HEADER MEMBRANE PROTEIN 29-MAR-23 8IVX TITLE CRYSTAL STRUCTURE OF NRP2 IN COMPLEX WITH ANRP2-14 FAB FRAGMENT COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANRP2-14; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: VASCULAR ENDOTHELIAL CELL GROWTH FACTOR 165 RECEPTOR 2; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HEAVY CHAIN OF ANTIBODY 14V4 FAB FRAGMENT; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: LIGHT CHAIN OF ANTIBODY 14V4 FAB FRAGMENT; COMPND 12 CHAIN: L; COMPND 13 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: NRP2, VEGF165R2; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; 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 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS COMPLEX, ANTIBODY, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR Y.GENG,L.ZHAI JRNL AUTH Z.XU,H.L.GOEL,C.BURKART,L.BURMAN,Y.E.CHONG,A.G.BARBER, JRNL AUTH 2 Y.GENG,L.ZHAI,M.WANG,A.KUMAR,A.MENEFEE,C.POLIZZI,L.EIDE, JRNL AUTH 3 K.RAUCH,J.RAHMAN,K.HAMEL,Z.FOGASSY,S.KLOPP-SAVINO,S.PAZ, JRNL AUTH 4 M.ZHANG,A.CUBITT,L.A.NANGLE,A.M.MERCURIO JRNL TITL INHIBITION OF VEGF BINDING TO NEUROPILIN-2 ENHANCES JRNL TITL 2 CHEMOSENSITIVITY AND INHIBITS METASTASIS IN TRIPLE-NEGATIVE JRNL TITL 3 BREAST CANCER. JRNL REF SCI TRANSL MED V. 15 F1128 2023 JRNL REFN ESSN 1946-6242 JRNL PMID 37134152 JRNL DOI 10.1126/SCITRANSLMED.ADF1128 REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0352 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) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.65 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1 REMARK 3 NUMBER OF REFLECTIONS : 74703 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) : 0.193 REMARK 3 R VALUE (WORKING SET) : 0.191 REMARK 3 FREE R VALUE : 0.225 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200 REMARK 3 FREE R VALUE TEST SET COUNT : 4067 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95 REMARK 3 REFLECTION IN BIN (WORKING SET) : 5286 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.78 REMARK 3 BIN R VALUE (WORKING SET) : 0.3000 REMARK 3 BIN FREE R VALUE SET COUNT : 256 REMARK 3 BIN FREE R VALUE : 0.3250 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6525 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 4 REMARK 3 SOLVENT ATOMS : 416 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.36 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.51000 REMARK 3 B22 (A**2) : 0.72000 REMARK 3 B33 (A**2) : -0.06000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -1.04000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.144 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.134 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.111 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.705 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6709 ; 0.006 ; 0.016 REMARK 3 BOND