HEADER IMMUNE SYSTEM 23-MAR-10 3MAC
TITLE CRYSTAL STRUCTURE OF GP41-DERIVED PROTEIN COMPLEXED WITH FAB 8062
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSMEMBRANE GLYCOPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: FAB8062;
COMPND 7 CHAIN: H;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: FAB8062;
COMPND 11 CHAIN: L;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_TAXID: 9606
KEYWDS GP41, FAB8062, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR M.LI,E.GUSTCHINA,J.LOUIS,A.GUSTCHINA,A.WLODAWER,M.CLORE
REVDAT 3 06-SEP-23 3MAC 1 REMARK
REVDAT 2 08-NOV-17 3MAC 1 REMARK
REVDAT 1 08-DEC-10 3MAC 0
JRNL AUTH E.GUSTCHINA,M.LI,J.M.LOUIS,D.E.ANDERSON,J.LLOYD,C.FRISCH,
JRNL AUTH 2 C.A.BEWLEY,A.GUSTCHINA,A.WLODAWER,G.M.CLORE
JRNL TITL STRUCTURAL BASIS OF HIV-1 NEUTRALIZATION BY AFFINITY MATURED
JRNL TITL 2 FABS DIRECTED AGAINST THE INTERNAL TRIMERIC COILED-COIL OF
JRNL TITL 3 GP41.
JRNL REF PLOS PATHOG. V. 6 01182 2010
JRNL REFN ISSN 1553-7366
JRNL PMID 21085615
JRNL DOI 10.1371/JOURNAL.PPAT.1001182
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0104
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 22917
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100
REMARK 3 FREE R VALUE TEST SET COUNT : 728
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1525
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE SET COUNT : 46
REMARK 3 BIN FREE R VALUE : 0.3690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4798
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 69
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.40000
REMARK 3 B22 (A**2) : -0.25000
REMARK 3 B33 (A**2) : -1.41000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.58000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.602
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.310
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.224
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.692
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4900 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6669 ; 1.190 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 615 ; 6.003 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 215 ;34.243 ;25.628
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 808 ;18.280 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;15.336 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 754 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3697 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3085 ; 1.405 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4977 ; 2.390 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1815 ; 1.801 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1691 ; 2.649 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 104
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6812 36.2614 34.4561
REMARK 3 T TENSOR
REMARK 3 T11: 0.2516 T22: 0.1249
REMARK 3 T33: 0.1245 T12: 0.0390
REMARK 3 T13: -0.0260 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 4.2947 L22: 3.8639
REMARK 3 L33: 5.4160 L12: -0.4064
