HEADER IMMUNE SYSTEM 16-SEP-15 5DRZ
TITLE CRYSTAL STRUCTURE OF ANTI-HIV-1 ANTIBODY F240 FAB IN COMPLEX WITH GP41
TITLE 2 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV ANTIBODY F240 LIGHT CHAIN;
COMPND 3 CHAIN: L, A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HIV ANTIBODY F240 HEAVY CHAIN;
COMPND 7 CHAIN: H, B;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN GP160;
COMPND 11 CHAIN: Q, P;
COMPND 12 SYNONYM: ENV POLYPROTEIN;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: HEK-293;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM_CELL_LINE: HEK-293;
SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: HIV-1 M:B_ARV2/SF2;
SOURCE 18 ORGANISM_COMMON: HIV-1;
SOURCE 19 ORGANISM_TAXID: 11685
KEYWDS IGG, VIRAL PROTEIN, HIV GP41 ENVELOPE PROTEIN, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR N.GOHAIN,W.D.TOLBERT,M.PAZGIER
REVDAT 4 27-SEP-23 5DRZ 1 REMARK
REVDAT 3 27-SEP-17 5DRZ 1 REMARK
REVDAT 2 24-MAY-17 5DRZ 1 JRNL
REVDAT 1 19-OCT-16 5DRZ 0
JRNL AUTH N.GOHAIN,W.D.TOLBERT,C.ORLANDI,J.RICHARD,S.DING,X.CHEN,
JRNL AUTH 2 D.A.BONSOR,E.J.SUNDBERG,W.LU,K.RAY,A.FINZI,G.K.LEWIS,
JRNL AUTH 3 M.PAZGIER
JRNL TITL MOLECULAR BASIS FOR EPITOPE RECOGNITION BY NON-NEUTRALIZING
JRNL TITL 2 ANTI-GP41 ANTIBODY F240.
JRNL REF SCI REP V. 6 36685 2016
JRNL REFN ESSN 2045-2322
JRNL PMID 27827447
JRNL DOI 10.1038/SREP36685
REMARK 2
REMARK 2 RESOLUTION. 2.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
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) : 2.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 168.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 30876
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1649
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) : 2.54
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2164
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.15
REMARK 3 BIN R VALUE (WORKING SET) : 0.3530
REMARK 3 BIN FREE R VALUE SET COUNT : 113
REMARK 3 BIN FREE R VALUE : 0.3710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7031
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 153
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.09000
REMARK 3 B22 (A**2) : -0.71000
REMARK 3 B33 (A**2) : 0.82000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.15000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.996
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.325
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.298
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.977
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.894
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7229 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6633 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9837 ; 1.397 ; 1.939
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15296 ; 0.968 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 920 ; 7.157 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 301 ;35.485 ;23.821