LENGTHS OTHERS (A): 5903 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9123 ; 1.057 ; 1.803 REMARK 3 BOND ANGLES OTHERS (DEGREES): 13817 ; 0.365 ; 1.559 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 861 ; 6.579 ; 5.203 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1074 ;11.247 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 999 ; 0.059 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7577 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1351 ; 0.001 ; 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): 3334 ; 3.145 ; 2.333 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3334 ; 3.142 ; 2.333 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4150 ; 4.213 ; 3.468 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4151 ; 4.217 ; 3.469 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3375 ; 4.597 ; 2.743 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3376 ; 4.596 ; 2.744 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4974 ; 6.313 ; 3.947 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 7104 ; 7.861 ;31.082 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 7027 ; 7.850 ;29.776 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 : 3 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 : A 149 A 595 REMARK 3 ORIGIN FOR THE GROUP (A): -23.2180 -15.1510 50.3320 REMARK 3 T TENSOR REMARK 3 T11: 0.3291 T22: 0.3515 REMARK 3 T33: 0.0071 T12: -0.0632 REMARK 3 T13: 0.0331 T23: 0.0003 REMARK 3 L TENSOR REMARK 3 L11: 1.0040 L22: 1.4313 REMARK 3 L33: 1.5840 L12: -0.1166 REMARK 3 L13: -0.2986 L23: -0.0583 REMARK 3 S TENSOR REMARK 3 S11: 0.0574 S12: -0.3588 S13: 0.0045 REMARK 3 S21: 0.4828 S22: -0.0140 S23: 0.0931 REMARK 3 S31: -0.1024 S32: -0.0588 S33: -0.0435 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 221 REMARK 3 ORIGIN FOR THE GROUP (A): -21.8820 -8.9020 1.8590 REMARK 3 T TENSOR REMARK 3 T11: 0.0790 T22: 0.0735 REMARK 3 T33: 0.0018 T12: 0.0120 REMARK 3 T13: 0.0037 T23: -0.0056 REMARK 3 L TENSOR REMARK 3 L11: 0.3763 L22: 0.8114 REMARK 3 L33: 1.8510 L12: 0.0871 REMARK 3 L13: -0.1815 L23: -0.3553 REMARK 3 S TENSOR REMARK 3 S11: 0.0074 S12: 0.0388 S13: -0.0053 REMARK 3 S21: -0.1311 S22: -0.0384 S23: -0.0265 REMARK 3 S31: 0.0449 S32: 0.0189 S33: 0.0310 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 : L 1 L 213 REMARK 3 ORIGIN FOR THE GROUP (A): -19.9600 8.3220 -4.7110 REMARK 3 T TENSOR REMARK 3 T11: 0.1186 T22: 0.1063 REMARK 3 T33: 0.0332 T12: 0.0195 REMARK 3 T13: -0.0096 T23: -0.0030 REMARK 3 L TENSOR REMARK 3 L11: 0.2469 L22: 0.6032 REMARK 3 L33: 1.8325 L12: 0.0584 REMARK 3 L13: -0.1438 L23: -0.0774 REMARK 3 S TENSOR REMARK 3 S11: -0.0023 S12: 0.0419 S13: -0.0004 REMARK 3 S21: -0.0640 S22: -0.0337 S23: 0.0540 REMARK 3 S31: 0.0037 S32: 0.0028 S33: 0.0360 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.00 REMARK 3 ION PROBE RADIUS : 0.70 REMARK 3 SHRINKAGE RADIUS : 0.70 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS REMARK 3 U VALUES : RESIDUAL ONLY REMARK 4 REMARK 4 8IVX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ. REMARK 100 THE DEPOSITION ID IS D_1300036612. