARK 465 MET B 537
REMARK 465 LEU B 581
REMARK 465 SER B 622
REMARK 465 GLY B 623
REMARK 465 GLY B 624
REMARK 465 GLY C 535
REMARK 465 PRO C 536
REMARK 465 MET C 537
REMARK 465 LEU C 581
REMARK 465 SER C 622
REMARK 465 GLY D 535
REMARK 465 PRO D 536
REMARK 465 MET D 537
REMARK 465 LEU D 581
REMARK 465 SER D 622
REMARK 465 GLY E 535
REMARK 465 PRO E 536
REMARK 465 MET E 537
REMARK 465 LEU E 581
REMARK 465 SER E 622
REMARK 465 GLY F 535
REMARK 465 PRO F 536
REMARK 465 MET F 537
REMARK 465 LEU F 581
REMARK 465 SER F 622
REMARK 465 GLY F 623
REMARK 465 GLY F 624
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 636 CD OE1 OE2
REMARK 480 GLN A 653 CD OE1 NE2
REMARK 480 GLU B 636 CD OE1 OE2
REMARK 480 GLN B 653 CD OE1 NE2
REMARK 480 GLU C 636 CD OE1 OE2
REMARK 480 GLN C 653 CD OE1 NE2
REMARK 480 GLU D 636 CD OE1 OE2
REMARK 480 GLU E 636 CD OE1 OE2
REMARK 480 GLN E 653 CD OE1 NE2
REMARK 480 ARG F 542 CZ NH1 NH2
REMARK 480 GLU F 636 CD OE1 OE2
REMARK 480 GLN F 653 CD OE1 NE2
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 GLN F 653 O HOH F 801 1.92
REMARK 500 O HOH A 722 O HOH F 817 2.02
REMARK 500 OE1 GLN C 563 O HOH C 701 2.04
REMARK 500 O HOH E 704 O HOH E 721 2.10
REMARK 500 OH TYR C 638 O HOH C 702 2.12
REMARK 500 OE1 GLN F 567 O HOH F 802 2.14
REMARK 500 OE1 GLN A 562 O HOH A 701 2.14
REMARK 500 OH TYR E 638 O HOH E 701 2.15
REMARK 500 OE2 GLU A 643 O HOH A 702 2.16
REMARK 500 OE1 GLU F 643 O HOH F 803 2.17
REMARK 500 OE1 GLN F 562 O HOH F 804 2.18
REMARK 500 OE1 GLU E 630 O HOH E 702 2.19
REMARK 500 OE1 GLU C 630 O HOH C 703 2.19
REMARK 500 O HOH C 711 O HOH C 722 2.19
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 ARG D 625 -3.67 62.71
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 TAM B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TAM F 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5HFL RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE 622-627 IS FUSION LINKER, AND RESIDUE 654-656 IS ARTIFICIAL
REMARK 999 TAIL.
DBREF 5HFM A 539 581 UNP Q70626 ENV_HV1LW 539 581
DBREF 5HFM A 622 656 PDB 5HFM 5HFM 622 656
DBREF 5HFM B 539 581 UNP Q70626 ENV_HV1LW 539 581
DBREF 5HFM B 622 656 PDB 5HFM 5HFM 622 656
DBREF 5HFM C 539 581 UNP Q70626 ENV_HV1LW 539 581
DBREF 5HFM C 622 656 PDB 5HFM 5HFM 622 656
DBREF 5HFM D 539 581 UNP Q70626 ENV_HV1LW 539 581
DBREF 5HFM D 622 656 PDB 5HFM 5HFM 622 656
DBREF 5HFM E 539 581 UNP Q70626 ENV_HV1LW 539 581
DBREF 5HFM E 622 656 PDB 5HFM 5HFM 622 656
DBREF 5HFM F 539 581 UNP Q70626 ENV_HV1LW 539 581
DBREF 5HFM F 622 656 PDB 5HFM 5HFM 622 656
SEQADV 5HFM GLY A 535 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM PRO A 536 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM MET A 537 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM ALA A 538 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM GLY B 535 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM PRO B 536 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM MET B 537 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM ALA B 538 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM GLY C 535 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM PRO C 536 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM MET C 537 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM ALA C 538 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM GLY D 535 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM PRO D 536 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM MET D 537 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM ALA D 538 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM GLY E 535 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM PRO E 536 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM MET E 537 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM ALA E 538 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM GLY F 535 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM PRO F 536 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM MET F 537 UNP Q70626 EXPRESSION TAG