REMARK 3 L13: 0.5216 L23: 0.8604
REMARK 3 S TENSOR
REMARK 3 S11: -0.0278 S12: -0.0713 S13: 0.3297
REMARK 3 S21: -0.1937 S22: 0.1238 S23: 0.2948
REMARK 3 S31: -0.9098 S32: -0.3249 S33: -0.0960
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 105 L 211
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9124 36.5450 70.8141
REMARK 3 T TENSOR
REMARK 3 T11: 0.1448 T22: 0.0500
REMARK 3 T33: 0.0658 T12: 0.0171
REMARK 3 T13: 0.0124 T23: -0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 4.0079 L22: 2.3309
REMARK 3 L33: 6.2157 L12: -1.0293
REMARK 3 L13: 1.2602 L23: -1.0144
REMARK 3 S TENSOR
REMARK 3 S11: 0.1585 S12: 0.0471 S13: 0.2019
REMARK 3 S21: 0.0078 S22: -0.2314 S23: -0.0666
REMARK 3 S31: -0.3555 S32: 0.0611 S33: 0.0729
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 106
REMARK 3 ORIGIN FOR THE GROUP (A): 25.5479 21.4864 34.1875
REMARK 3 T TENSOR
REMARK 3 T11: 0.1098 T22: 0.2976
REMARK 3 T33: 0.0882 T12: -0.0331
REMARK 3 T13: -0.0113 T23: -0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 1.3435 L22: 0.6147
REMARK 3 L33: 5.1749 L12: -0.8005
REMARK 3 L13: 1.1526 L23: 0.0587
REMARK 3 S TENSOR
REMARK 3 S11: -0.0801 S12: -0.0021 S13: -0.0418
REMARK 3 S21: 0.0266 S22: 0.1202 S23: 0.0380
REMARK 3 S31: -0.0720 S32: 0.6667 S33: -0.0401
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 107 H 224
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4920 20.3317 68.2636
REMARK 3 T TENSOR
REMARK 3 T11: 0.2122 T22: 0.1776
REMARK 3 T33: 0.1329 T12: 0.0466
REMARK 3 T13: 0.0243 T23: -0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 0.1318 L22: 0.5389
REMARK 3 L33: 4.9281 L12: 0.2055
REMARK 3 L13: -0.2551 L23: -0.0341
REMARK 3 S TENSOR
REMARK 3 S11: 0.0054 S12: 0.0525 S13: -0.0286
REMARK 3 S21: 0.1463 S22: -0.0267 S23: -0.0079
REMARK 3 S31: 0.3567 S32: 0.2286 S33: 0.0213
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 217
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7953 23.4187 5.4005
REMARK 3 T TENSOR
REMARK 3 T11: 0.1978 T22: 0.0406
REMARK 3 T33: 0.1670 T12: 0.0189
REMARK 3 T13: 0.0200 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 3.5117 L22: 1.3195
REMARK 3 L33: 2.2161 L12: 0.4345
REMARK 3 L13: 0.9915 L23: 0.1118
REMARK 3 S TENSOR
REMARK 3 S11: -0.0624 S12: 0.0280 S13: 0.0657
REMARK 3 S21: -0.0302 S22: 0.0084 S23: -0.0044
REMARK 3 S31: -0.0413 S32: 0.2772 S33: 0.0540
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3MAC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058307.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARCCD300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23655
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 29.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.52400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: PDB ENTRY 2CMR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% POLYETHYLENE GLYCOL 10K, 0.1M
REMARK 280 AMMONIUM SULFATE, 5% ETHYLENE GLYCOL, PH 8.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 20.87050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L
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 42