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1137 ;15.719 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;15.705 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1103 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8240 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1690 ; 0.002 ; 0.020
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): 3680 ; 0.900 ; 2.557
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3679 ; 0.900 ; 2.556
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4594 ; 1.616 ; 3.830
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4595 ; 1.616 ; 3.831
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3549 ; 0.800 ; 2.607
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3550 ; 0.800 ; 2.607
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5242 ; 1.404 ; 3.868
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 29139 ; 3.944 ;23.870
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 29103 ; 3.937 ;23.862
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 : 6
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 2 L 211
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2143 -11.0532 79.4978
REMARK 3 T TENSOR
REMARK 3 T11: 0.0336 T22: 0.0464
REMARK 3 T33: 0.0949 T12: -0.0028
REMARK 3 T13: -0.0479 T23: 0.0335
REMARK 3 L TENSOR
REMARK 3 L11: 2.9822 L22: 0.6478
REMARK 3 L33: 2.0634 L12: -0.0269
REMARK 3 L13: -1.4815 L23: 0.1243
REMARK 3 S TENSOR
REMARK 3 S11: -0.0716 S12: -0.1906 S13: -0.0705
REMARK 3 S21: 0.0203 S22: 0.0246 S23: -0.0022
REMARK 3 S31: 0.0869 S32: 0.0840 S33: 0.0470
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 : H 1 H 215
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0001 -8.2692 66.4000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0382 T22: 0.1150
REMARK 3 T33: 0.1063 T12: -0.0023
REMARK 3 T13: -0.0325 T23: 0.0274
REMARK 3 L TENSOR
REMARK 3 L11: 1.8227 L22: 0.7005
REMARK 3 L33: 1.7342 L12: 0.4077
REMARK 3 L13: -0.8961 L23: -0.1469
REMARK 3 S TENSOR
REMARK 3 S11: -0.0844 S12: 0.2775 S13: -0.0362
REMARK 3 S21: -0.1113 S22: 0.0730 S23: 0.0243
REMARK 3 S31: 0.1149 S32: -0.1385 S33: 0.0114
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 : A 2 A 213
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3368 10.7283 10.7308
REMARK 3 T TENSOR
REMARK 3 T11: 0.0453 T22: 0.0727
REMARK 3 T33: 0.1663 T12: -0.0204
REMARK 3 T13: -0.0093 T23: 0.0391
REMARK 3 L TENSOR
REMARK 3 L11: 1.1844 L22: 1.1455
REMARK 3 L33: 3.8996 L12: 0.1110
REMARK 3 L13: 0.0504 L23: -0.0910
REMARK 3 S TENSOR
REMARK 3 S11: -0.0115 S12: 0.0085 S13: 0.0181
REMARK 3 S21: -0.1552 S22: -0.0487 S23: -0.0808
REMARK 3 S31: -0.2670 S32: 0.1677 S33: 0.0602
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 : B 1 B 215
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4728 8.2838 13.3006
REMARK 3 T TENSOR
REMARK 3 T11: 0.0530 T22: 0.1511
REMARK 3 T33: 0.1611 T12: -0.0114
REMARK 3 T13: -0.0521 T23: 0.0345
REMARK 3 L TENSOR
REMARK 3 L11: 0.8103 L22: 0.9421
REMARK 3 L33: 2.0050 L12: -0.0658
REMARK 3 L13: -0.4300 L23: -0.2691