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-MAR-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL19U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78778 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 200 DATA REDUNDANCY : 5.900 REMARK 200 R MERGE (I) : 0.07400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 23.2800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1 REMARK 200 DATA REDUNDANCY IN SHELL : 6.10 REMARK 200 R MERGE FOR SHELL (I) : 0.59000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.410 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.08 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG300, 0.1M SODIUM ACETATE REMARK 280 TRIHYDRATE PH 4.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 289K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 44.75050 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.70550 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 44.75050 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 44.70550 REMARK 290 SMTRY3 4 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 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 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 H 565 LIES ON A SPECIAL POSITION. 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 HIS A 13 REMARK 465 HIS A 14 REMARK 465 HIS A 15 REMARK 465 HIS A 16 REMARK 465 HIS A 17 REMARK 465 HIS A 18 REMARK 465 GLU A 19 REMARK 465 ASN A 20 REMARK 465 LEU A 21 REMARK 465 TYR A 22 REMARK 465 PHE A 23 REMARK 465 GLN A 24 REMARK 465 ASP A 25 REMARK 465 PRO A 26 REMARK 465 PRO A 27 REMARK 465 CYS A 28 REMARK 465 GLY A 29 REMARK 465 GLY A 30 REMARK 465 ARG A 31 REMARK 465 LEU A 32 REMARK 465 ASN A 33 REMARK 465 SER A 34 REMARK 465 LYS A 35 REMARK 465 ASP A 36 REMARK 465 ALA A 37 REMARK 465 GLY A 38 REMARK 465 TYR A 39 REMARK 465 ILE A 40 REMARK 465 THR A 41 REMARK 465 SER A 42 REMARK 465 PRO A 43 REMARK 465 GLY A 44 REMARK 465 TYR A 45 REMARK 465 PRO A 46 REMARK 465 GLN A 47 REMARK 465 ASP A 48 REMARK 465 TYR A 49 REMARK 465 PRO A 50 REMARK 465 SER A 51 REMARK 465 HIS A 52 REMARK 465 GLN A 53 REMARK 465 ASN A 54 REMARK 465 CYS A 55 REMARK 465 GLU A 56 REMARK 465 TRP A 57 REMARK 465 ILE A 58 REMARK 465 VAL A 59 REMARK 465 TYR A 60 REMARK 465 ALA A 61 REMARK 465 PRO A 62 REMARK 465 GLU A 63 REMARK 465 PRO A 64 REMARK 465 ASN A 65 REMARK 465 GLN A 66 REMARK 465 LYS A 67 REMARK 465 ILE A 68 REMARK 465 VAL A 69 REMARK 465 LEU A 70 REMARK 465 ASN A 71 REMARK 465 PHE A 72 REMARK 465 ASN A 73 REMARK 465 PRO A 74 REMARK 465 HIS A 75 REMARK 465 PHE A 76 REMARK 465 GLU A 77 REMARK 465 