SEQADV 5HFM ALA F 538 UNP Q70626 EXPRESSION TAG
SEQRES 1 A 82 GLY PRO MET ALA VAL GLN ALA ARG GLN LEU LEU SER GLY
SEQRES 2 A 82 ILE VAL GLN GLN GLN ASN ASN LEU LEU ARG ALA ILE GLU
SEQRES 3 A 82 ALA GLN GLN HIS LEU LEU GLN LEU THR VAL TRP GLY ILE
SEQRES 4 A 82 LYS GLN LEU GLN ALA ARG ILE LEU SER GLY GLY ARG GLY
SEQRES 5 A 82 GLY TRP GLU GLU TRP ASP LYS LYS ILE GLU GLU TYR THR
SEQRES 6 A 82 LYS LYS ILE GLU GLU LEU ILE LYS LYS SER GLN ASN GLN
SEQRES 7 A 82 GLN ILE ASP LEU
SEQRES 1 B 82 GLY PRO MET ALA VAL GLN ALA ARG GLN LEU LEU SER GLY
SEQRES 2 B 82 ILE VAL GLN GLN GLN ASN ASN LEU LEU ARG ALA ILE GLU
SEQRES 3 B 82 ALA GLN GLN HIS LEU LEU GLN LEU THR VAL TRP GLY ILE
SEQRES 4 B 82 LYS GLN LEU GLN ALA ARG ILE LEU SER GLY GLY ARG GLY
SEQRES 5 B 82 GLY TRP GLU GLU TRP ASP LYS LYS ILE GLU GLU TYR THR
SEQRES 6 B 82 LYS LYS ILE GLU GLU LEU ILE LYS LYS SER GLN ASN GLN
SEQRES 7 B 82 GLN ILE ASP LEU
SEQRES 1 C 82 GLY PRO MET ALA VAL GLN ALA ARG GLN LEU LEU SER GLY
SEQRES 2 C 82 ILE VAL GLN GLN GLN ASN ASN LEU LEU ARG ALA ILE GLU
SEQRES 3 C 82 ALA GLN GLN HIS LEU LEU GLN LEU THR VAL TRP GLY ILE
SEQRES 4 C 82 LYS GLN LEU GLN ALA ARG ILE LEU SER GLY GLY ARG GLY
SEQRES 5 C 82 GLY TRP GLU GLU TRP ASP LYS LYS ILE GLU GLU TYR THR
SEQRES 6 C 82 LYS LYS ILE GLU GLU LEU ILE LYS LYS SER GLN ASN GLN
SEQRES 7 C 82 GLN ILE ASP LEU
SEQRES 1 D 82 GLY PRO MET ALA VAL GLN ALA ARG GLN LEU LEU SER GLY
SEQRES 2 D 82 ILE VAL GLN GLN GLN ASN ASN LEU LEU ARG ALA ILE GLU
SEQRES 3 D 82 ALA GLN GLN HIS LEU LEU GLN LEU THR VAL TRP GLY ILE
SEQRES 4 D 82 LYS GLN LEU GLN ALA ARG ILE LEU SER GLY GLY ARG GLY
SEQRES 5 D 82 GLY TRP GLU GLU TRP ASP LYS LYS ILE GLU GLU TYR THR
SEQRES 6 D 82 LYS LYS ILE GLU GLU LEU ILE LYS LYS SER GLN ASN GLN
SEQRES 7 D 82 GLN ILE ASP LEU
SEQRES 1 E 82 GLY PRO MET ALA VAL GLN ALA ARG GLN LEU LEU SER GLY
SEQRES 2 E 82 ILE VAL GLN GLN GLN ASN ASN LEU LEU ARG ALA ILE GLU
SEQRES 3 E 82 ALA GLN GLN HIS LEU LEU GLN LEU THR VAL TRP GLY ILE
SEQRES 4 E 82 LYS GLN LEU GLN ALA ARG ILE LEU SER GLY GLY ARG GLY
SEQRES 5 E 82 GLY TRP GLU GLU TRP ASP LYS LYS ILE GLU GLU TYR THR
SEQRES 6 E 82 LYS LYS ILE GLU GLU LEU ILE LYS LYS SER GLN ASN GLN
SEQRES 7 E 82 GLN ILE ASP LEU
SEQRES 1 F 82 GLY PRO MET ALA VAL GLN ALA ARG GLN LEU LEU SER GLY
SEQRES 2 F 82 ILE VAL GLN GLN GLN ASN ASN LEU LEU ARG ALA ILE GLU
SEQRES 3 F 82 ALA GLN GLN HIS LEU LEU GLN LEU THR VAL TRP GLY ILE
SEQRES 4 F 82 LYS GLN LEU GLN ALA ARG ILE LEU SER GLY GLY ARG GLY
SEQRES 5 F 82 GLY TRP GLU GLU TRP ASP LYS LYS ILE GLU GLU TYR THR
SEQRES 6 F 82 LYS LYS ILE GLU GLU LEU ILE LYS LYS SER GLN ASN GLN
SEQRES 7 F 82 GLN ILE ASP LEU
HET TAM B 701 11
HET TAM F 701 11
HETNAM TAM TRIS(HYDROXYETHYL)AMINOMETHANE
FORMUL 7 TAM 2(C7 H17 N O3)
FORMUL 9 HOH *142(H2 O)
HELIX 1 AA1 ALA A 538 ALA A 578 1 41
HELIX 2 AA2 TRP A 628 GLN A 653 1 26
HELIX 3 AA3 VAL B 539 ARG B 579 1 41
HELIX 4 AA4 TRP B 628 GLN B 653 1 26
HELIX 5 AA5 VAL C 539 ARG C 579 1 41
HELIX 6 AA6 TRP C 628 GLN C 653 1 26
HELIX 7 AA7 VAL D 539 ILE D 580 1 42
HELIX 8 AA8 TRP D 628 GLN D 653 1 26
HELIX 9 AA9 VAL E 539 ILE E 580 1 42
HELIX 10 AB1 TRP E 628 GLN E 653 1 26
HELIX 11 AB2 VAL F 539 ARG F 579 1 41
HELIX 12 AB3 TRP F 628 GLN F 653 1 26
SITE 1 AC1 2 TYR B 638 HOH B 811
SITE 1 AC2 2 LYS F 634 TYR F 638
CRYST1 39.112 39.076 90.602 90.03 89.98 120.06 P 1 6
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 0.025568 0.014799 0.000000 0.00000
SCALE2 0.000000 0.029569 0.000016 0.00000
SCALE3 0.000000 0.000000 0.011037 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