REMARK 3 S TENSOR
REMARK 3 S11: 0.0143 S12: 0.0459 S13: 0.0293
REMARK 3 S21: -0.0899 S22: 0.0798 S23: 0.0860
REMARK 3 S31: -0.1669 S32: -0.3006 S33: -0.0940
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 : Q 595 Q 609
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5261 3.7471 43.8233
REMARK 3 T TENSOR
REMARK 3 T11: 0.2511 T22: 0.3618
REMARK 3 T33: 0.1411 T12: 0.0054
REMARK 3 T13: -0.0178 T23: -0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 9.6131 L22: 5.6734
REMARK 3 L33: 1.0353 L12: -3.7882
REMARK 3 L13: -2.4503 L23: -0.3414
REMARK 3 S TENSOR
REMARK 3 S11: -0.2420 S12: -1.2042 S13: 0.9653
REMARK 3 S21: 0.1160 S22: 0.4449 S23: -0.4950
REMARK 3 S31: 0.0804 S32: 0.3142 S33: -0.2029
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 595 P 609
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4638 -3.7270 46.0618
REMARK 3 T TENSOR
REMARK 3 T11: 0.1696 T22: 0.3304
REMARK 3 T33: 0.3906 T12: -0.0407
REMARK 3 T13: 0.0375 T23: 0.0529
REMARK 3 L TENSOR
REMARK 3 L11: 3.4094 L22: 5.9764
REMARK 3 L33: 11.0085 L12: 0.4267
REMARK 3 L13: 5.7044 L23: -2.1694
REMARK 3 S TENSOR
REMARK 3 S11: 0.1537 S12: 0.3145 S13: -0.0784
REMARK 3 S21: -0.1180 S22: -0.1310 S23: -0.5789
REMARK 3 S31: 0.4011 S32: 0.5333 S33: -0.0227
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 5DRZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000213690.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0-5.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9753
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : RH COATED FLAT MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33289
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.540
REMARK 200 RESOLUTION RANGE LOW (A) : 168.790
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.15800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.95700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
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: 3TNN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 15% ISOPROPANOL, 0.2M
REMARK 280 AMMONIUM CITRATE PH4.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 294K
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 30.24400
REMARK 290 SMTRY3 2 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 APPLY THE FOLLOWING TO CHAINS: L, H, P
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 APPLY THE FOLLOWING TO CHAINS: A, B, Q
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 GLU L 1
REMARK 465 GLY L 212
REMARK 465 GLU L 213
REMARK 465 CYS L 214
REMARK 465 CYS H 216
REMARK 465 ASP H 217
REMARK 465 LYS H 218
REMARK 465 THR H 219
REMARK 465 HIS H 220
REMARK 465 GLU A 1
REMARK 465 CYS A 214
REMARK 465 CYS B 216
REMARK 465 ASP B 217
REMARK 465 LYS B 218
REMARK 465 THR B 219
REMARK 465 HIS B 220
REMARK 465 VAL Q 583
REMARK 465 GLU Q 584
REMARK 465 ARG Q 585
REMARK 465 TYR Q 586
REMARK 465 LEU Q 587
REMARK 465 ARG Q 588
REMARK 465 ASP Q 589
REMARK 465 GLN Q 590
REMARK 465 GLN Q 591
REMARK 465 LEU Q 592
REMARK 465 LEU Q 593