ILE A 78 REMARK 465 GLU A 79 REMARK 465 LYS A 80 REMARK 465 HIS A 81 REMARK 465 ASP A 82 REMARK 465 CYS A 83 REMARK 465 LYS A 84 REMARK 465 TYR A 85 REMARK 465 ASP A 86 REMARK 465 PHE A 87 REMARK 465 ILE A 88 REMARK 465 GLU A 89 REMARK 465 ILE A 90 REMARK 465 ARG A 91 REMARK 465 ASP A 92 REMARK 465 GLY A 93 REMARK 465 ASP A 94 REMARK 465 SER A 95 REMARK 465 GLU A 96 REMARK 465 SER A 97 REMARK 465 ALA A 98 REMARK 465 ASP A 99 REMARK 465 LEU A 100 REMARK 465 LEU A 101 REMARK 465 GLY A 102 REMARK 465 LYS A 103 REMARK 465 HIS A 104 REMARK 465 CYS A 105 REMARK 465 GLY A 106 REMARK 465 ASN A 107 REMARK 465 ILE A 108 REMARK 465 ALA A 109 REMARK 465 PRO A 110 REMARK 465 PRO A 111 REMARK 465 THR A 112 REMARK 465 ILE A 113 REMARK 465 ILE A 114 REMARK 465 SER A 115 REMARK 465 SER A 116 REMARK 465 GLY A 117 REMARK 465 SER A 118 REMARK 465 MET A 119 REMARK 465 LEU A 120 REMARK 465 TYR A 121 REMARK 465 ILE A 122 REMARK 465 LYS A 123 REMARK 465 PHE A 124 REMARK 465 THR A 125 REMARK 465 SER A 126 REMARK 465 ASP A 127 REMARK 465 TYR A 128 REMARK 465 ALA A 129 REMARK 465 ARG A 130 REMARK 465 GLN A 131 REMARK 465 GLY A 132 REMARK 465 ALA A 133 REMARK 465 GLY A 134 REMARK 465 PHE A 135 REMARK 465 SER A 136 REMARK 465 LEU A 137 REMARK 465 ARG A 138 REMARK 465 TYR A 139 REMARK 465 GLU A 140 REMARK 465 ILE A 141 REMARK 465 PHE A 142 REMARK 465 LYS A 143 REMARK 465 THR A 144 REMARK 465 GLY A 145 REMARK 465 SER A 146 REMARK 465 GLU A 147 REMARK 465 ASP A 148 REMARK 465 GLU A 197 REMARK 465 HIS A 198 REMARK 465 ASP A 199 REMARK 465 PRO A 200 REMARK 465 LEU A 201 REMARK 465 GLN A 202 REMARK 465 VAL A 203 REMARK 465 GLY A 204 REMARK 465 GLU A 205 REMARK 465 GLY A 206 REMARK 465 ASP A 207 REMARK 465 CYS A 208 REMARK 465 LYS A 209 REMARK 465 LYS A 257 REMARK 465 ASP A 258 REMARK 465 GLU A 270 REMARK 465 PRO A 271 REMARK 465 LEU A 272 REMARK 465 GLU A 273 REMARK 465 GLY A 378 REMARK 465 LYS A 379 REMARK 465 ASN A 380 REMARK 465 TYR A 458 REMARK 465 LEU A 459 REMARK 465 ARG A 477 REMARK 465 ILE A 478 REMARK 465 PRO A 479 REMARK 465 GLN A 480 REMARK 465 ALA A 481 REMARK 465 GLN A 482 REMARK 465 GLY A 508 REMARK 465 GLY A 509 REMARK 465 ASP A 510 REMARK 465 SER A 511 REMARK 465 ILE A 512 REMARK 465 THR A 513 REMARK 465 ALA A 514 REMARK 465 VAL A 515 REMARK 465 GLU A 516 REMARK 465 ALA A 517 REMARK 465 SER H 135 REMARK 465 ALA H 136 REMARK 465 ALA H 137 REMARK 465 GLN H 138 REMARK 465 THR H 139 REMARK 465 ASN H 140 REMARK 465 CYS H 222 REMARK 465 GLY H 223 REMARK 465 GLY H 224 REMARK 465 SER H 225 REMARK 465 HIS H 226 REMARK 465 HIS H 227 REMARK 465 HIS H 228 REMARK 465 HIS H 229 REMARK 465 HIS H 230 REMARK 465 HIS H 231 REMARK 465 GLU L 214 REMARK 465 CYS L 215 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 VAL A 222 -61.15 -127.23 REMARK 500 CYS A 230 -51.78 -128.23 REMARK 500 ASP A 252 -165.19 -121.00 REMARK 500 SER A 309 