HEADER MEMBRANE PROTEIN/INHIBITOR 13-NOV-12 3W19
TITLE POTENT HIV FUSION INHIBITOR CP32M-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSMEMBRANE PROTEIN GP41;
COMPND 3 CHAIN: C;
COMPND 4 FRAGMENT: N-PEPTIDE T21, UNP RESIDIES 552-589;
COMPND 5 SYNONYM: TM, GLYCOPROTEIN 41, GLYCOPROTEIN 120, GP120;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: FUSION INHIBITOR CP32M-2;
COMPND 9 CHAIN: D;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1;
SOURCE 4 ORGANISM_COMMON: HIV-1;
SOURCE 5 ORGANISM_TAXID: 11676;
SOURCE 6 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HIV-1 VIRUS;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 OTHER_DETAILS: THIS SEQUENCE DOES NOT OCCUR NATURALLY IN HIV-1, BUT
SOURCE 10 DESIGNED BASED ON SEQUENCE OF HIV-1 GP41 CHR AND ITS PARENTAL
SOURCE 11 PEPTIDE CP32M
KEYWDS 6-HELIX-BUNDLE, MT-HOOK, INHIBIT HIV MEMBRANE FUSION, MEMBRANE
KEYWDS 2 PROTEIN-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR X.YAO,S.WALTERSPERGER,M.T.WANG,S.CUI
REVDAT 2 08-NOV-23 3W19 1 SEQADV LINK
REVDAT 1 11-DEC-13 3W19 0
JRNL AUTH X.YAO,S.WALTERSPERGER,M.T.WANG,S.CUI
JRNL TITL OPTIMIZATION OF NOVEL ANTI-HIV FUSION INHIBITOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
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) : 1.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.14
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.460
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 21146
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.172
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1059
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 36.1582 - 2.5560 0.99 2664 141 0.1838 0.1794
REMARK 3 2 2.5560 - 2.0288 1.00 2527 133 0.1318 0.1435
REMARK 3 3 2.0288 - 1.7723 1.00 2538 133 0.1333 0.1953
REMARK 3 4 1.7723 - 1.6103 1.00 2500 132 0.1108 0.1460
REMARK 3 5 1.6103 - 1.4949 0.99 2486 131 0.1118 0.1371
REMARK 3 6 1.4949 - 1.4067 0.99 2473 131 0.1401 0.1806
REMARK 3 7 1.4067 - 1.3363 1.00 2473 130 0.1751 0.2373
REMARK 3 8 1.3363 - 1.2781 0.98 2426 128 0.2039 0.2619
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 44.51
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.640
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.93200
REMARK 3 B22 (A**2) : 0.93200
REMARK 3 B33 (A**2) : -1.86410
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 : 0.005 649
REMARK 3 ANGLE : 0.794 886
REMARK 3 CHIRALITY : 0.046 95
REMARK 3 PLANARITY : 0.003 112
REMARK 3 DIHEDRAL : 14.320 260
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 3W19 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-NOV-12.
REMARK 100 THE DEPOSITION ID IS D_1000095758.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.82656
REMARK 200 MONOCHROMATOR : BARTELS MONOCHROMATOR CRYSTAL
REMARK 200 TYPE SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS PACKAGE
REMARK 200 DATA SCALING SOFTWARE : XDS PACKAGE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21170
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.278
REMARK 200 RESOLUTION RANGE LOW (A) : 36.144
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.02600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.9200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.28
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.45900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.490
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER FOR MR
REMARK 200 STARTING MODEL: PDB ID 3VGX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.1 M HEPES,
REMARK 280 16%(W/V) PEG 4000, 10%(W/V) ISOPROPANOL, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 22.24400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 12.84258
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 69.58033
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 22.24400
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 12.84258
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 69.58033
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 22.24400
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 12.84258
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 69.58033
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 22.24400
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 12.84258
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 69.58033
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 22.24400
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 12.84258
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 69.58033
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 22.24400
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 12.84258
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 69.58033
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 25.68516
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 139.16067
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 25.68516
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 139.16067
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 25.68516
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 139.16067
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 25.68516
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 139.16067
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 25.68516
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 139.16067
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 25.68516
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 139.16067
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 -22.24400
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 38.52774
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -44.48800
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
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 C 601 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 613 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 646 LIES ON A SPECIAL POSITION.