REMARK 465 GLY Q 594
REMARK 465 TRP Q 610
REMARK 465 ASN Q 611
REMARK 465 ALA Q 612
REMARK 465 SER Q 613
REMARK 465 TRP Q 614
REMARK 465 SER Q 615
REMARK 465 ASN Q 616
REMARK 465 LYS Q 617
REMARK 465 SER Q 618
REMARK 465 VAL P 583
REMARK 465 GLU P 584
REMARK 465 ARG P 585
REMARK 465 TYR P 586
REMARK 465 LEU P 587
REMARK 465 ARG P 588
REMARK 465 ASP P 589
REMARK 465 GLN P 590
REMARK 465 GLN P 591
REMARK 465 LEU P 592
REMARK 465 LEU P 593
REMARK 465 GLY P 594
REMARK 465 TRP P 610
REMARK 465 ASN P 611
REMARK 465 ALA P 612
REMARK 465 SER P 613
REMARK 465 TRP P 614
REMARK 465 SER P 615
REMARK 465 ASN P 616
REMARK 465 LYS P 617
REMARK 465 SER P 618
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 THR H 131 O THR H 135 1.77
REMARK 500 O LYS B 129 OG SER B 132 2.01
REMARK 500 O ASP B 53 N SER B 55 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP B 84 O THR B 131 2655 1.99
REMARK 500 OD1 ASP B 84 O THR B 131 2655 2.10
REMARK 500 CG ASP B 84 O THR B 131 2655 2.14
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 ASN L 28 -19.71 146.08
REMARK 500 ALA L 51 -37.79 68.19
REMARK 500 ALA L 84 -176.77 -177.22
REMARK 500 ASN L 158 27.63 -149.56
REMARK 500 THR H 28 96.15 -69.86
REMARK 500 ASP H 53 78.42 163.12
REMARK 500 SER H 55 93.25 -40.04
REMARK 500 GLN H 64 54.84 -65.04
REMARK 500 ALA H 74 -55.14 156.30
REMARK 500 THR H 82B 55.91 36.69
REMARK 500 SER H 130 -96.45 -92.63
REMARK 500 SER H 130 -94.73 -93.84
REMARK 500 THR H 131 -91.04 59.92
REMARK 500 THR H 131 -91.04 58.57
REMARK 500 SER H 132 -174.29 50.21
REMARK 500 ASP H 144 62.40 63.99
REMARK 500 ALA A 51 -40.40 63.92
REMARK 500 ASP A 151 44.44 70.58
REMARK 500 ASN A 152 -10.15 67.97
REMARK 500 ARG A 211 85.39 -56.83
REMARK 500 GLN B 64 46.64 -83.88
REMARK 500 ASP B 100 -155.94 -145.79
REMARK 500 SER B 127 -88.43 -113.84
REMARK 500 LYS B 129 -61.62 108.83
REMARK 500 THR B 131 -42.95 -132.01
REMARK 500 SER B 132 -90.08 -90.71
REMARK 500 ASP B 144 67.67 61.51
REMARK 500 LYS B 214 -141.41 85.05
REMARK 500 TRP Q 596 116.85 178.22
REMARK 500 ALA Q 607 32.30 -89.54
REMARK 500 VAL Q 608 -73.35 -61.97
REMARK 500 TRP P 596 103.29 173.96
REMARK 500 LEU P 602 -59.81 140.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP H 53 GLY H 54 149.50
REMARK 500 GLY H 54 SER H 55 -146.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH L 434 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A 329 DISTANCE = 6.07 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 301
DBREF 5DRZ L 1 214 PDB 5DRZ 5DRZ 1 214
DBREF 5DRZ H 1 220 PDB 5DRZ 5DRZ 1 220
DBREF 5DRZ A 1 214 PDB 5DRZ 5DRZ 1 214
DBREF 5DRZ B 1 220 PDB 5DRZ 5DRZ 1 220
DBREF 5DRZ Q 583 618 UNP P03378 ENV_HV1A2 582 617
DBREF 5DRZ P 583 618 UNP P03378 ENV_HV1A2 582 617
SEQRES 1 L 220 GLU PHE LEU LEU THR GLN SER PRO ASP SER LEU ALA VAL
SEQRES 2 L 220 THR LEU GLY GLU THR ALA THR ILE THR CYS ARG SER SER
SEQRES 3 L 220 ARG ASN ILE LEU HIS SER LEU ASN ASN LYS ASN TYR LEU
SEQRES 4 L 220 ALA TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO LYS LEU