REMARK 465 GLY A 43
REMARK 465 SER A 44
REMARK 465 GLY A 45
REMARK 465 GLY A 46
REMARK 465 HIS A 47
REMARK 465 SER A 86
REMARK 465 SER A 87
REMARK 465 GLY A 88
REMARK 465 LEU A 128
REMARK 465 ALA A 129
REMARK 465 GLY A 130
REMARK 465 GLY A 131
REMARK 465 SER A 132
REMARK 465 GLY A 133
REMARK 465 GLY A 134
REMARK 465 HIS A 135
REMARK 465 THR A 136
REMARK 465 GLY A 173
REMARK 465 SER A 174
REMARK 465 SER A 175
REMARK 465 GLY A 176
REMARK 465 ALA A 217
REMARK 465 GLN H 1
REMARK 465 VAL H 2
REMARK 465 LYS H 136
REMARK 465 SER H 137
REMARK 465 THR H 138
REMARK 465 SER H 139
REMARK 465 GLY H 140
REMARK 465 GLU H 225
REMARK 465 GLN H 226
REMARK 465 LYS H 227
REMARK 465 LEU H 228
REMARK 465 ILE H 229
REMARK 465 SER H 230
REMARK 465 GLU H 231
REMARK 465 GLU H 232
REMARK 465 ASP H 233
REMARK 465 LEU H 234
REMARK 465 ASN H 235
REMARK 465 GLY H 236
REMARK 465 ALA H 237
REMARK 465 PRO H 238
REMARK 465 HIS H 239
REMARK 465 HIS H 240
REMARK 465 HIS H 241
REMARK 465 HIS H 242
REMARK 465 HIS H 243
REMARK 465 HIS H 244
REMARK 465 ASP L 1
REMARK 465 GLU L 212
REMARK 465 ALA L 213
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLY A 85 CA C O
REMARK 470 VAL H 57 CG1 CG2
REMARK 470 GLN H 199 CB CG 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 OG1 THR L 94 O HOH L 218 2.17
REMARK 500 OE1 GLU A 169 O HOH A 228 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU H 185 CA - CB - CG ANGL. DEV. = 15.9 DEGREES
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 ALA A 125 34.14 -91.11
REMARK 500 ALA A 213 5.41 -67.71
REMARK 500 GLU H 223 45.13 -92.56
REMARK 500 ASP L 25 -74.48 -70.05
REMARK 500 PRO L 39 123.14 -38.76
REMARK 500 THR L 77 130.83 -39.25
REMARK 500 ALA L 83 -177.87 -176.41
REMARK 500 VAL L 95 45.14 38.47
REMARK 500 SER L 154 -8.19 75.68
REMARK 500 GLN L 169 -94.44 -67.48
REMARK 500 SER L 170 -55.89 -154.87
REMARK 500 ASN L 172 36.31 -87.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MA9 RELATED DB: PDB
DBREF 3MAC A 1 217 UNP D0VWW0 D0VWW0_9HIV1 1 217
DBREF 3MAC H 1 244 PDB 3MAC 3MAC 1 244
DBREF 3MAC L 1 213 PDB 3MAC 3MAC 1 213
SEQRES 1 A 217 MET GLN LEU LEU SER GLY ILE VAL GLN GLN GLN ASN ASN
SEQRES 2 A 217 LEU LEU ARG ALA ILE GLU ALA GLN GLN HIS LEU LEU GLN
SEQRES 3 A 217 LEU THR VAL TRP GLY ILE LYS GLN LEU GLN ALA ARG ILE
SEQRES 4 A 217 LEU ALA GLY GLY SER GLY GLY HIS THR THR TRP MET GLU
SEQRES 5 A 217 TRP ASP ARG GLU ILE ASN ASN TYR THR SER LEU ILE HIS
SEQRES 6 A 217 SER LEU ILE GLU GLU SER GLN ASN GLN GLN GLU LYS ASN
SEQRES 7 A 217 GLU GLN GLU LEU LEU GLU GLY SER SER GLY GLY GLN LEU
SEQRES 8 A 217 LEU SER GLY ILE VAL GLN GLN GLN ASN ASN LEU LEU ARG
SEQRES 9 A 217 ALA ILE GLU ALA GLN GLN HIS LEU LEU GLN LEU THR VAL
SEQRES 10 A 217 TRP GLY ILE LYS GLN LEU GLN ALA ARG ILE LEU ALA GLY
SEQRES 11 A 217 GLY SER GLY GLY HIS THR THR TRP MET GLU TRP ASP ARG
SEQRES 12 A 217 GLU ILE ASN ASN TYR THR SER LEU ILE HIS SER LEU ILE
SEQRES 13 A 217 GLU GLU SER GLN ASN GLN GLN GLU LYS ASN GLU GLN GLU
SEQRES 14 A 217 LEU LEU GLU GLY SER SER GLY GLY GLN LEU LEU SER GLY
SEQRES 15 A 217 ILE VAL GLN GLN GLN ASN ASN LEU LEU ARG ALA ILE GLU