39.61 -82.00 REMARK 500 ASN A 316 -129.81 52.98 REMARK 500 ARG A 334 -30.66 79.03 REMARK 500 ALA A 386 -118.08 -113.64 REMARK 500 SER A 416 -40.40 70.54 REMARK 500 SER A 435 43.68 -141.80 REMARK 500 GLN A 456 42.76 -105.14 REMARK 500 VAL A 468 -50.25 67.99 REMARK 500 SER A 472 -88.28 -142.96 REMARK 500 GLU A 485 -35.75 -138.69 REMARK 500 ALA L 51 -41.64 70.00 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 239 0.08 SIDE_CHAIN REMARK 500 ARG A 263 0.07 SIDE_CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 8IVX A 25 595 UNP O60462 NRP2_HUMAN 25 595 DBREF 8IVX H 1 231 PDB 8IVX 8IVX 1 231 DBREF 8IVX L 1 215 PDB 8IVX 8IVX 1 215 SEQADV 8IVX HIS A 13 UNP O60462 EXPRESSION TAG SEQADV 8IVX HIS A 14 UNP O60462 EXPRESSION TAG SEQADV 8IVX HIS A 15 UNP O60462 EXPRESSION TAG SEQADV 8IVX HIS A 16 UNP O60462 EXPRESSION TAG SEQADV 8IVX HIS A 17 UNP O60462 EXPRESSION TAG SEQADV 8IVX HIS A 18 UNP O60462 EXPRESSION TAG SEQADV 8IVX GLU A 19 UNP O60462 EXPRESSION TAG SEQADV 8IVX ASN A 20 UNP O60462 EXPRESSION TAG SEQADV 8IVX LEU A 21 UNP O60462 EXPRESSION TAG SEQADV 8IVX TYR A 22 UNP O60462 EXPRESSION TAG SEQADV 8IVX PHE A 23 UNP O60462 EXPRESSION TAG SEQADV 8IVX GLN A 24 UNP O60462 EXPRESSION TAG SEQRES 1 A 583 HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN ASP SEQRES 2 A 583 PRO PRO CYS GLY GLY ARG LEU ASN SER LYS ASP ALA GLY SEQRES 3 A 583 TYR ILE THR SER PRO GLY TYR PRO GLN ASP TYR PRO SER SEQRES 4 A 583 HIS GLN ASN CYS GLU TRP ILE VAL TYR ALA PRO GLU PRO SEQRES 5 A 583 ASN GLN LYS ILE VAL LEU ASN PHE ASN PRO HIS PHE GLU SEQRES 6 A 583 ILE GLU LYS HIS ASP CYS LYS TYR ASP PHE ILE GLU ILE SEQRES 7 A 583 ARG ASP GLY ASP SER GLU SER ALA ASP LEU LEU GLY LYS SEQRES 8 A 583 HIS CYS GLY ASN ILE ALA PRO PRO THR ILE ILE SER SER SEQRES 9 A 583 GLY SER MET LEU TYR ILE LYS PHE THR SER ASP TYR ALA SEQRES 10 A 583 ARG GLN GLY ALA GLY PHE SER LEU ARG TYR GLU ILE PHE SEQRES 11 A 583 LYS THR GLY SER GLU ASP CYS SER LYS ASN PHE THR SER SEQRES 12 A 583 PRO ASN GLY THR ILE GLU SER PRO GLY PHE PRO GLU LYS SEQRES 13 A 583 TYR PRO HIS ASN LEU ASP CYS THR PHE THR ILE LEU ALA SEQRES 14 A 583 LYS PRO LYS MET GLU ILE ILE LEU GLN PHE LEU ILE PHE SEQRES 15 A 583 ASP LEU GLU HIS ASP PRO LEU GLN VAL GLY GLU GLY ASP SEQRES 16 A 583 CYS LYS TYR ASP TRP LEU ASP ILE TRP ASP GLY ILE PRO SEQRES 17 A 583 HIS VAL GLY PRO LEU ILE GLY LYS TYR CYS GLY THR LYS SEQRES 18 A 583 THR PRO SER GLU LEU ARG SER SER THR GLY ILE LEU SER SEQRES 19 A 583 LEU THR PHE HIS THR ASP MET ALA VAL ALA LYS ASP GLY SEQRES 20 A 583 PHE SER ALA ARG TYR TYR LEU VAL HIS GLN GLU PRO LEU SEQRES 21 A 583 GLU ASN PHE GLN CYS ASN VAL PRO LEU GLY MET GLU SER SEQRES 22 A 583 GLY ARG ILE ALA ASN GLU GLN ILE SER ALA SER SER THR SEQRES 23 A 583 TYR SER ASP GLY ARG TRP THR PRO GLN GLN SER ARG LEU SEQRES 24 A 583 HIS GLY ASP ASP ASN GLY TRP THR PRO ASN LEU ASP SER SEQRES 25 