SEQRES 5 L 220 LEU VAL ILE TRP ALA SER MET ARG VAL SER GLY VAL ALA
SEQRES 6 L 220 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE ALA
SEQRES 7 L 220 LEU THR ILE SER SER LEU GLN PRO GLU ASP ALA ALA VAL
SEQRES 8 L 220 TYR TYR CYS GLN HIS TYR TYR THR THR HIS ARG THR PHE
SEQRES 9 L 220 GLY GLN GLY THR ARG VAL GLU ILE ARG ARG THR VAL ALA
SEQRES 10 L 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN
SEQRES 11 L 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN
SEQRES 12 L 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL
SEQRES 13 L 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL
SEQRES 14 L 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER
SEQRES 15 L 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS
SEQRES 16 L 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER
SEQRES 17 L 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS
SEQRES 1 H 232 GLN VAL GLN LEU VAL GLN SER GLY GLY GLY VAL VAL LYS
SEQRES 2 H 232 PRO GLY ALA SER SER ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 H 232 PHE THR PHE THR ASP TYR TYR MET SER TRP ILE ARG GLN
SEQRES 4 H 232 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA TYR ILE THR
SEQRES 5 H 232 LYS ASP GLY SER GLU LYS LYS TYR ALA ASP SER LEU GLN
SEQRES 6 H 232 HIS ARG PHE ALA VAL SER ARG ASP ASN ALA ASN ASN LEU
SEQRES 7 H 232 VAL PHE LEU GLN LEU ASN THR VAL GLU ASP ASP ASP THR
SEQRES 8 H 232 GLY VAL TYR TYR CYS ALA ARG ASP ASP GLY TYR TYR ASP
SEQRES 9 H 232 ARG SER GLY TYR TYR GLY VAL PHE ASP LEU TRP GLY GLN
SEQRES 10 H 232 GLY ILE ARG VAL THR VAL SER SER ALA SER THR LYS GLY
SEQRES 11 H 232 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR
SEQRES 12 H 232 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP
SEQRES 13 H 232 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY
SEQRES 14 H 232 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU
SEQRES 15 H 232 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR
SEQRES 16 H 232 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS
SEQRES 17 H 232 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS
SEQRES 18 H 232 ARG VAL GLU PRO LYS SER CYS ASP LYS THR HIS
SEQRES 1 A 220 GLU PHE LEU LEU THR GLN SER PRO ASP SER LEU ALA VAL
SEQRES 2 A 220 THR LEU GLY GLU THR ALA THR ILE THR CYS ARG SER SER
SEQRES 3 A 220 ARG ASN ILE LEU HIS SER LEU ASN ASN LYS ASN TYR LEU
SEQRES 4 A 220 ALA TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO LYS LEU
SEQRES 5 A 220 LEU VAL ILE TRP ALA SER MET ARG VAL SER GLY VAL ALA
SEQRES 6 A 220 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE ALA
SEQRES 7 A 220 LEU THR ILE SER SER LEU GLN PRO GLU ASP ALA ALA VAL
SEQRES 8 A 220 TYR TYR CYS GLN HIS TYR TYR THR THR HIS ARG THR PHE
SEQRES 9 A 220 GLY GLN GLY THR ARG VAL GLU ILE ARG ARG THR VAL ALA
SEQRES 10 A 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN
SEQRES 11 A 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN
SEQRES 12 A 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL
SEQRES 13 A 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL
SEQRES 14 A 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER
SEQRES 15 A 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS
SEQRES 16 A 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER
SEQRES 17 A 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS
SEQRES 1 B 232 GLN VAL GLN LEU VAL GLN SER GLY GLY GLY VAL VAL LYS
SEQRES 2 B 232 PRO GLY ALA SER SER ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 B 232 PHE THR PHE THR ASP TYR TYR MET SER TRP ILE ARG GLN
SEQRES 4 B 232 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA TYR ILE THR
SEQRES 5 B 232 LYS ASP GLY SER GLU LYS LYS TYR ALA ASP SER LEU GLN
SEQRES 6 B 232 HIS ARG PHE ALA VAL SER ARG ASP ASN ALA ASN ASN LEU
SEQRES 7 B 232 VAL PHE LEU GLN LEU ASN THR VAL GLU ASP ASP ASP THR
SEQRES 8 B 232 GLY VAL TYR TYR CYS ALA ARG ASP ASP GLY TYR TYR ASP
SEQRES 9 B 232 ARG SER GLY TYR TYR GLY VAL PHE ASP LEU TRP GLY GLN
SEQRES 10 B 232 GLY ILE ARG VAL THR VAL SER SER ALA SER THR LYS GLY
SEQRES 11 B 232 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR
SEQRES 12 B 232 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP
SEQRES 13 B 232 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY
SEQRES 14 B 232 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU
SEQRES 15 B 232 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR
SEQRES 16 B 232 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS
SEQRES 17 B 232 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS
SEQRES 18 B 232 ARG VAL GLU PRO LYS SER CYS ASP LYS THR HIS
SEQRES 1 Q 36 VAL GLU ARG TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE
SEQRES 2 Q 36 TRP GLY CYS SER GLY LYS LEU ILE CYS THR THR ALA VAL
SEQRES 3 Q 36 PRO TRP ASN ALA SER TRP SER ASN LYS SER
SEQRES 1 P 36 VAL GLU ARG TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE
SEQRES 2 P 36 TRP GLY CYS SER GLY LYS LEU ILE CYS THR THR ALA VAL
SEQRES 3 P 36 PRO TRP ASN ALA SER TRP SER ASN LYS SER
HET MG L 301 1
HETNAM MG MAGNESIUM ION
FORMUL 7 MG MG 2+
FORMUL 8 HOH *153(H2 O)
HELIX 1 AA1 GLN L 79 ALA L 83 5 5
HELIX 2 AA2 SER L 121 LYS L 126 1 6
HELIX 3 AA3 LYS L 183 GLU L 187 1 5
HELIX 4 AA4 THR H 28 TYR H 32 5 5
HELIX 5 AA5 SER H 156 ALA H 158 5 3
HELIX 6 AA6 SER H 187 LEU H 189 5 3
HELIX 7 AA7 LYS H 201 ASN H 204 5 4
HELIX 8 AA8 GLN A 79 ALA A 83 5 5
HELIX 9 AA9 SER A 121 LYS A 126 1 6
HELIX 10 AB1 LYS A 183 GLU A 187 1 5
HELIX 11 AB2 THR B 28 TYR B 32 5 5
HELIX 12 AB3 GLU B 83 THR B 87 5 5
HELIX 13 AB4 SER B 156 ALA B 158 5 3
HELIX 14 AB5 SER B 187 LEU B 189 5 3
HELIX 15 AB6 LYS B 201 ASN B 204 5 4
SHEET 1 AA1 4 LEU L 4 SER L 7 0
SHEET 2 AA1 4 ALA L 19 SER L 25 -1 O THR L 22 N SER L 7
SHEET 3 AA1 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21
SHEET 4 AA1 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74
SHEET 1 AA2 6 SER L 10 THR L 14 0
SHEET 2 AA2 6 THR L 102 ARG L 107 1 O GLU L 105 N LEU L 11
SHEET 3 AA2 6 ALA L 84 HIS L 90 -1 N ALA L 84 O VAL L 104