SEQRES 16 A 217 ALA GLN GLN HIS LEU LEU GLN LEU THR VAL TRP GLY ILE
SEQRES 17 A 217 LYS GLN LEU GLN ALA ARG ILE LEU ALA
SEQRES 1 H 245 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 H 245 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY
SEQRES 3 H 245 GLY THR PHE ASN SER TYR ALA PHE SER TRP VAL ARG GLN
SEQRES 4 H 245 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY SER ILE ILE
SEQRES 5 H 245 PRO LEU PHE GLY PHE VAL VAL TYR ALA GLN LYS PHE GLN
SEQRES 6 H 245 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR
SEQRES 7 H 245 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 H 245 ALA VAL TYR TYR CYS ALA ARG TYR PHE ASP THR TYR ASN
SEQRES 9 H 245 ASN TYR GLY PHE ALA ASN TRP GLY GLN GLY THR LEU VAL
SEQRES 10 H 245 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE
SEQRES 11 H 245 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR
SEQRES 12 H 245 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU
SEQRES 13 H 245 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER
SEQRES 14 H 245 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY
SEQRES 15 H 245 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER
SEQRES 16 H 245 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS
SEQRES 17 H 245 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO
SEQRES 18 H 245 LYS SER GLU PHE GLU GLN LYS LEU ILE SER GLU GLU ASP
SEQRES 19 H 245 LEU ASN GLY ALA PRO HIS HIS HIS HIS HIS HIS
SEQRES 1 L 213 ASP ILE GLU LEU THR GLN PRO PRO SER VAL SER VAL VAL
SEQRES 2 L 213 PRO GLY GLN THR ALA ARG ILE SER CYS SER GLY ASP ASN
SEQRES 3 L 213 ILE PRO TYR GLU TYR ALA SER TRP TYR GLN GLN LYS PRO
SEQRES 4 L 213 GLY GLN ALA PRO VAL LEU VAL ILE TYR GLY ASP ASN ASN
SEQRES 5 L 213 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN
SEQRES 6 L 213 SER GLY ASN THR ALA THR LEU THR ILE SER GLY THR GLN
SEQRES 7 L 213 ALA GLU ASP GLU ALA ASP TYR TYR CYS ALA SER TRP ASP
SEQRES 8 L 213 SER MET THR VAL ASP GLY VAL PHE GLY GLY GLY THR LYS
SEQRES 9 L 213 LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL
SEQRES 10 L 213 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN
SEQRES 11 L 213 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO
SEQRES 12 L 213 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO
SEQRES 13 L 213 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN
SEQRES 14 L 213 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU
SEQRES 15 L 213 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS
SEQRES 16 L 213 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL
SEQRES 17 L 213 ALA PRO THR GLU ALA
FORMUL 4 HOH *69(H2 O)
HELIX 1 1 MET A 1 LEU A 40 1 40
HELIX 2 2 THR A 48 GLU A 84 1 37
HELIX 3 3 GLY A 89 ALA A 125 1 37
HELIX 4 4 THR A 137 GLU A 172 1 36
HELIX 5 5 GLY A 177 ALA A 213 1 37
HELIX 6 6 THR H 28 TYR H 32 5 5
HELIX 7 7 GLN H 61 GLN H 64 5 4
HELIX 8 8 ARG H 86 THR H 90 5 5
HELIX 9 9 SER H 194 LEU H 196 5 3
HELIX 10 10 LYS H 208 ASN H 211 5 4
HELIX 11 11 GLN L 78 GLU L 82 5 5
HELIX 12 12 SER L 123 ALA L 129 1 7
HELIX 13 13 THR L 183 SER L 189 1 7