A 583 ASN LYS GLU TYR LEU GLN VAL ASP LEU ARG PHE LEU THR SEQRES 26 A 583 MET LEU THR ALA ILE ALA THR GLN GLY ALA ILE SER ARG SEQRES 27 A 583 GLU THR GLN ASN GLY TYR TYR VAL LYS SER TYR LYS LEU SEQRES 28 A 583 GLU VAL SER THR ASN GLY GLU ASP TRP MET VAL TYR ARG SEQRES 29 A 583 HIS GLY LYS ASN HIS LYS VAL PHE GLN ALA ASN ASN ASP SEQRES 30 A 583 ALA THR GLU VAL VAL LEU ASN LYS LEU HIS ALA PRO LEU SEQRES 31 A 583 LEU THR ARG PHE VAL ARG ILE ARG PRO GLN THR TRP HIS SEQRES 32 A 583 SER GLY ILE ALA LEU ARG LEU GLU LEU PHE GLY CYS ARG SEQRES 33 A 583 VAL THR ASP ALA PRO CYS SER ASN MET LEU GLY MET LEU SEQRES 34 A 583 SER GLY LEU ILE ALA ASP SER GLN ILE SER ALA SER SER SEQRES 35 A 583 THR GLN GLU TYR LEU TRP SER PRO SER ALA ALA ARG LEU SEQRES 36 A 583 VAL SER SER ARG SER GLY TRP PHE PRO ARG ILE PRO GLN SEQRES 37 A 583 ALA GLN PRO GLY GLU GLU TRP LEU GLN VAL ASP LEU GLY SEQRES 38 A 583 THR PRO LYS THR VAL LYS GLY VAL ILE ILE GLN GLY ALA SEQRES 39 A 583 ARG GLY GLY ASP SER ILE THR ALA VAL GLU ALA ARG ALA SEQRES 40 A 583 PHE VAL ARG LYS PHE LYS VAL SER TYR SER LEU ASN GLY SEQRES 41 A 583 LYS ASP TRP GLU TYR ILE GLN ASP PRO ARG THR GLN GLN SEQRES 42 A 583 PRO LYS LEU PHE GLU GLY ASN MET HIS TYR ASP THR PRO SEQRES 43 A 583 ASP ILE ARG ARG PHE ASP PRO ILE PRO ALA GLN TYR VAL SEQRES 44 A 583 ARG VAL TYR PRO GLU ARG TRP SER PRO ALA GLY ILE GLY SEQRES 45 A 583 MET ARG LEU GLU VAL LEU GLY CYS ASP TRP THR SEQRES 1 H 231 GLN VAL GLN LEU LYS GLN SER GLY PRO GLY LEU VAL GLN SEQRES 2 H 231 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY SEQRES 3 H 231 PHE SER LEU THR SER TYR GLY VAL HIS TRP VAL ARG GLN SEQRES 4 H 231 SER PRO GLY LYS GLY LEU GLU TRP LEU GLY LEU ILE TRP SEQRES 5 H 231 SER GLY GLY SER THR ASP TYR SER PRO ALA PHE ILE SER SEQRES 6 H 231 ARG LEU SER ILE SER GLU ASP ASN SER LYS SER GLN VAL SEQRES 7 H 231 PHE PHE LYS MET ASN SER LEU GLN ALA ASP ASP THR ALA SEQRES 8 H 231 ILE TYR PHE CYS ALA ARG ASN SER TYR SER SER GLY TYR SEQRES 9 H 231 TYR ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR SEQRES 10 H 231 VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO SEQRES 11 H 231 LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL SEQRES 12 H 231 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO SEQRES 13 H 231 VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY SEQRES 14 H 231 VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR SEQRES 15 H 231 THR LEU SER SER SER VAL THR VAL PRO SER SER THR TRP SEQRES 16 H 231 PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SEQRES 17 H 231 SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP SEQRES 18 H 231 CYS GLY GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 L 215 ASP ILE VAL MET THR GLN SER GLN LYS PHE MET SER THR SEQRES 2 L 215 THR VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 L 215 GLN ASN VAL GLY THR ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 L 215 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 L 215 ASN ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 L 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER ASN MET SEQRES 7 L 215 GLN SER GLU ASP LEU ALA ASP TYR PHE CYS GLN GLN TYR SEQRES 8 L 215 SER SER TYR PRO PRO TYR THR PHE GLY GLY GLY THR LYS SEQRES 9 L 215 LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER SEQRES 10 L 215 ILE PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY SEQRES 11 L 215 ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS SEQRES 12 L 215 ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG SEQRES 13 L 215 GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER MET SER SER THR LEU THR LEU SEQRES 15 L 215 THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS SEQRES 16 L 215 GLU ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SEQRES 17 L 215 SER PHE ASN ARG ASN GLU CYS HET EDO H 301 4 HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 4 EDO C2 H6 O2 FORMUL 5 HOH *416(H2 O) HELIX 1 AA1 ALA A 289 GLU A 291 5 3 HELIX 2 AA2 THR A 305 SER A 309 5 5 HELIX 3 AA3 ARG A 428 ALA A 432 5 5 HELIX 4 AA4 ALA A 446 SER A 448 5 3 HELIX 5 AA5 SER A 461 ARG A 466 5 6 HELIX 6 AA6 ASN H 73 LYS H 75 5 3 HELIX 7 AA7 GLN H 86 THR H 90 5 5 HELIX 8 AA8 SER H 163 SER H 165 5 3 HELIX 9 AA9 PRO H 207 SER H 210 5 4 HELIX 10 AB1 GLN L 79 LEU L 83 5 5 HELIX 11 AB2 SER L 122 SER L 128 1 7 HELIX 12 AB3 LYS L 184 ARG L 189 1 6 SHEET 1 AA1 5 LYS A 151 PHE A 153 0 SHEET 2 AA1 5 ASP A 174 LEU A 180 1 O THR A 178 N PHE A 153 SHEET 3 AA1 5 ILE A 244 HIS A 250 -1 O LEU A 247 N PHE A 177 SHEET 4 AA1 5 TRP A 212 TRP A 216 -1 N ASP A 214 O THR A 248 SHEET 5 AA1 5 LEU A 225 TYR A 229 -1 O ILE A 226 N ILE A 215 SHEET 1 AA2 4 ASN A 157 GLU A 161 0 SHEET 2 AA2 4 PHE A 260 HIS A 268 -1 O ALA A 262 N ILE A 160 SHEET 3 AA2 4 MET A 185 PHE A 194 -1 N GLU A 186 O VAL A 267 SHEET 4 AA2 4 LEU A 238 SER A 240 -1 O SER A 240 N ILE A 187 SHEET 1 AA3 9 VAL A 279 PRO A 280 0 SHEET 2 AA3 9 ILE A 293 ALA A 295 0 SHEET 3 AA3 9 LEU A 329 GLN A 345 -1 O GLN A 330 N SER A 294 SHEET 4 AA3 9 ALA A 347 ILE A 348 0 SHEET 5 AA3 9 GLY A 355 SER A 366 -1 O TYR A 356 N ALA A 347 SHEET 6 AA3 9 MET A 373 VAL A 374 -1 O MET A 373 N VAL A 365 SHEET 7 AA3 9 PHE A 384 GLN A 385 -1 O PHE A 384 N TYR A 361 SHEET 8 AA3 9 VAL A 394 HIS A 415 -1 O PHE A 406 N SER A 366 SHEET 9 AA3 9 ARG A 421 CYS A 427 -1 O PHE A 425 N THR A 340 SHEET 1 AA4 8 ASN A 436 MET A 437 0 SHEET 2 AA4 8 ILE A 450 ALA A 452 0 SHEET 3 AA4 8 LEU A 488 GLN A 504 -1 O GLN A 489 N SER A 451 SHEET 4 AA4 8 VAL A 521 SER A 529 0 SHEET 5 AA4 8 GLU A 536 TYR A 537 -1 O GLU A 536 N TYR A 528 SHEET 6 AA4 8 PHE A 549 GLU A 550 -1 O PHE A 549 N PHE A 524 SHEET 7 AA4 8 ASP A 559 TRP A 578 -1 O GLU A 576 N LYS A 523 SHEET 8 AA4 8 ARG A 586 ASP A 593 -1 O LEU A 