SHEET 4 AA2 6 LEU L 33 GLN L 38 -1 N ALA L 34 O GLN L 89
SHEET 5 AA2 6 LYS L 45 ILE L 49 -1 O LEU L 47 N TRP L 35
SHEET 6 AA2 6 MET L 53 ARG L 54 -1 O MET L 53 N ILE L 49
SHEET 1 AA3 4 SER L 114 PHE L 118 0
SHEET 2 AA3 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118
SHEET 3 AA3 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136
SHEET 4 AA3 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178
SHEET 1 AA4 4 ALA L 153 LEU L 154 0
SHEET 2 AA4 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153
SHEET 3 AA4 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149
SHEET 4 AA4 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196
SHEET 1 AA5 4 GLN H 3 GLY H 8 0
SHEET 2 AA5 4 SER H 18 SER H 25 -1 O ALA H 23 N VAL H 5
SHEET 3 AA5 4 LEU H 77 LEU H 82 -1 O LEU H 80 N LEU H 20
SHEET 4 AA5 4 PHE H 67 ASP H 72 -1 N ASP H 72 O LEU H 77
SHEET 1 AA6 4 GLY H 10 VAL H 12 0
SHEET 2 AA6 4 ILE H 107 VAL H 111 1 O THR H 110 N GLY H 10
SHEET 3 AA6 4 GLY H 88 ASP H 100 -1 N TYR H 90 O ILE H 107
SHEET 4 AA6 4 TYR H 100D TRP H 103 -1 O LEU H 102 N ARG H 94
SHEET 1 AA7 5 LYS H 57 TYR H 59 0
SHEET 2 AA7 5 LEU H 45 ILE H 51 -1 N TYR H 50 O LYS H 58
SHEET 3 AA7 5 TYR H 33 GLN H 39 -1 N ARG H 38 O GLU H 46
SHEET 4 AA7 5 GLY H 88 ASP H 100 -1 O TYR H 91 N ILE H 37
SHEET 5 AA7 5 TRP P 596 SER P 599 -1 O GLY P 597 N TYR H 99
SHEET 1 AA8 4 SER H 120 LEU H 124 0
SHEET 2 AA8 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124
SHEET 3 AA8 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145
SHEET 4 AA8 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181
SHEET 1 AA9 4 SER H 120 LEU H 124 0
SHEET 2 AA9 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124
SHEET 3 AA9 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145
SHEET 4 AA9 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177
SHEET 1 AB1 3 THR H 151 TRP H 154 0
SHEET 2 AB1 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153
SHEET 3 AB1 3 THR H 205 ARG H 210 -1 O THR H 205 N HIS H 200
SHEET 1 AB2 4 LEU A 4 SER A 7 0
SHEET 2 AB2 4 ALA A 19 SER A 25 -1 O THR A 22 N SER A 7
SHEET 3 AB2 4 ASP A 70 ILE A 75 -1 O ILE A 75 N ALA A 19
SHEET 4 AB2 4 PHE A 62 SER A 67 -1 N SER A 65 O ALA A 72
SHEET 1 AB3 6 SER A 10 THR A 14 0
SHEET 2 AB3 6 THR A 102 ARG A 107 1 O GLU A 105 N LEU A 11
SHEET 3 AB3 6 ALA A 84 HIS A 90 -1 N ALA A 84 O VAL A 104
SHEET 4 AB3 6 LEU A 33 GLN A 38 -1 N TYR A 36 O TYR A 87
SHEET 5 AB3 6 LYS A 45 ILE A 49 -1 O LEU A 47 N TRP A 35
SHEET 6 AB3 6 MET A 53 ARG A 54 -1 O MET A 53 N ILE A 49
SHEET 1 AB4 4 SER A 10 THR A 14 0
SHEET 2 AB4 4 THR A 102 ARG A 107 1 O GLU A 105 N LEU A 11
SHEET 3 AB4 4 ALA A 84 HIS A 90 -1 N ALA A 84 O VAL A 104
SHEET 4 AB4 4 THR A 97 PHE A 98 -1 O THR A 97 N HIS A 90
SHEET 1 AB5 2 LEU A 27C HIS A 27D 0
SHEET 2 AB5 2 LYS A 30 ASN A 31 -1 O LYS A 30 N HIS A 27D
SHEET 1 AB6 4 SER A 114 PHE A 118 0
SHEET 2 AB6 4 THR A 129 PHE A 139 -1 O LEU A 135 N PHE A 116
SHEET 3 AB6 4 TYR A 173 SER A 182 -1 O LEU A 179 N VAL A 132
SHEET 4 AB6 4 SER A 159 VAL A 163 -1 N GLN A 160 O THR A 178