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 OE1 GLU D 636 O HOH D 709 2.14
REMARK 500 OE2 GLU D 636 O HOH D 706 2.15
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 CHAIN D OF FUSION INHIBITOR
REMARK 800 CP32M-2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VH7 RELATED DB: PDB
REMARK 900 RELATED ID: 3VGY RELATED DB: PDB
REMARK 900 RELATED ID: 3VGX RELATED DB: PDB
DBREF 3W19 C 553 590 UNP P03375 ENV_HV1B1 553 590
DBREF 3W19 D 623 651 PDB 3W19 3W19 623 651
SEQADV 3W19 ACE C 552 UNP P03375 ACETYLATION
SEQADV 3W19 NH2 C 591 UNP P03375 AMIDATION
SEQRES 1 C 40 ACE ASN ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN HIS
SEQRES 2 C 40 LEU LEU GLN LEU THR VAL TRP GLY ILE LYS GLN LEU GLN
SEQRES 3 C 40 ALA ARG ILE LEU ALA VAL GLU ARG TYR LEU LYS ASP GLN
SEQRES 4 C 40 NH2
SEQRES 1 D 29 TRP ASN GLU MET THR TRP MET GLU TRP GLU ARG GLU ILE
SEQRES 2 D 29 GLU ASN TYR THR LYS LEU ILE TYR LYS ILE LEU GLU GLU
SEQRES 3 D 29 SER GLN GLU
HET ACE C 552 3
HET NH2 C 591 1
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
FORMUL 1 ACE C2 H4 O
FORMUL 1 NH2 H2 N
FORMUL 3 HOH *75(H2 O)
HELIX 1 1 ASN C 553 GLN C 590 1 38
HELIX 2 2 THR D 627 GLU D 651 1 25
LINK C ACE C 552 N ASN C 553 1555 1555 1.33
LINK C GLN C 590 N NH2 C 591 1555 1555 1.33
SITE 1 AC1 37 ASN C 553 ASN C 554 LEU C 556 ARG C 557
SITE 2 AC1 37 ALA C 561 GLN C 562 GLN C 563 HIS C 564
SITE 3 AC1 37 LEU C 565 GLN C 567 LEU C 568 TRP C 571
SITE 4 AC1 37 GLY C 572 ILE C 573 LYS C 574 GLN C 575
SITE 5 AC1 37 GLN C 577 ARG C 579 ASP C 589 GLN C 590
SITE 6 AC1 37 HOH C 641 HOH C 656 HOH C 657 HOH D 701
SITE 7 AC1 37 HOH D 702 HOH D 703 HOH D 704 HOH D 705
SITE 8 AC1 37 HOH D 706 HOH D 707 HOH D 708 HOH D 709
SITE 9 AC1 37 HOH D 710 HOH D 711 HOH D 713 HOH D 715
SITE 10 AC1 37 HOH D 717
CRYST1 44.488 44.488 208.741 90.00 90.00 120.00 H 3 2 18
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 0.022478 0.012978 0.000000 0.00000
SCALE2 0.000000 0.025955 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004791 0.00000
HETATM 1 C ACE C 552 -18.745 16.899 -10.342 1.00 39.51 C
ANISOU 1 C ACE C 552 5840 5947 3226 958 -1983 418 C
HETATM 2 O ACE C 552 -18.624 16.410 -9.214 1.00 32.10 O
ANISOU 2 O ACE C 552 6495 3909 1793 -218 -588 163 O
HETATM 3 CH3 ACE C 552 -19.689 16.276 -11.366 1.00 48.03 C
ANISOU 3 CH3 ACE C 552 7205 7431 3612 275 -815 -207 C
(ATOM LINES ARE NOT SHOWN.)
END