SHEET 1 A 4 LEU H 4 GLN H 6 0
SHEET 2 A 4 VAL H 18 ALA H 24 -1 O LYS H 23 N VAL H 5
SHEET 3 A 4 THR H 77 LEU H 82 -1 O MET H 80 N VAL H 20
SHEET 4 A 4 VAL H 67 ASP H 72 -1 N THR H 70 O TYR H 79
SHEET 1 B 6 GLU H 10 LYS H 12 0
SHEET 2 B 6 THR H 114 VAL H 118 1 O THR H 117 N LYS H 12
SHEET 3 B 6 ALA H 91 TYR H 98 -1 N ALA H 91 O VAL H 116
SHEET 4 B 6 ALA H 33 GLN H 39 -1 N VAL H 37 O TYR H 94
SHEET 5 B 6 LEU H 45 ILE H 51 -1 O MET H 48 N TRP H 36
SHEET 6 B 6 VAL H 57 TYR H 59 -1 O VAL H 58 N SER H 50
SHEET 1 C 4 GLU H 10 LYS H 12 0
SHEET 2 C 4 THR H 114 VAL H 118 1 O THR H 117 N LYS H 12
SHEET 3 C 4 ALA H 91 TYR H 98 -1 N ALA H 91 O VAL H 116
SHEET 4 C 4 ASN H 109 TRP H 110 -1 O ASN H 109 N ARG H 97
SHEET 1 D 4 SER H 127 LEU H 131 0
SHEET 2 D 4 THR H 142 TYR H 152 -1 O LEU H 148 N PHE H 129
SHEET 3 D 4 TYR H 183 PRO H 192 -1 O LEU H 185 N VAL H 149
SHEET 4 D 4 VAL H 170 THR H 172 -1 N HIS H 171 O VAL H 188
SHEET 1 E 4 SER H 127 LEU H 131 0
SHEET 2 E 4 THR H 142 TYR H 152 -1 O LEU H 148 N PHE H 129
SHEET 3 E 4 TYR H 183 PRO H 192 -1 O LEU H 185 N VAL H 149
SHEET 4 E 4 VAL H 176 LEU H 177 -1 N VAL H 176 O SER H 184
SHEET 1 F 3 THR H 158 TRP H 161 0
SHEET 2 F 3 ILE H 202 HIS H 207 -1 O ASN H 206 N THR H 158
SHEET 3 F 3 THR H 212 LYS H 217 -1 O VAL H 214 N VAL H 205
SHEET 1 G 5 SER L 9 VAL L 12 0
SHEET 2 G 5 THR L 103 VAL L 107 1 O THR L 106 N VAL L 10
SHEET 3 G 5 ALA L 83 TRP L 90 -1 N ALA L 83 O LEU L 105
SHEET 4 G 5 SER L 33 GLN L 37 -1 N GLN L 37 O ASP L 84
SHEET 5 G 5 VAL L 44 ILE L 47 -1 O VAL L 46 N TRP L 34
SHEET 1 H 4 SER L 9 VAL L 12 0
SHEET 2 H 4 THR L 103 VAL L 107 1 O THR L 106 N VAL L 10
SHEET 3 H 4 ALA L 83 TRP L 90 -1 N ALA L 83 O LEU L 105
SHEET 4 H 4 GLY L 97 PHE L 99 -1 O VAL L 98 N SER L 89
SHEET 1 I 3 ALA L 18 SER L 23 0
SHEET 2 I 3 THR L 69 ILE L 74 -1 O LEU L 72 N ILE L 20
SHEET 3 I 3 PHE L 61 ASN L 65 -1 N SER L 62 O THR L 73
SHEET 1 J 4 SER L 116 PHE L 120 0
SHEET 2 J 4 ALA L 132 PHE L 141 -1 O SER L 139 N SER L 116
SHEET 3 J 4 TYR L 174 LEU L 182 -1 O LEU L 182 N ALA L 132
SHEET 4 J 4 VAL L 161 THR L 163 -1 N GLU L 162 O TYR L 179
SHEET 1 K 4 SER L 116 PHE L 120 0
SHEET 2 K 4 ALA L 132 PHE L 141 -1 O SER L 139 N SER L 116
SHEET 3 K 4 TYR L 174 LEU L 182 -1 O LEU L 182 N ALA L 132
SHEET 4 K 4 SER L 167 LYS L 168 -1 N SER L 167 O ALA L 175
SHEET 1 L 4 SER L 155 PRO L 156 0
SHEET 2 L 4 THR L 147 ALA L 152 -1 N ALA L 152 O SER L 155
SHEET 3 L 4 TYR L 193 HIS L 199 -1 O THR L 198 N THR L 147
SHEET 4 L 4 SER L 202 VAL L 208 -1 O VAL L 204 N VAL L 197
SSBOND 1 CYS H 22 CYS H 95 1555 1555 2.06
SSBOND 2 CYS H 147 CYS H 203 1555 1555 2.05
SSBOND 3 CYS L 22 CYS L 87 1555 1555 2.06
SSBOND 4 CYS L 136 CYS L 195 1555 1555 2.04
CISPEP 1 PHE H 153 PRO H 154 0 -12.98
CISPEP 2 GLU H 155 PRO H 156 0 -0.65
CISPEP 3 TYR L 142 PRO L 143 0 -4.38
CRYST1 83.668 41.741 98.602 90.00 94.85 90.00 P 1 21 1 2
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 0.011952 0.000000 0.001014 0.00000
SCALE2 0.000000 0.023957 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010178 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