SHEET 1 AB7 4 ALA A 153 LEU A 154 0
SHEET 2 AB7 4 LYS A 145 VAL A 150 -1 N VAL A 150 O ALA A 153
SHEET 3 AB7 4 VAL A 191 THR A 197 -1 O ALA A 193 N LYS A 149
SHEET 4 AB7 4 VAL A 205 ASN A 210 -1 O LYS A 207 N CYS A 194
SHEET 1 AB8 4 GLN B 3 SER B 7 0
SHEET 2 AB8 4 SER B 18 SER B 25 -1 O ALA B 23 N VAL B 5
SHEET 3 AB8 4 LEU B 77 LEU B 82 -1 O LEU B 82 N SER B 18
SHEET 4 AB8 4 PHE B 67 ASP B 72 -1 N ALA B 68 O GLN B 81
SHEET 1 AB9 4 VAL B 11 VAL B 12 0
SHEET 2 AB9 4 ILE B 107 VAL B 111 1 O THR B 110 N VAL B 12
SHEET 3 AB9 4 GLY B 88 ASP B 100 -1 N TYR B 90 O ILE B 107
SHEET 4 AB9 4 TYR B 100D TRP B 103 -1 O VAL B 100G N ASP B 96
SHEET 1 AC1 5 LYS B 57 TYR B 59 0
SHEET 2 AC1 5 LEU B 45 ILE B 51 -1 N TYR B 50 O LYS B 58
SHEET 3 AC1 5 TYR B 33 GLN B 39 -1 N ARG B 38 O GLU B 46
SHEET 4 AC1 5 GLY B 88 ASP B 100 -1 O TYR B 91 N ILE B 37
SHEET 5 AC1 5 TRP Q 596 SER Q 599 -1 O SER Q 599 N GLY B 97
SHEET 1 AC2 4 SER B 120 LEU B 124 0
SHEET 2 AC2 4 THR B 135 TYR B 145 -1 O GLY B 139 N LEU B 124
SHEET 3 AC2 4 TYR B 176 PRO B 185 -1 O TYR B 176 N TYR B 145
SHEET 4 AC2 4 VAL B 163 THR B 165 -1 N HIS B 164 O VAL B 181
SHEET 1 AC3 4 SER B 120 LEU B 124 0
SHEET 2 AC3 4 THR B 135 TYR B 145 -1 O GLY B 139 N LEU B 124
SHEET 3 AC3 4 TYR B 176 PRO B 185 -1 O TYR B 176 N TYR B 145
SHEET 4 AC3 4 VAL B 169 LEU B 170 -1 N VAL B 169 O SER B 177
SHEET 1 AC4 3 THR B 151 TRP B 154 0
SHEET 2 AC4 3 ILE B 195 HIS B 200 -1 O ASN B 199 N THR B 151
SHEET 3 AC4 3 THR B 205 ARG B 210 -1 O THR B 205 N HIS B 200
SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.09
SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.01
SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.08
SSBOND 4 CYS H 140 CYS H 196 1555 1555 2.01
SSBOND 5 CYS A 23 CYS A 88 1555 1555 2.09
SSBOND 6 CYS A 134 CYS A 194 1555 1555 2.02
SSBOND 7 CYS B 22 CYS B 92 1555 1555 2.91
SSBOND 8 CYS B 140 CYS B 196 1555 1555 1.98
SSBOND 9 CYS Q 598 CYS Q 604 1555 1555 2.00
SSBOND 10 CYS P 598 CYS P 604 1555 1555 2.05
CISPEP 1 SER L 7 PRO L 8 0 -2.23
CISPEP 2 TYR L 140 PRO L 141 0 6.42
CISPEP 3 GLY H 133 GLY H 134 0 -13.47
CISPEP 4 PHE H 146 PRO H 147 0 -1.55
CISPEP 5 GLU H 148 PRO H 149 0 5.68
CISPEP 6 LYS H 214 SER H 215 0 -7.53
CISPEP 7 SER A 7 PRO A 8 0 -0.68
CISPEP 8 TYR A 140 PRO A 141 0 3.75
CISPEP 9 LYS B 129 SER B 130 0 -10.44
CISPEP 10 THR B 131 SER B 132 0 -20.56
CISPEP 11 PHE B 146 PRO B 147 0 -4.49
CISPEP 12 GLU B 148 PRO B 149 0 0.88
CISPEP 13 VAL Q 608 PRO Q 609 0 7.85
SITE 1 AC1 5 PRO L 80 ALA L 83 ILE L 106 ASP L 167
SITE 2 AC1 5 SER L 171
CRYST1 49.317 60.488 169.228 90.00 94.13 90.00 P 1 21 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 0.020277 0.000000 0.001466 0.00000
SCALE2 0.000000 0.016532 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005925 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 0.770664 -0.025536 0.636730 -24.89372 1
MTRIX2 2 -0.026459 -0.999617 -0.008066 0.64049 1
MTRIX3 2 0.636692 -0.010631 -0.771045 68.72703 1
(ATOM LINES ARE NOT SHOWN.)
END