590 N GLY A 500 SHEET 1 AA5 2 GLN A 539 ASP A 540 0 SHEET 2 AA5 2 GLN A 545 PRO A 546 -1 O GLN A 545 N ASP A 540 SHEET 1 AA6 4 GLN H 3 SER H 7 0 SHEET 2 AA6 4 LEU H 18 SER H 25 -1 O THR H 23 N LYS H 5 SHEET 3 AA6 4 GLN H 77 MET H 82 -1 O PHE H 80 N ILE H 20 SHEET 4 AA6 4 LEU H 67 ASP H 72 -1 N SER H 70 O PHE H 79 SHEET 1 AA7 7 LEU H 11 VAL H 12 0 SHEET 2 AA7 7 VAL H 34 SER H 40 0 SHEET 3 AA7 7 GLY H 44 ILE H 51 -1 O LEU H 48 N TRP H 36 SHEET 4 AA7 7 THR H 57 TYR H 59 -1 O ASP H 58 N LEU H 50 SHEET 5 AA7 7 ALA H 91 ASN H 98 -1 O ALA H 96 N HIS H 35 SHEET 6 AA7 7 MET H 107 TRP H 110 -1 O TYR H 109 N ARG H 97 SHEET 7 AA7 7 THR H 114 VAL H 118 -1 O VAL H 116 N ALA H 91 SHEET 1 AA8 5 SER H 127 LEU H 131 0 SHEET 2 AA8 5 MET H 142 TYR H 152 -1 O GLY H 146 N LEU H 131 SHEET 3 AA8 5 VAL H 170 THR H 172 0 SHEET 4 AA8 5 VAL H 176 GLN H 178 0 SHEET 5 AA8 5 LEU H 181 PRO H 191 -1 O LEU H 181 N GLN H 178 SHEET 1 AA9 3 THR H 158 TRP H 161 0 SHEET 2 AA9 3 THR H 201 HIS H 206 -1 O ASN H 203 N THR H 160 SHEET 3 AA9 3 THR H 211 LYS H 216 -1 O VAL H 213 N VAL H 204 SHEET 1 AB1 4 MET L 4 THR L 5 0 SHEET 2 AB1 4 VAL L 19 ALA L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AB1 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AB1 4 PHE L 62 SER L 67 -1 N THR L 63 O THR L 74 SHEET 1 AB2 7 PHE L 10 THR L 14 0 SHEET 2 AB2 7 VAL L 33 GLN L 38 0 SHEET 3 AB2 7 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 4 AB2 7 ASN L 53 ARG L 54 -1 O ASN L 53 N TYR L 49 SHEET 5 AB2 7 ASP L 85 GLN L 90 -1 O ASP L 85 N GLN L 38 SHEET 6 AB2 7 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 90 SHEET 7 AB2 7 THR L 103 LYS L 108 -1 O THR L 103 N TYR L 86 SHEET 1 AB3 4 THR L 115 PHE L 119 0 SHEET 2 AB3 4 GLY L 130 PHE L 140 -1 O ASN L 138 N THR L 115 SHEET 3 AB3 4 TYR L 174 THR L 183 -1 O MET L 176 N LEU L 137 SHEET 4 AB3 4 VAL L 160 TRP L 164 -1 N SER L 163 O SER L 177 SHEET 1 AB4 4 SER L 154 ARG L 156 0 SHEET 2 AB4 4 ASN L 146 ILE L 151 -1 N ILE L 151 O SER L 154 SHEET 3 AB4 4 SER L 192 THR L 198 -1 O GLU L 196 N LYS L 148 SHEET 4 AB4 4 ILE L 206 ASN L 211 -1 O LYS L 208 N CYS L 195 SSBOND 1 CYS A 149 CYS A 175 1555 1555 2.04 SSBOND 2 CYS A 277 CYS A 427 1555 1555 2.03 SSBOND 3 CYS A 434 CYS A 592 1555 1555 2.04 SSBOND 4 CYS H 22 CYS H 95 1555 1555 2.39 SSBOND 5 CYS H 147 CYS H 202 1555 1555 2.12 SSBOND 6 CYS L 23 CYS L 88 1555 1555 2.27 SSBOND 7 CYS L 135 CYS L 195 1555 1555 2.14 CISPEP 1 PHE A 165 PRO A 166 0 4.16 CISPEP 2 PHE H 153 PRO H 154 0 -5.29 CISPEP 3 GLU H 155 PRO H 156 0 -2.60 CISPEP 4 TRP H 195 PRO H 196 0 8.64 CISPEP 5 TYR L 94 PRO L 95 0 -7.57 CISPEP 6 TYR L 141 PRO L 142 0 3.77 CRYST1 89.501 89.411 130.877 90.00 94.18 90.00 C 1 2 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 0.011173 0.000000 0.000817 0.00000 SCALE2 0.000000 0.011184 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007661 0.00000